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Found 12 matching records:

Displaying record number 3291

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MAb ID	CH235.9 (CH493, CH235.09)
HXB2 Location	Env	Env Epitope Map
Author Location	Env
Epitope
Subtype	C
Ab Type	gp120 CD4BS
Neutralizing	P (tier 2)  View neutralization details
Contacts and Features	View contacts and features
Species (Isotype)	human
Patient	Donor CH505
Immunogen	HIV-1 infection
Keywords	antibody binding site, antibody generation, antibody interactions, antibody lineage, antibody sequence, binding affinity, broad neutralizer, escape, mutation acquisition, neutralization, review, structure

Notes

Showing 4 of 4 notes.

• CH235.09: Analyses of all PDB HIV1-Env trimer (prefusion, closed) structures fulfilling certain parameters of resolution were performed to classify them on the basis of (a) antibody class which was informed by parental B cells as well as structural recognition, and (b) Env residues defining recognized HIV epitopes. Structural features of the 206 HIV epitope and bNAb paratopes were correlated with functional properties of the breadth and potency of neutralization against a 208-strain panel. bNAbs with >25% breadth of neutralization belonged to 20 classes of antibody with a large number of protruding loops and somatic hypermutation (SHM). HIV epitopes recognized placed the bNAbs into 6 categories (viz. V1V2, Glycan-V3, CD4-binding site, Silent face center, Fusion peptide and Subunit Interface). The epitopes contained high numbers of independent sequence segments and glycosylated surface area. CH235.9-Env formed a distinct group within the CD4bs category, Class 8ANC131. Crystal structure data for VH1-46 germline-derived bNAb CH235.9 complexed to HIV-1 Clade A/E 93TH057 gp120 was found in PDB ID: 5F9O. Chuang2019 (antibody binding site, antibody interactions, binding affinity, antibody sequence, structure, antibody lineage, broad neutralizer)
• CH235.9: This review discussed antibody-virus coevolution and lineage development as a path to elicit broadly neutralizing Abs. CD4bs mAbs from donor CH505 (lineages CH103 and CH235) were used as main examples. Bonsignori2017a (review, antibody lineage)
• This patent application states that CH493 is also referred to as CH235.9. Lam2017
• CH235.9: In 5 years additional members of the CH235 clonal lineage were isolated based on deep sequencing of donor CH505's V_L and V_H chains at 17 timepoints in the donor's infection. Two of these had greater neutralization potency, CH235.9 and CH235.12. Study of crystal structures indicated a site of vulnerability near the Env CD4 binding site. The lineages of CH103 and CH235, both derived from Donor CH505 were compared - CH103 lineage K_d increased an order of magnitude each step of maturation but maintained a fast association rate; CH235 lineage however, had slower K_ds and K_as over maturation. This mAb was autoreactive, at the cytoplasmic level. CH235.9 CDRL3 interacts with HIV-1 N280 in gp120, forming 3 H-bonds which are proposed to be disrupted due to autologous virus escape mutations in patient CH505, N280S and N280T. CH235.9 was produced as a recombinant mAb of V_H and V_L sequences found at week 152. CH235.9 neutralized 44% of a 75-autologous virus panel, 77% of a 202-multiclade Env-psuedovirus panel and 58% of an 113-patient CH505-derived autologous pseudoviral panel as part of CH235 lineages, all at potencies of <50 µg/ml. It also acquired the ability to neutralize all loop D mutants that were resistant to early members of the CH235 lineage. Bonsignori2016 (antibody generation, mutation acquisition, neutralization, escape, binding affinity, antibody sequence, antibody lineage)

References

Showing 4 of 4 references.

Isolation Paper
Bonsignori2016 Mattia Bonsignori, Tongqing Zhou, Zizhang Sheng, Lei Chen, Feng Gao, M. Gordon Joyce, Gabriel Ozorowski, Gwo-Yu Chuang, Chaim A. Schramm, Kevin Wiehe, S. Munir Alam, Todd Bradley, Morgan A. Gladden, Kwan-Ki Hwang, Sheelah Iyengar, Amit Kumar, Xiaozhi Lu, Kan Luo, Michael C. Mangiapani, Robert J. Parks, Hongshuo Song, Priyamvada Acharya, Robert T. Bailer, Allen Cao, Aliaksandr Druz, Ivelin S. Georgiev, Young D. Kwon, Mark K. Louder, Baoshan Zhang, Anqi Zheng, Brenna J. Hill, Rui Kong, Cinque Soto, NISC Comparative Sequencing Program, James C. Mullikin, Daniel C. Douek, David C. Montefiori, Michael A. Moody, George M. Shaw, Beatrice H. Hahn, Garnett Kelsoe, Peter T. Hraber, Bette T. Korber, Scott D. Boyd, Andrew Z. Fire, Thomas B. Kepler, Lawrence Shapiro, Andrew B. Ward, John R. Mascola, Hua-Xin Liao, Peter D. Kwong, and Barton F. Haynes. Maturation Pathway from Germline to Broad HIV-1 Neutralizer of a CD4-Mimic Antibody. Cell, 165(2):449-463, 7 Apr 2016. PubMed ID: 26949186. Show all entries for this paper.

Bonsignori2017a Mattia Bonsignori, Hua-Xin Liao, Feng Gao, Wilton B. Williams, S. Munir Alam, David C. Montefiori, and Barton F. Haynes. Antibody-Virus Co-evolution in HIV Infection: Paths for HIV Vaccine Development. Immunol. Rev., 275(1):145-160, Jan 2017. PubMed ID: 28133802. Show all entries for this paper.

Chuang2019 Gwo-Yu Chuang, Jing Zhou, Priyamvada Acharya, Reda Rawi, Chen-Hsiang Shen, Zizhang Sheng, Baoshan Zhang, Tongqing Zhou, Robert T. Bailer, Venkata P. Dandey, Nicole A. Doria-Rose, Mark K. Louder, Krisha McKee, John R. Mascola, Lawrence Shapiro, and Peter D. Kwong. Structural Survey of Broadly Neutralizing Antibodies Targeting the HIV-1 Env Trimer Delineates Epitope Categories and Characteristics of Recognition. Structure, 27(1):196-206.e6, 2 Jan 2019. PubMed ID: 30471922. Show all entries for this paper.

Lam2017 C. Y. K. Lam, J. L. Nordstrom, B. F. Haynes, and M. Bonsignori. Bispecific Molecules Comprising an HIV-1 Envelope Targeting Arm. WIPO patent application, Jan 2017. URL: https://patentscope.wipo.int/search/en/detail.jsf?docId=WO2017011414. Application number: PCT/US2016/041809. Show all entries for this paper.

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Displaying record number 3292

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MAb ID	CH235.12 (CH557)
HXB2 Location	Env	Env Epitope Map
Author Location	Env
Epitope
Subtype	C
Ab Type	gp120 CD4BS
Neutralizing	P (tier 2)  View neutralization details
Contacts and Features	View contacts and features
Species (Isotype)	human
Patient	Donor CH505
Immunogen	HIV-1 infection
Keywords	antibody binding site, antibody generation, antibody interactions, antibody lineage, antibody sequence, binding affinity, broad neutralizer, computational epitope prediction, neutralization, review, structure, vaccine antigen design

Notes

Showing 6 of 6 notes.

• CH235.12: Analyses of all PDB HIV1-Env trimer (prefusion, closed) structures fulfilling certain parameters of resolution were performed to classify them on the basis of (a) antibody class which was informed by parental B cells as well as structural recognition, and (b) Env residues defining recognized HIV epitopes. Structural features of the 206 HIV epitope and bNAb paratopes were correlated with functional properties of the breadth and potency of neutralization against a 208-strain panel. bNAbs with >25% breadth of neutralization belonged to 20 classes of antibody with a large number of protruding loops and somatic hypermutation (SHM). HIV epitopes recognized placed the bNAbs into 6 categories (viz. V1V2, Glycan-V3, CD4-binding site, Silent face center, Fusion peptide and Subunit Interface). The epitopes contained high numbers of independent sequence segments and glycosylated surface area. CH235.12-Env formed a distinct group within the CD4bs category, Class 8ANC131, and was chosen as a representative for neutralization studies as it had the highest breadth. Chuang2019 (antibody binding site, antibody interactions, neutralization, binding affinity, antibody sequence, structure, antibody lineage, broad neutralizer)
• CH235.12: This study demonstrated that bNAb signatures can be utilized to engineer HIV-1 Env vaccine immunogens eliciting Ab responses with greater neutralization breadth. Data from four large virus panels were used to comprehensively map viral signatures associated with bNAb sensitivity, hypervariable region characteristics, and clade effects. The bNAb signatures defined for the V2 epitope region were then employed to inform immunogen design in a proof-of-concept exploration of signature-based epitope targeted (SET) vaccines. V2 bNAb signature-guided mutations were introduced into Env 459C to create a trivalent vaccine which resulted in increased breadth of NAb responses compared with Env 459C alone. CH235.12 was used for analyzing clade sensitivity and had enhanced recognition of A clade viruses. Bricault2019 (antibody binding site, vaccine antigen design, computational epitope prediction, broad neutralizer)
• CH235.12: This review discussed antibody-virus coevolution and lineage development as a path to elicit broadly neutralizing Abs. CD4bs mAbs from donor CH505 (lineages CH103 and CH235) were used as main examples. Bonsignori2017a (review, antibody lineage)
• CH235.12: This review summarizes vaccine approaches to counter HIV diversity. A structural map illustrated the contact regions of several bNAbs: VRC26.09, PGT128, CH235.12, and 10E8. Structures illustrating the bNAbs' tolerance for sequence variation were illustrated for CH235.12, PGT128, VRC26.09, and 10E8. CD4BS bNAbs such as VRC01 and CH235.12 illustrate that bNAbs bind to both conserved and hypervariable regions of Env. These bNAbs aren't broad because their epitopes are highly conserved, but rather they arise due to selective pressures of the autologous viruses. Donor CH505 initially developed mAb lineage CH103; its maturation was facilitated by escape mutants, which were selected by early antibodies in the CH235 lineage, illustrating lineage cooperation. Korber2017 (antibody binding site, vaccine antigen design, review)
• This patent application states that CH557 is also referred to as CH235.12. Lam2017
• CH235.12: In 5 years additional members of the CH235 clonal lineage were isolated based on deep sequencing of donor CH505's V_L and V_H chains at 17 timepoints in the donor's infection. Two of these had greater neutralization potency, CH235.9 and CH235.12. Study of crystal structures indicated a site of vulnerability near the Env CD4 binding site. The lineages of CH103 and CH235, both derived from Donor CH505 were compared - CH103 lineage K_d increased an order of magnitude each step of maturation but maintained a fast association rate; CH235 lineage however, had slower K_ds and K_as over maturation. Unlike its precursors, CH235.12 though with high neutralization breadth, was not auto- or poly-reactive to DNA as other CH235 mAbs are. CH235.12 was isolated from cultured B cells as naturally paired V_H and V_L. CH235.9 neutralized 56% of a 75-autologous virus panel, 90% of a 202-multiclade Env-psuedovirus panel and 60% of a 113-patient CH505-derived autologous pseudoviral panel as part of CH235 lineages, all at potencies of <50 µg/ml. It also acquired the ability to neutralize all loop D mutants that were resistant to early members of the CH235 lineage. Bonsignori2016 (antibody generation, neutralization, binding affinity, antibody sequence, antibody lineage)

References

Showing 6 of 6 references.

Isolation Paper
Bonsignori2016 Mattia Bonsignori, Tongqing Zhou, Zizhang Sheng, Lei Chen, Feng Gao, M. Gordon Joyce, Gabriel Ozorowski, Gwo-Yu Chuang, Chaim A. Schramm, Kevin Wiehe, S. Munir Alam, Todd Bradley, Morgan A. Gladden, Kwan-Ki Hwang, Sheelah Iyengar, Amit Kumar, Xiaozhi Lu, Kan Luo, Michael C. Mangiapani, Robert J. Parks, Hongshuo Song, Priyamvada Acharya, Robert T. Bailer, Allen Cao, Aliaksandr Druz, Ivelin S. Georgiev, Young D. Kwon, Mark K. Louder, Baoshan Zhang, Anqi Zheng, Brenna J. Hill, Rui Kong, Cinque Soto, NISC Comparative Sequencing Program, James C. Mullikin, Daniel C. Douek, David C. Montefiori, Michael A. Moody, George M. Shaw, Beatrice H. Hahn, Garnett Kelsoe, Peter T. Hraber, Bette T. Korber, Scott D. Boyd, Andrew Z. Fire, Thomas B. Kepler, Lawrence Shapiro, Andrew B. Ward, John R. Mascola, Hua-Xin Liao, Peter D. Kwong, and Barton F. Haynes. Maturation Pathway from Germline to Broad HIV-1 Neutralizer of a CD4-Mimic Antibody. Cell, 165(2):449-463, 7 Apr 2016. PubMed ID: 26949186. Show all entries for this paper.

Bonsignori2017a Mattia Bonsignori, Hua-Xin Liao, Feng Gao, Wilton B. Williams, S. Munir Alam, David C. Montefiori, and Barton F. Haynes. Antibody-Virus Co-evolution in HIV Infection: Paths for HIV Vaccine Development. Immunol. Rev., 275(1):145-160, Jan 2017. PubMed ID: 28133802. Show all entries for this paper.

Bricault2019 Christine A. Bricault, Karina Yusim, Michael S. Seaman, Hyejin Yoon, James Theiler, Elena E. Giorgi, Kshitij Wagh, Maxwell Theiler, Peter Hraber, Jennifer P. Macke, Edward F. Kreider, Gerald H. Learn, Beatrice H. Hahn, Johannes F. Scheid, James M. Kovacs, Jennifer L. Shields, Christy L. Lavine, Fadi Ghantous, Michael Rist, Madeleine G. Bayne, George H. Neubauer, Katherine McMahan, Hanqin Peng, Coraline Chéneau, Jennifer J. Jones, Jie Zeng, Christina Ochsenbauer, Joseph P. Nkolola, Kathryn E. Stephenson, Bing Chen, S. Gnanakaran, Mattia Bonsignori, LaTonya D. Williams, Barton F. Haynes, Nicole Doria-Rose, John R. Mascola, David C. Montefiori, Dan H. Barouch, and Bette Korber. HIV-1 Neutralizing Antibody Signatures and Application to Epitope-Targeted Vaccine Design. Cell Host Microbe, 25(1):59-72.e8, 9 Jan 2019. PubMed ID: 30629920. Show all entries for this paper.

Chuang2019 Gwo-Yu Chuang, Jing Zhou, Priyamvada Acharya, Reda Rawi, Chen-Hsiang Shen, Zizhang Sheng, Baoshan Zhang, Tongqing Zhou, Robert T. Bailer, Venkata P. Dandey, Nicole A. Doria-Rose, Mark K. Louder, Krisha McKee, John R. Mascola, Lawrence Shapiro, and Peter D. Kwong. Structural Survey of Broadly Neutralizing Antibodies Targeting the HIV-1 Env Trimer Delineates Epitope Categories and Characteristics of Recognition. Structure, 27(1):196-206.e6, 2 Jan 2019. PubMed ID: 30471922. Show all entries for this paper.

Korber2017 Bette Korber, Peter Hraber, Kshitij Wagh, and Beatrice H. Hahn. Polyvalent Vaccine Approaches to Combat HIV-1 Diversity. Immunol. Rev., 275(1):230-244, Jan 2017. PubMed ID: 28133800. Show all entries for this paper.

Lam2017 C. Y. K. Lam, J. L. Nordstrom, B. F. Haynes, and M. Bonsignori. Bispecific Molecules Comprising an HIV-1 Envelope Targeting Arm. WIPO patent application, Jan 2017. URL: https://patentscope.wipo.int/search/en/detail.jsf?docId=WO2017011414. Application number: PCT/US2016/041809. Show all entries for this paper.

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Displaying record number 3381

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MAb ID	CH235.7 (CH491)
HXB2 Location	Env	Env Epitope Map
Author Location	Env
Epitope
Subtype	C
Ab Type	gp120 CD4BS
Neutralizing	P (tier 2)
Species (Isotype)	human
Patient	Donor CH505
Immunogen	HIV-1 infection
Keywords	antibody lineage, antibody sequence, binding affinity, neutralization, review

Notes

Showing 3 of 3 notes.

• CH235.7: This review discussed antibody-virus coevolution and lineage development as a path to elicit broadly neutralizing Abs. CD4bs mAbs from donor CH505 (lineages CH103 and CH235) were used as main examples. Bonsignori2017a (review, antibody lineage)
• This patent application states that CH491 is also referred to as CH235.7. Lam2017
• CH235.7: In 5 years additional members of the CH235 clonal lineage were isolated based on deep sequencing of donor CH505's V_L and V_H chains at 17 timepoints in the donor's infection. Two of these had greater neutralization potency, CH235.9 and CH235.12. Study of crystal structures indicated a site of vulnerability near the Env CD4 binding site. The lineages of CH103 and CH235, both derived from Donor CH505 were compared - CH103 lineage K_d increased an order of magnitude each step of maturation but maintained a fast association rate; CH235 lineage however, had slower K_ds and K_as over maturation. CH235.7, an intermediate of the CH235 lineage neutralized 35% of a 75-autologous virus panel, and 47% of a 113-patient CH505-derived autologous pseudoviral panel both at potencies of <50 µg/ml. Bonsignori2016 (neutralization, binding affinity, antibody sequence, antibody lineage)

References

Showing 3 of 3 references.

Isolation Paper
Bonsignori2016 Mattia Bonsignori, Tongqing Zhou, Zizhang Sheng, Lei Chen, Feng Gao, M. Gordon Joyce, Gabriel Ozorowski, Gwo-Yu Chuang, Chaim A. Schramm, Kevin Wiehe, S. Munir Alam, Todd Bradley, Morgan A. Gladden, Kwan-Ki Hwang, Sheelah Iyengar, Amit Kumar, Xiaozhi Lu, Kan Luo, Michael C. Mangiapani, Robert J. Parks, Hongshuo Song, Priyamvada Acharya, Robert T. Bailer, Allen Cao, Aliaksandr Druz, Ivelin S. Georgiev, Young D. Kwon, Mark K. Louder, Baoshan Zhang, Anqi Zheng, Brenna J. Hill, Rui Kong, Cinque Soto, NISC Comparative Sequencing Program, James C. Mullikin, Daniel C. Douek, David C. Montefiori, Michael A. Moody, George M. Shaw, Beatrice H. Hahn, Garnett Kelsoe, Peter T. Hraber, Bette T. Korber, Scott D. Boyd, Andrew Z. Fire, Thomas B. Kepler, Lawrence Shapiro, Andrew B. Ward, John R. Mascola, Hua-Xin Liao, Peter D. Kwong, and Barton F. Haynes. Maturation Pathway from Germline to Broad HIV-1 Neutralizer of a CD4-Mimic Antibody. Cell, 165(2):449-463, 7 Apr 2016. PubMed ID: 26949186. Show all entries for this paper.

Lam2017 C. Y. K. Lam, J. L. Nordstrom, B. F. Haynes, and M. Bonsignori. Bispecific Molecules Comprising an HIV-1 Envelope Targeting Arm. WIPO patent application, Jan 2017. URL: https://patentscope.wipo.int/search/en/detail.jsf?docId=WO2017011414. Application number: PCT/US2016/041809. Show all entries for this paper.

Bonsignori2017a Mattia Bonsignori, Hua-Xin Liao, Feng Gao, Wilton B. Williams, S. Munir Alam, David C. Montefiori, and Barton F. Haynes. Antibody-Virus Co-evolution in HIV Infection: Paths for HIV Vaccine Development. Immunol. Rev., 275(1):145-160, Jan 2017. PubMed ID: 28133802. Show all entries for this paper.

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Displaying record number 3382

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MAb ID	CH235.10 (CH555)
HXB2 Location	Env	Env Epitope Map
Author Location	Env
Epitope
Subtype	C
Ab Type	gp120 CD4BS
Neutralizing	P (tier 2)
Species (Isotype)	human
Patient	Donor CH505
Immunogen	HIV-1 infection
Keywords	antibody lineage, antibody sequence, binding affinity, neutralization, review

Notes

Showing 3 of 3 notes.

• CH235.10: This review discussed antibody-virus coevolution and lineage development as a path to elicit broadly neutralizing Abs. CD4bs mAbs from donor CH505 (lineages CH103 and CH235) were used as main examples. Bonsignori2017a (review, antibody lineage)
• This patent application states that CH555 is also referred to as CH235.10. Lam2017
• CH235.10: In 5 years additional members of the CH235 clonal lineage were isolated based on deep sequencing of donor CH505's V_L and V_H chains at 17 timepoints in the donor's infection. Two of these had greater neutralization potency, CH235.9 and CH235.12. Study of crystal structures indicated a site of vulnerability near the Env CD4 binding site. The lineages of CH103 and CH235, both derived from Donor CH505 were compared - CH103 lineage K_d increased an order of magnitude each step of maturation but maintained a fast association rate; CH235 lineage however, had slower K_ds and K_as over maturation. CH235.7, an intermediate of the CH235 lineage neutralized 39% of a 75-autologous virus panel, and 47% of a 113-patient CH505-derived autologous pseudoviral panel both at potencies of <50 µg/ml. Bonsignori2016 (neutralization, binding affinity, antibody sequence, antibody lineage)

References

Showing 3 of 3 references.

Isolation Paper
Bonsignori2016 Mattia Bonsignori, Tongqing Zhou, Zizhang Sheng, Lei Chen, Feng Gao, M. Gordon Joyce, Gabriel Ozorowski, Gwo-Yu Chuang, Chaim A. Schramm, Kevin Wiehe, S. Munir Alam, Todd Bradley, Morgan A. Gladden, Kwan-Ki Hwang, Sheelah Iyengar, Amit Kumar, Xiaozhi Lu, Kan Luo, Michael C. Mangiapani, Robert J. Parks, Hongshuo Song, Priyamvada Acharya, Robert T. Bailer, Allen Cao, Aliaksandr Druz, Ivelin S. Georgiev, Young D. Kwon, Mark K. Louder, Baoshan Zhang, Anqi Zheng, Brenna J. Hill, Rui Kong, Cinque Soto, NISC Comparative Sequencing Program, James C. Mullikin, Daniel C. Douek, David C. Montefiori, Michael A. Moody, George M. Shaw, Beatrice H. Hahn, Garnett Kelsoe, Peter T. Hraber, Bette T. Korber, Scott D. Boyd, Andrew Z. Fire, Thomas B. Kepler, Lawrence Shapiro, Andrew B. Ward, John R. Mascola, Hua-Xin Liao, Peter D. Kwong, and Barton F. Haynes. Maturation Pathway from Germline to Broad HIV-1 Neutralizer of a CD4-Mimic Antibody. Cell, 165(2):449-463, 7 Apr 2016. PubMed ID: 26949186. Show all entries for this paper.

Lam2017 C. Y. K. Lam, J. L. Nordstrom, B. F. Haynes, and M. Bonsignori. Bispecific Molecules Comprising an HIV-1 Envelope Targeting Arm. WIPO patent application, Jan 2017. URL: https://patentscope.wipo.int/search/en/detail.jsf?docId=WO2017011414. Application number: PCT/US2016/041809. Show all entries for this paper.

Bonsignori2017a Mattia Bonsignori, Hua-Xin Liao, Feng Gao, Wilton B. Williams, S. Munir Alam, David C. Montefiori, and Barton F. Haynes. Antibody-Virus Co-evolution in HIV Infection: Paths for HIV Vaccine Development. Immunol. Rev., 275(1):145-160, Jan 2017. PubMed ID: 28133802. Show all entries for this paper.

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Displaying record number 3383

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MAb ID	CH235.11 (CH556)
HXB2 Location	Env	Env Epitope Map
Author Location	Env
Epitope
Subtype	C
Ab Type	gp120 CD4BS
Neutralizing	P (tier 2)
Species (Isotype)	human
Patient	Donor CH505
Immunogen	HIV-1 infection
Keywords	antibody lineage, antibody sequence, binding affinity, neutralization, review

Notes

Showing 3 of 3 notes.

• CH235.11: This review discussed antibody-virus coevolution and lineage development as a path to elicit broadly neutralizing Abs. CD4bs mAbs from donor CH505 (lineages CH103 and CH235) were used as main examples. Bonsignori2017a (review, antibody lineage)
• This patent application states that CH556 is also referred to as CH235.11. Lam2017
• CH235.11: In 5 years additional members of the CH235 clonal lineage were isolated based on deep sequencing of donor CH505's V_L and V_H chains at 17 timepoints in the donor's infection. Two of these had greater neutralization potency, CH235.9 and CH235.12. Study of crystal structures indicated a site of vulnerability near the Env CD4 binding site. The lineages of CH103 and CH235, both derived from Donor CH505 were compared - CH103 lineage K_d increased an order of magnitude each step of maturation but maintained a fast association rate; CH235 lineage however, had slower K_ds and K_as over maturation. CH235.7, an intermediate of the CH235 lineage neutralized 20% of a 75-autologous virus panel, and 50% of a 113-patient CH505-derived autologous pseudoviral panel both at potencies of <50 µg/ml. Bonsignori2016 (neutralization, binding affinity, antibody sequence, antibody lineage)

References

Showing 3 of 3 references.

Isolation Paper
Bonsignori2016 Mattia Bonsignori, Tongqing Zhou, Zizhang Sheng, Lei Chen, Feng Gao, M. Gordon Joyce, Gabriel Ozorowski, Gwo-Yu Chuang, Chaim A. Schramm, Kevin Wiehe, S. Munir Alam, Todd Bradley, Morgan A. Gladden, Kwan-Ki Hwang, Sheelah Iyengar, Amit Kumar, Xiaozhi Lu, Kan Luo, Michael C. Mangiapani, Robert J. Parks, Hongshuo Song, Priyamvada Acharya, Robert T. Bailer, Allen Cao, Aliaksandr Druz, Ivelin S. Georgiev, Young D. Kwon, Mark K. Louder, Baoshan Zhang, Anqi Zheng, Brenna J. Hill, Rui Kong, Cinque Soto, NISC Comparative Sequencing Program, James C. Mullikin, Daniel C. Douek, David C. Montefiori, Michael A. Moody, George M. Shaw, Beatrice H. Hahn, Garnett Kelsoe, Peter T. Hraber, Bette T. Korber, Scott D. Boyd, Andrew Z. Fire, Thomas B. Kepler, Lawrence Shapiro, Andrew B. Ward, John R. Mascola, Hua-Xin Liao, Peter D. Kwong, and Barton F. Haynes. Maturation Pathway from Germline to Broad HIV-1 Neutralizer of a CD4-Mimic Antibody. Cell, 165(2):449-463, 7 Apr 2016. PubMed ID: 26949186. Show all entries for this paper.

Lam2017 C. Y. K. Lam, J. L. Nordstrom, B. F. Haynes, and M. Bonsignori. Bispecific Molecules Comprising an HIV-1 Envelope Targeting Arm. WIPO patent application, Jan 2017. URL: https://patentscope.wipo.int/search/en/detail.jsf?docId=WO2017011414. Application number: PCT/US2016/041809. Show all entries for this paper.

Bonsignori2017a Mattia Bonsignori, Hua-Xin Liao, Feng Gao, Wilton B. Williams, S. Munir Alam, David C. Montefiori, and Barton F. Haynes. Antibody-Virus Co-evolution in HIV Infection: Paths for HIV Vaccine Development. Immunol. Rev., 275(1):145-160, Jan 2017. PubMed ID: 28133802. Show all entries for this paper.

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Displaying record number 3643

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MAb ID	DH270.1 (DH270)
HXB2 Location	Env	Env Epitope Map
Author Location	gp120
Epitope
Subtype	C
Ab Type	gp120 V3 // V3 glycan (V3g)
Neutralizing	P (tier 2)  View neutralization details
Contacts and Features	View contacts and features
Species (Isotype)	human(IgG)
Patient	CH848
Immunogen	HIV-1 infection
Country	Malawi
Keywords	antibody binding site, antibody generation, antibody lineage, antibody sequence, autologous responses, binding affinity, broad neutralizer, computational epitope prediction, neutralization, review, structure, vaccine antigen design

Notes

Showing 6 of 6 notes.

• DH270.1: This study looks at the role of somatic mutations within antibody variable and framework regions (FWR) in bNAbs and how these mutations alter thermostability and neutralization as the Ab lineage reaches maturation. The emergence and selection of different mutations in the complementarity-determining and framework regions are necessary to maintain a balance between antibody function and stability. The study shows that all major classes of bnAbs (DH2070, CH103, CH235 etc.) have lower thermostability than their corresponding inferred UCA antibodies. DH270 had the greatest reduction. Mutations in the DH270 UCA show that the mutants have lower thermostability and stronger neutralization. Henderson2019 (neutralization, antibody lineage, broad neutralizer)
• DH270.1: This study demonstrated that bNAb signatures can be utilized to engineer HIV-1 Env vaccine immunogens eliciting Ab responses with greater neutralization breadth. Data from four large virus panels were used to comprehensively map viral signatures associated with bNAb sensitivity, hypervariable region characteristics, and clade effects. The bNAb signatures defined for the V2 epitope region were then employed to inform immunogen design in a proof-of-concept exploration of signature-based epitope targeted (SET) vaccines. V2 bNAb signature-guided mutations were introduced into Env 459C to create a trivalent vaccine which resulted in increased breadth of NAb responses compared with Env 459C alone. DH270.1 was used for analyzing clade sensitivity. Bricault2019 (antibody binding site, vaccine antigen design, computational epitope prediction, broad neutralizer)
• DH270: Man₉-V3, a synthetic minimal immunogen designed to reflect the HIV-1 native Env V3-glycan bNAb epitope, binds memory B cells and V3-glycan bNAbs as well as germline bNAbs. Man₉-V3 was used to isolate a bNAb from an HIV-1+ subject and also induce V3-glycan-targeting antibodies in rhesus macaques. Using the crystal structure of PGT128-gp120 Env OD (outer domain), Man₉-V3 glycopeptide was synthesized based on Clade B JRFL with deletion of residues 305-320, retention of P321 and stabilization of disulfide bridge C296-C331. Man₉-V3 is bound by DH270 lineage bNAb. Alam2017 (antibody binding site)
• DH270: This review summarizes vaccine approaches to counter HIV diversity. The lineages DH270, DH272 and DH475 from donor CH848 were used to illustrate lineage-based vaccine design. The two earlier lineages (DH272 and DH475) neutralized the founder virus, which had an atypically long V1 loop. Shorter V1 loops were selected, allowing the development of the more broadly neutralizing lineage DH270. Korber2017 (vaccine antigen design, review, antibody lineage)
• This patent application states that DH270 is also referred to as DH270.1. Lam2017
• DH270.1: The study isolated 3 new V3-glycan antibody lineages (DH270, DH272, DH475) from donor CH848, who was followed for 5 years starting from the time of transmission. The DH272 and DH475 lineages had neutralization patterns that likely selected for observed viral escape variants, which, in turn, stimulated the DH270 lineage to potent neutralization breadth. DH270 antibodies were recovered from memory B cells at all three sampling times (weeks 205, 232, and 234 post-infection). Clonal expansion occurred at week 186, concurrent with the development of plasma neutralization breadth. Like some previously-characterized Abs (PGT124, PGT128, PGT135), the DH270 lineage mAbs bound to Env N332, and their neutralization was reduced or abrogated by mutation of this residue. Bonsignori2017 (antibody binding site, antibody generation, autologous responses, neutralization, binding affinity, antibody sequence, structure, antibody lineage, broad neutralizer)

References

Showing 6 of 6 references.

Isolation Paper
Bonsignori2017 Mattia Bonsignori, Edward F. Kreider, Daniela Fera, R. Ryan Meyerhoff, Todd Bradley, Kevin Wiehe, S. Munir Alam, Baptiste Aussedat, William E. Walkowicz, Kwan-Ki Hwang, Kevin O. Saunders, Ruijun Zhang, Morgan A. Gladden, Anthony Monroe, Amit Kumar, Shi-Mao Xia, Melissa Cooper, Mark K. Louder, Krisha McKee, Robert T. Bailer, Brendan W. Pier, Claudia A. Jette, Garnett Kelsoe, Wilton B. Williams, Lynn Morris, John Kappes, Kshitij Wagh, Gift Kamanga, Myron S. Cohen, Peter T. Hraber, David C. Montefiori, Ashley Trama, Hua-Xin Liao, Thomas B. Kepler, M. Anthony Moody, Feng Gao, Samuel J. Danishefsky, John R. Mascola, George M. Shaw, Beatrice H. Hahn, Stephen C. Harrison, Bette T. Korber, and Barton F. Haynes. Staged Induction of HIV-1 Glycan-Dependent Broadly Neutralizing Antibodies. Sci. Transl. Med., 9(381), 15 Mar 2017. PubMed ID: 28298420. Show all entries for this paper.

Alam2017 S. Munir Alam, Baptiste Aussedat, Yusuf Vohra, R. Ryan Meyerhoff, Evan M. Cale, William E. Walkowicz, Nathan A. Radakovich, Kara Anasti, Lawrence Armand, Robert Parks, Laura Sutherland, Richard Scearce, M. Gordon Joyce, Marie Pancera, Aliaksandr Druz, Ivelin S. Georgiev, Tarra Von Holle, Amanda Eaton, Christopher Fox, Steven G. Reed, Mark Louder, Robert T. Bailer, Lynn Morris, Salim S. Abdool-Karim, Myron Cohen, Hua-Xin Liao, David C. Montefiori, Peter K. Park, Alberto Fernández-Tejada, Kevin Wiehe, Sampa Santra, Thomas B. Kepler, Kevin O. Saunders, Joseph Sodroski, Peter D. Kwong, John R. Mascola, Mattia Bonsignori, M. Anthony Moody, Samuel Danishefsky, and Barton F. Haynes. Mimicry of an HIV Broadly Neutralizing Antibody Epitope with a Synthetic Glycopeptide. Sci. Transl. Med., 9(381), 15 Mar 2017. PubMed ID: 28298421. Show all entries for this paper.

Bricault2019 Christine A. Bricault, Karina Yusim, Michael S. Seaman, Hyejin Yoon, James Theiler, Elena E. Giorgi, Kshitij Wagh, Maxwell Theiler, Peter Hraber, Jennifer P. Macke, Edward F. Kreider, Gerald H. Learn, Beatrice H. Hahn, Johannes F. Scheid, James M. Kovacs, Jennifer L. Shields, Christy L. Lavine, Fadi Ghantous, Michael Rist, Madeleine G. Bayne, George H. Neubauer, Katherine McMahan, Hanqin Peng, Coraline Chéneau, Jennifer J. Jones, Jie Zeng, Christina Ochsenbauer, Joseph P. Nkolola, Kathryn E. Stephenson, Bing Chen, S. Gnanakaran, Mattia Bonsignori, LaTonya D. Williams, Barton F. Haynes, Nicole Doria-Rose, John R. Mascola, David C. Montefiori, Dan H. Barouch, and Bette Korber. HIV-1 Neutralizing Antibody Signatures and Application to Epitope-Targeted Vaccine Design. Cell Host Microbe, 25(1):59-72.e8, 9 Jan 2019. PubMed ID: 30629920. Show all entries for this paper.

Henderson2019 Rory Henderson, Brian E. Watts, Hieu N. Ergin, Kara Anasti, Robert Parks, Shi-Mao Xia, Ashley Trama, Hua-Xin Liao, Kevin O. Saunders, Mattia Bonsignori, Kevin Wiehe, Barton F. Haynes, and S. Munir Alam. Selection of Immunoglobulin Elbow Region Mutations Impacts Interdomain Conformational Flexibility in HIV-1 Broadly Neutralizing Antibodies. Nat. Commun., 10(1):654, 8 Feb 2019. PubMed ID: 30737386. Show all entries for this paper.

Korber2017 Bette Korber, Peter Hraber, Kshitij Wagh, and Beatrice H. Hahn. Polyvalent Vaccine Approaches to Combat HIV-1 Diversity. Immunol. Rev., 275(1):230-244, Jan 2017. PubMed ID: 28133800. Show all entries for this paper.

Lam2017 C. Y. K. Lam, J. L. Nordstrom, B. F. Haynes, and M. Bonsignori. Bispecific Molecules Comprising an HIV-1 Envelope Targeting Arm. WIPO patent application, Jan 2017. URL: https://patentscope.wipo.int/search/en/detail.jsf?docId=WO2017011414. Application number: PCT/US2016/041809. Show all entries for this paper.

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Displaying record number 3649

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MAb ID	DH270.2 (DH473)
HXB2 Location	Env	Env Epitope Map
Author Location	gp120
Epitope
Subtype	C
Ab Type	gp120 V3 // V3 glycan (V3g)
Neutralizing	P (tier 2)  View neutralization details
Species (Isotype)	human(IgG)
Patient	CH848
Immunogen	HIV-1 infection
Country	Malawi
Keywords	antibody binding site, antibody generation, antibody lineage, antibody sequence, autologous responses, binding affinity, broad neutralizer, neutralization, structure

Notes

Showing 2 of 2 notes.

• This patent application states that DH473 is also referred to as DH270.2. Lam2017
• DH270.2: The study isolated 3 new V3-glycan antibody lineages (DH270, DH272, DH475) from donor CH848, who was followed for 5 years starting from the time of transmission. The DH272 and DH475 lineages had neutralization patterns that likely selected for observed viral escape variants, which, in turn, stimulated the DH270 lineage to potent neutralization breadth. DH270 antibodies were recovered from memory B cells at all three sampling times (weeks 205, 232, and 234 post-infection). Clonal expansion occurred at week 186, concurrent with the development of plasma neutralization breadth. Like some previously-characterized Abs (PGT124, PGT128, PGT135), the DH270 lineage mAbs bound to Env N332, and their neutralization was reduced or abrogated by mutation of this residue. Bonsignori2017 (antibody binding site, antibody generation, autologous responses, neutralization, binding affinity, antibody sequence, structure, antibody lineage, broad neutralizer)

References

Showing 2 of 2 references.

Isolation Paper
Bonsignori2017 Mattia Bonsignori, Edward F. Kreider, Daniela Fera, R. Ryan Meyerhoff, Todd Bradley, Kevin Wiehe, S. Munir Alam, Baptiste Aussedat, William E. Walkowicz, Kwan-Ki Hwang, Kevin O. Saunders, Ruijun Zhang, Morgan A. Gladden, Anthony Monroe, Amit Kumar, Shi-Mao Xia, Melissa Cooper, Mark K. Louder, Krisha McKee, Robert T. Bailer, Brendan W. Pier, Claudia A. Jette, Garnett Kelsoe, Wilton B. Williams, Lynn Morris, John Kappes, Kshitij Wagh, Gift Kamanga, Myron S. Cohen, Peter T. Hraber, David C. Montefiori, Ashley Trama, Hua-Xin Liao, Thomas B. Kepler, M. Anthony Moody, Feng Gao, Samuel J. Danishefsky, John R. Mascola, George M. Shaw, Beatrice H. Hahn, Stephen C. Harrison, Bette T. Korber, and Barton F. Haynes. Staged Induction of HIV-1 Glycan-Dependent Broadly Neutralizing Antibodies. Sci. Transl. Med., 9(381), 15 Mar 2017. PubMed ID: 28298420. Show all entries for this paper.

Lam2017 C. Y. K. Lam, J. L. Nordstrom, B. F. Haynes, and M. Bonsignori. Bispecific Molecules Comprising an HIV-1 Envelope Targeting Arm. WIPO patent application, Jan 2017. URL: https://patentscope.wipo.int/search/en/detail.jsf?docId=WO2017011414. Application number: PCT/US2016/041809. Show all entries for this paper.

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Displaying record number 3650

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MAb ID	DH270.3 (DH391)
HXB2 Location	Env	Env Epitope Map
Author Location	gp120
Epitope
Subtype	C
Ab Type	gp120 V3 // V3 glycan (V3g)
Neutralizing	P (tier 2)  View neutralization details
Species (Isotype)	human(IgG)
Patient	CH848
Immunogen	HIV-1 infection
Country	Malawi
Keywords	antibody binding site, antibody generation, antibody lineage, antibody sequence, autologous responses, binding affinity, broad neutralizer, neutralization, structure

Notes

Showing 2 of 2 notes.

• This patent application states that DH391 is also referred to as DH270.3. Lam2017
• DH270.3: The study isolated 3 new V3-glycan antibody lineages (DH270, DH272, DH475) from donor CH848, who was followed for 5 years starting from the time of transmission. The DH272 and DH475 lineages had neutralization patterns that likely selected for observed viral escape variants, which, in turn, stimulated the DH270 lineage to potent neutralization breadth. DH270 antibodies were recovered from memory B cells at all three sampling times (weeks 205, 232, and 234 post-infection). Clonal expansion occurred at week 186, concurrent with the development of plasma neutralization breadth. Like some previously-characterized Abs (PGT124, PGT128, PGT135), the DH270 lineage mAbs bound to Env N332, and their neutralization was reduced or abrogated by mutation of this residue. Bonsignori2017 (antibody binding site, antibody generation, autologous responses, neutralization, binding affinity, antibody sequence, structure, antibody lineage, broad neutralizer)

References

Showing 2 of 2 references.

Isolation Paper
Bonsignori2017 Mattia Bonsignori, Edward F. Kreider, Daniela Fera, R. Ryan Meyerhoff, Todd Bradley, Kevin Wiehe, S. Munir Alam, Baptiste Aussedat, William E. Walkowicz, Kwan-Ki Hwang, Kevin O. Saunders, Ruijun Zhang, Morgan A. Gladden, Anthony Monroe, Amit Kumar, Shi-Mao Xia, Melissa Cooper, Mark K. Louder, Krisha McKee, Robert T. Bailer, Brendan W. Pier, Claudia A. Jette, Garnett Kelsoe, Wilton B. Williams, Lynn Morris, John Kappes, Kshitij Wagh, Gift Kamanga, Myron S. Cohen, Peter T. Hraber, David C. Montefiori, Ashley Trama, Hua-Xin Liao, Thomas B. Kepler, M. Anthony Moody, Feng Gao, Samuel J. Danishefsky, John R. Mascola, George M. Shaw, Beatrice H. Hahn, Stephen C. Harrison, Bette T. Korber, and Barton F. Haynes. Staged Induction of HIV-1 Glycan-Dependent Broadly Neutralizing Antibodies. Sci. Transl. Med., 9(381), 15 Mar 2017. PubMed ID: 28298420. Show all entries for this paper.

Lam2017 C. Y. K. Lam, J. L. Nordstrom, B. F. Haynes, and M. Bonsignori. Bispecific Molecules Comprising an HIV-1 Envelope Targeting Arm. WIPO patent application, Jan 2017. URL: https://patentscope.wipo.int/search/en/detail.jsf?docId=WO2017011414. Application number: PCT/US2016/041809. Show all entries for this paper.

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Displaying record number 3651

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MAb ID	DH270.4 (DH429)
HXB2 Location	Env	Env Epitope Map
Author Location	gp120
Epitope
Subtype	C
Ab Type	gp120 V3 // V3 glycan (V3g)
Neutralizing	P (tier 2)  View neutralization details
Species (Isotype)	human(IgG)
Patient	CH848
Immunogen	HIV-1 infection
Country	Malawi
Keywords	antibody binding site, antibody generation, antibody lineage, antibody sequence, autologous responses, binding affinity, broad neutralizer, neutralization, structure

Notes

Showing 2 of 2 notes.

• This patent application states that DH429 is also referred to as DH270.4. Lam2017
• DH270.4: The study isolated 3 new V3-glycan antibody lineages (DH270, DH272, DH475) from donor CH848, who was followed for 5 years starting from the time of transmission. The DH272 and DH475 lineages had neutralization patterns that likely selected for observed viral escape variants, which, in turn, stimulated the DH270 lineage to potent neutralization breadth. DH270 antibodies were recovered from memory B cells at all three sampling times (weeks 205, 232, and 234 post-infection). Clonal expansion occurred at week 186, concurrent with the development of plasma neutralization breadth. Like some previously-characterized Abs (PGT124, PGT128, PGT135), the DH270 lineage mAbs bound to Env N332, and their neutralization was reduced or abrogated by mutation of this residue. Bonsignori2017 (antibody binding site, antibody generation, autologous responses, neutralization, binding affinity, antibody sequence, structure, antibody lineage, broad neutralizer)

References

Showing 2 of 2 references.

Isolation Paper
Bonsignori2017 Mattia Bonsignori, Edward F. Kreider, Daniela Fera, R. Ryan Meyerhoff, Todd Bradley, Kevin Wiehe, S. Munir Alam, Baptiste Aussedat, William E. Walkowicz, Kwan-Ki Hwang, Kevin O. Saunders, Ruijun Zhang, Morgan A. Gladden, Anthony Monroe, Amit Kumar, Shi-Mao Xia, Melissa Cooper, Mark K. Louder, Krisha McKee, Robert T. Bailer, Brendan W. Pier, Claudia A. Jette, Garnett Kelsoe, Wilton B. Williams, Lynn Morris, John Kappes, Kshitij Wagh, Gift Kamanga, Myron S. Cohen, Peter T. Hraber, David C. Montefiori, Ashley Trama, Hua-Xin Liao, Thomas B. Kepler, M. Anthony Moody, Feng Gao, Samuel J. Danishefsky, John R. Mascola, George M. Shaw, Beatrice H. Hahn, Stephen C. Harrison, Bette T. Korber, and Barton F. Haynes. Staged Induction of HIV-1 Glycan-Dependent Broadly Neutralizing Antibodies. Sci. Transl. Med., 9(381), 15 Mar 2017. PubMed ID: 28298420. Show all entries for this paper.

Lam2017 C. Y. K. Lam, J. L. Nordstrom, B. F. Haynes, and M. Bonsignori. Bispecific Molecules Comprising an HIV-1 Envelope Targeting Arm. WIPO patent application, Jan 2017. URL: https://patentscope.wipo.int/search/en/detail.jsf?docId=WO2017011414. Application number: PCT/US2016/041809. Show all entries for this paper.

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Displaying record number 3652

Download this epitope record as JSON.

MAb ID	DH270.5 (DH471)
HXB2 Location	Env	Env Epitope Map
Author Location	gp120
Epitope
Subtype	C
Ab Type	gp120 V3 // V3 glycan (V3g)
Neutralizing	P (tier 2)  View neutralization details
Contacts and Features	View contacts and features
Species (Isotype)	human(IgG)
Patient	CH848
Immunogen	HIV-1 infection
Country	Malawi
Keywords	antibody binding site, antibody generation, antibody lineage, antibody sequence, autologous responses, binding affinity, broad neutralizer, computational epitope prediction, neutralization, structure, vaccine antigen design

Notes

Showing 3 of 3 notes.

• DH270.5: This study demonstrated that bNAb signatures can be utilized to engineer HIV-1 Env vaccine immunogens eliciting Ab responses with greater neutralization breadth. Data from four large virus panels were used to comprehensively map viral signatures associated with bNAb sensitivity, hypervariable region characteristics, and clade effects. The bNAb signatures defined for the V2 epitope region were then employed to inform immunogen design in a proof-of-concept exploration of signature-based epitope targeted (SET) vaccines. V2 bNAb signature-guided mutations were introduced into Env 459C to create a trivalent vaccine which resulted in increased breadth of NAb responses compared with Env 459C alone. DH270.5 was used for analyzing clade sensitivity. Bricault2019 (antibody binding site, vaccine antigen design, computational epitope prediction, broad neutralizer)
• This patent application states that DH471 is also referred to as DH270.5. Lam2017
• DH270.5: The study isolated 3 new V3-glycan antibody lineages (DH270, DH272, DH475) from donor CH848, who was followed for 5 years starting from the time of transmission. The DH272 and DH475 lineages had neutralization patterns that likely selected for observed viral escape variants, which, in turn, stimulated the DH270 lineage to potent neutralization breadth. DH270 antibodies were recovered from memory B cells at all three sampling times (weeks 205, 232, and 234 post-infection). Clonal expansion occurred at week 186, concurrent with the development of plasma neutralization breadth. Like some previously-characterized Abs (PGT124, PGT128, PGT135), the DH270 lineage mAbs bound to Env N332, and their neutralization was reduced or abrogated by mutation of this residue. Bonsignori2017 (antibody binding site, antibody generation, autologous responses, neutralization, binding affinity, antibody sequence, structure, antibody lineage, broad neutralizer)

References

Showing 3 of 3 references.

Isolation Paper
Bonsignori2017 Mattia Bonsignori, Edward F. Kreider, Daniela Fera, R. Ryan Meyerhoff, Todd Bradley, Kevin Wiehe, S. Munir Alam, Baptiste Aussedat, William E. Walkowicz, Kwan-Ki Hwang, Kevin O. Saunders, Ruijun Zhang, Morgan A. Gladden, Anthony Monroe, Amit Kumar, Shi-Mao Xia, Melissa Cooper, Mark K. Louder, Krisha McKee, Robert T. Bailer, Brendan W. Pier, Claudia A. Jette, Garnett Kelsoe, Wilton B. Williams, Lynn Morris, John Kappes, Kshitij Wagh, Gift Kamanga, Myron S. Cohen, Peter T. Hraber, David C. Montefiori, Ashley Trama, Hua-Xin Liao, Thomas B. Kepler, M. Anthony Moody, Feng Gao, Samuel J. Danishefsky, John R. Mascola, George M. Shaw, Beatrice H. Hahn, Stephen C. Harrison, Bette T. Korber, and Barton F. Haynes. Staged Induction of HIV-1 Glycan-Dependent Broadly Neutralizing Antibodies. Sci. Transl. Med., 9(381), 15 Mar 2017. PubMed ID: 28298420. Show all entries for this paper.

Lam2017 C. Y. K. Lam, J. L. Nordstrom, B. F. Haynes, and M. Bonsignori. Bispecific Molecules Comprising an HIV-1 Envelope Targeting Arm. WIPO patent application, Jan 2017. URL: https://patentscope.wipo.int/search/en/detail.jsf?docId=WO2017011414. Application number: PCT/US2016/041809. Show all entries for this paper.

Bricault2019 Christine A. Bricault, Karina Yusim, Michael S. Seaman, Hyejin Yoon, James Theiler, Elena E. Giorgi, Kshitij Wagh, Maxwell Theiler, Peter Hraber, Jennifer P. Macke, Edward F. Kreider, Gerald H. Learn, Beatrice H. Hahn, Johannes F. Scheid, James M. Kovacs, Jennifer L. Shields, Christy L. Lavine, Fadi Ghantous, Michael Rist, Madeleine G. Bayne, George H. Neubauer, Katherine McMahan, Hanqin Peng, Coraline Chéneau, Jennifer J. Jones, Jie Zeng, Christina Ochsenbauer, Joseph P. Nkolola, Kathryn E. Stephenson, Bing Chen, S. Gnanakaran, Mattia Bonsignori, LaTonya D. Williams, Barton F. Haynes, Nicole Doria-Rose, John R. Mascola, David C. Montefiori, Dan H. Barouch, and Bette Korber. HIV-1 Neutralizing Antibody Signatures and Application to Epitope-Targeted Vaccine Design. Cell Host Microbe, 25(1):59-72.e8, 9 Jan 2019. PubMed ID: 30629920. Show all entries for this paper.

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Displaying record number 3669

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MAb ID	CH235.8 (CH492)
HXB2 Location	Env	Env Epitope Map
Author Location	Env
Epitope
Subtype	C
Ab Type	gp120 CD4BS
Neutralizing	P (tier 2)
Species (Isotype)	human
Patient
Immunogen	HIV-1 infection
Keywords	antibody generation, antibody lineage

Notes

Showing 2 of 2 notes.

• This patent application states that CH492 is also referred to as CH235.8. Lam2017
• CH235.8: In 5 years additional members of the CH235 clonal lineage were isolated based on deep sequencing of donor CH505's V_L and V_H chains at 17 timepoints in the donor's infection. Two of these had greater neutralization potency, CH235.9 and CH235.12. Study of crystal structures indicated a site of vulnerability near the Env CD4 binding site. The lineages of CH103 and CH235, both derived from Donor CH505 were compared - CH103 lineage K_d increased an order of magnitude each step of maturation but maintained a fast association rate; CH235 lineage however, had slower K_ds and K_as over maturation. This mAb was autoreactive, at the cytoplasmic level. Bonsignori2016 (antibody generation, antibody lineage)

References

Showing 2 of 2 references.

Isolation Paper
Bonsignori2016 Mattia Bonsignori, Tongqing Zhou, Zizhang Sheng, Lei Chen, Feng Gao, M. Gordon Joyce, Gabriel Ozorowski, Gwo-Yu Chuang, Chaim A. Schramm, Kevin Wiehe, S. Munir Alam, Todd Bradley, Morgan A. Gladden, Kwan-Ki Hwang, Sheelah Iyengar, Amit Kumar, Xiaozhi Lu, Kan Luo, Michael C. Mangiapani, Robert J. Parks, Hongshuo Song, Priyamvada Acharya, Robert T. Bailer, Allen Cao, Aliaksandr Druz, Ivelin S. Georgiev, Young D. Kwon, Mark K. Louder, Baoshan Zhang, Anqi Zheng, Brenna J. Hill, Rui Kong, Cinque Soto, NISC Comparative Sequencing Program, James C. Mullikin, Daniel C. Douek, David C. Montefiori, Michael A. Moody, George M. Shaw, Beatrice H. Hahn, Garnett Kelsoe, Peter T. Hraber, Bette T. Korber, Scott D. Boyd, Andrew Z. Fire, Thomas B. Kepler, Lawrence Shapiro, Andrew B. Ward, John R. Mascola, Hua-Xin Liao, Peter D. Kwong, and Barton F. Haynes. Maturation Pathway from Germline to Broad HIV-1 Neutralizer of a CD4-Mimic Antibody. Cell, 165(2):449-463, 7 Apr 2016. PubMed ID: 26949186. Show all entries for this paper.

Lam2017 C. Y. K. Lam, J. L. Nordstrom, B. F. Haynes, and M. Bonsignori. Bispecific Molecules Comprising an HIV-1 Envelope Targeting Arm. WIPO patent application, Jan 2017. URL: https://patentscope.wipo.int/search/en/detail.jsf?docId=WO2017011414. Application number: PCT/US2016/041809. Show all entries for this paper.

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Displaying record number 3670

Download this epitope record as JSON.

MAb ID	CH235.6 (CH490)
HXB2 Location	Env	Env Epitope Map
Author Location	Env
Epitope
Subtype	C
Ab Type	gp120 CD4BS
Neutralizing	P (tier 2)
Species (Isotype)	human
Patient
Immunogen	HIV-1 infection
Keywords	antibody generation, antibody lineage

Notes

Showing 2 of 2 notes.

• This patent application states that CH490 is also referred to as CH235.6. Lam2017
• CH235.6: In 5 years additional members of the CH235 clonal lineage were isolated based on deep sequencing of donor CH505's V_L and V_H chains at 17 timepoints in the donor's infection. Two of these had greater neutralization potency, CH235.9 and CH235.12. Study of crystal structures indicated a site of vulnerability near the Env CD4 binding site. The lineages of CH103 and CH235, both derived from Donor CH505 were compared - CH103 lineage K_d increased an order of magnitude each step of maturation but maintained a fast association rate; CH235 lineage however, had slower K_ds and K_as over maturation. This mAb was autoreactive, at the cytoplasmic level. Bonsignori2016 (antibody generation, antibody lineage)

References

Showing 2 of 2 references.

Isolation Paper
Bonsignori2016 Mattia Bonsignori, Tongqing Zhou, Zizhang Sheng, Lei Chen, Feng Gao, M. Gordon Joyce, Gabriel Ozorowski, Gwo-Yu Chuang, Chaim A. Schramm, Kevin Wiehe, S. Munir Alam, Todd Bradley, Morgan A. Gladden, Kwan-Ki Hwang, Sheelah Iyengar, Amit Kumar, Xiaozhi Lu, Kan Luo, Michael C. Mangiapani, Robert J. Parks, Hongshuo Song, Priyamvada Acharya, Robert T. Bailer, Allen Cao, Aliaksandr Druz, Ivelin S. Georgiev, Young D. Kwon, Mark K. Louder, Baoshan Zhang, Anqi Zheng, Brenna J. Hill, Rui Kong, Cinque Soto, NISC Comparative Sequencing Program, James C. Mullikin, Daniel C. Douek, David C. Montefiori, Michael A. Moody, George M. Shaw, Beatrice H. Hahn, Garnett Kelsoe, Peter T. Hraber, Bette T. Korber, Scott D. Boyd, Andrew Z. Fire, Thomas B. Kepler, Lawrence Shapiro, Andrew B. Ward, John R. Mascola, Hua-Xin Liao, Peter D. Kwong, and Barton F. Haynes. Maturation Pathway from Germline to Broad HIV-1 Neutralizer of a CD4-Mimic Antibody. Cell, 165(2):449-463, 7 Apr 2016. PubMed ID: 26949186. Show all entries for this paper.

Lam2017 C. Y. K. Lam, J. L. Nordstrom, B. F. Haynes, and M. Bonsignori. Bispecific Molecules Comprising an HIV-1 Envelope Targeting Arm. WIPO patent application, Jan 2017. URL: https://patentscope.wipo.int/search/en/detail.jsf?docId=WO2017011414. Application number: PCT/US2016/041809. Show all entries for this paper.

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