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Found 17 matching records:

Displaying record number 2663

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MAb ID	m66
HXB2 Location	gp160(663-666) DNA(8211..8222)	gp160 Epitope Map
Author Location
Epitope	`LDKW`	Epitope Alignment
Ab Type	gp41 MPER (membrane proximal external region)
Neutralizing	P View neutralization details
Species (Isotype)	human(IgG1)
Patient	SC44
Immunogen	HIV-1 infection
Country	Netherlands
Keywords	antibody binding site, antibody generation, antibody lineage, antibody sequence, neutralization, structure

Notes

Showing 2 of 2 notes.

m66: Crystal structure of m66 bound to its gp41 epitope and unbound structures of m66 and m66.6 are reported. Structure confirmed Env L660 and LDKW (663-666) as contact residues. Both m66 and 66.6 shared identical heavy chains,based on VH precursor IGHV5-51*01, but differ by 7.8% in their IGKVI-39*01 based light chains. For the Ab, heavy-chain residues W33, T100g, D54, D56 mediated hydrogen bonds and salt bridges, and hydrophobic contacts were mediated by heavy-chain residues W33, Y52, H97, Y100i, Y100k. Light-chain residues Y32, T94, F96 formed direct contacts with gp41, with Y32 and F96 that contact Env L660 and L663. Ofek2014 (structure)
m66: 2 human MAbs m66 and m66.6 were identified from 2F5-like serum of HIV-1-infected patient. These new MAbs mimic 2F5 in terms of their MPER binding profiles and neutralize a subset of the viruses neutralized by 2F5, while being significantly less divergent than 2F5 from their germ line-encoded counterparts (8 amino acid changes for VH and 11 for VL genes respectively, compared to 25 amino acid changes for 2F5). m66 and m66.6 VH gene was closest to the germ line IGHV5-51* and VL gene to the VK1-39*01. m66 and m66.6 bind to the DKW core 2F5 epitope and require also two upstream 660L and 663L residues indicating that their epitopes overlap but not are identical to 2F5 epitope. m66.6 had higher neutralizing activity than m66, but weaker than 2F5 in a TZM-bl cell assay. m66 was not polyreactive with the panel of autoantigens. Zhu2011 (antibody binding site, antibody generation, neutralization, antibody sequence, antibody lineage)

References

Showing 2 of 2 references.

Isolation Paper
Zhu2011 Zhongyu Zhu, Haiyan Rebekah Qin, Weizao Chen, Qi Zhao, Xiaoying Shen, Robert Schutte, Yanping Wang, Gilad Ofek, Emily Streaker, Ponraj Prabakaran, Genevieve G. Fouda, Hua-Xin Liao, John Owens, Mark Louder, Yongping Yang, Kristina-Ana Klaric, M. Anthony Moody, John R. Mascola, Jamie K. Scott, Peter D. Kwong, David Montefiori, Barton F. Haynes, Georgia D. Tomaras, and Dimiter S. Dimitrov. Cross-Reactive HIV-1-Neutralizing Human Monoclonal Antibodies Identified from a Patient with 2F5-Like Antibodies. J. Virol., 85(21):11401-11408, Nov 2011. PubMed ID: 21880764. Show all entries for this paper.

Ofek2014 Gilad Ofek, Brett Zirkle, Yongping Yang, Zhongyu Zhu, Krisha McKee, Baoshan Zhang, Gwo-Yu Chuang, Ivelin S. Georgiev, Sijy O'Dell, Nicole Doria-Rose, John R. Mascola, Dimiter S. Dimitrov, and Peter D. Kwong. Structural Basis for HIV-1 neutralization By 2F5-Like Antibodies m66 and m66.6. J. Virol., 88(5):2426-2441, Mar 2014. PubMed ID: 24335316. Show all entries for this paper.

Displaying record number 2664

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MAb ID	m66.6 (M66.6)
HXB2 Location	gp160(663-666) DNA(8211..8222)	gp160 Epitope Map
Author Location
Epitope	`LDKW`	Epitope Alignment
Ab Type	gp41 MPER (membrane proximal external region)
Neutralizing	P View neutralization details
Species (Isotype)	human(IgG1)
Patient	SC44
Immunogen	HIV-1 infection
Country	Netherlands
Keywords	antibody binding site, antibody generation, antibody interactions, antibody lineage, antibody polyreactivity, antibody sequence, broad neutralizer, memory cells, neutralization, review, structure, vaccine antigen design, vaccine-induced immune responses

Notes

Showing 5 of 5 notes.

m66.6: Crystal structure of m66 bound to its gp41 epitope and unbound structures of m66 and m66.6 are reported. m66.6 shares the same heavy chain with m66 based on VH precursor IGHV5-51*01, but differ by 7.8% in their IGKVI-39*01 based light chains, and it has a greater neutralization breadth than m66 (m66.6 neutralized 93% of 41 isolates, and m66 neutralized 2%). To understand the difference, 3 unique light chain CDR L1 m66.6 LC residues proximal to gp41 were introduced to m66 light chain, replacing S28, G30, S31, and the new variants were tested against the same virus panel. Single substitutions S28H, S31K and G30K increased breadth to 7%, 17% and 65% respectively, and all 3 substitutions introduced together increased breadth to 83%, confirming that these 3 residues of m66.6 LC are critical for neutralization, with K30 playing central role. Ofek2014 (structure)
m66.6: "Neutralization fingerprints" for 30 neutralizing antibodies were determined using a panel of 34 diverse HIV-1 strains. 10 antibody clusters were defined: VRC01-like, PG9-like, PGT128-like, 2F5-like, 10E8-like and separate clusters for b12, CD4, 2G12, HJ16, 8ANC195. This mAb belongs to 2F5-like cluster. Georgiev2013 (neutralization)
m66.6: This review discusses how analysis of infection and vaccine candidate-induced antibodies and their genes may guide vaccine design. This MAb is listed as cross-reactive neutralizing gp41 MPER antibody, and isolated after 2009 by neutralization screening of cultured, unselected IgG+ memory B cells. Bonsignori2012b (vaccine antigen design, vaccine-induced immune responses, review)
M66.6: The use of computationally derived B cell clonal lineages as templates for HIV-1 immunogen design is discussed. M66.6 has been discussed in terms of immunogenic and functional characteristics of representative HIV-1 BnAbs and their reactions to antigens. Haynes2012 (antibody interactions, memory cells, vaccine antigen design, review, antibody polyreactivity, broad neutralizer)
m66.6: Two human MAbs, m66 and m66.6, were identified from 2F5-like serum of HIV-1-infected patient. These new MAbs mimic 2F5 in terms of their MPER binding profiles and neutralize a subset of the viruses neutralized by 2F5, while being significantly less divergent than 2F5 from their germ line-encoded counterparts (8 amino acid changes for VH and 11 for VL genes respectively, compared to 25 amino acid changes for 2F5). The m66 and m66.6 VH gene was closest to the germ line IGHV5-51*, and the VL gene was closest to the VK1-39*01. Both m66 and m66.6 bind to the DKW core 2F5 epitope and also require two upstream 660L and 663L residues, indicating that their epitopes overlap but are not identical to the 2F5 epitope. m66.6 had higher neutralizing activity than m66, but weaker than 2F5 in a TZM-bl cell assay. m66.6, but not m66, was polyreactive with the panel of autoantigens. Zhu2011 (antibody binding site, antibody generation, neutralization, antibody sequence, antibody lineage, antibody polyreactivity)

References

Showing 5 of 5 references.

Bonsignori2012b Mattia Bonsignori, S. Munir Alam, Hua-Xin Liao, Laurent Verkoczy, Georgia D. Tomaras, Barton F. Haynes, and M. Anthony Moody. HIV-1 Antibodies from Infection and Vaccination: Insights for Guiding Vaccine Design. Trends Microbiol., 20(11):532-539, Nov 2012. PubMed ID: 22981828. Show all entries for this paper.

Georgiev2013 Ivelin S. Georgiev, Nicole A. Doria-Rose, Tongqing Zhou, Young Do Kwon, Ryan P. Staupe, Stephanie Moquin, Gwo-Yu Chuang, Mark K. Louder, Stephen D. Schmidt, Han R. Altae-Tran, Robert T. Bailer, Krisha McKee, Martha Nason, Sijy O'Dell, Gilad Ofek, Marie Pancera, Sanjay Srivatsan, Lawrence Shapiro, Mark Connors, Stephen A. Migueles, Lynn Morris, Yoshiaki Nishimura, Malcolm A. Martin, John R. Mascola, and Peter D. Kwong. Delineating Antibody Recognition in Polyclonal Sera from Patterns of HIV-1 Isolate Neutralization. Science, 340(6133):751-756, 10 May 2013. PubMed ID: 23661761. Show all entries for this paper.

Haynes2012 Barton F. Haynes, Garnett Kelsoe, Stephen C. Harrison, and Thomas B. Kepler. B-Cell-Lineage Immunogen Design in Vaccine Development with HIV-1 as a Case Study. Nat. Biotechnol., 30(5):423-433, May 2012. PubMed ID: 22565972. Show all entries for this paper.

Displaying record number 3119

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MAb ID	m66S28_LCH
HXB2 Location	gp160(663-666) DNA(8211..8222)	gp160 Epitope Map
Author Location
Epitope	`LDKW`	Epitope Alignment
Ab Type	gp41 MPER (membrane proximal external region)
Neutralizing	P View neutralization details
Species (Isotype)	human(IgG1)
Patient	SC44
Immunogen	HIV-1 infection
Country	Netherlands
Keywords	antibody generation, chimeric antibody, structure

Notes

Showing 1 of 1 note.

m66S28_LCH: Crystal structure of m66 bound to its gp41 epitope and unbound structures of m66 and m66.6 are reported. To test whether residues of the m66.6 CDRL1 were the basis for its greater neutralization capacity than m66, variants were designed by substituting m66.6 CDR L1 residues into m66 CDRL1. This m66 variant Ab contained His28 from m66.6 CDR LC replacing Ser28 and could neutralize 3 viruses from a panel of 41 virus isolates. This single substitution exhibited 7% increase in neutralization. Ofek2014 (antibody generation, structure, chimeric antibody)

References

Showing 1 of 1 reference.

Isolation Paper
Ofek2014 Gilad Ofek, Brett Zirkle, Yongping Yang, Zhongyu Zhu, Krisha McKee, Baoshan Zhang, Gwo-Yu Chuang, Ivelin S. Georgiev, Sijy O'Dell, Nicole Doria-Rose, John R. Mascola, Dimiter S. Dimitrov, and Peter D. Kwong. Structural Basis for HIV-1 neutralization By 2F5-Like Antibodies m66 and m66.6. J. Virol., 88(5):2426-2441, Mar 2014. PubMed ID: 24335316. Show all entries for this paper.

Displaying record number 3120

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MAb ID	m66G30_LCK
HXB2 Location	gp160(663-666) DNA(8211..8222)	gp160 Epitope Map
Author Location
Epitope	`LDKW`	Epitope Alignment
Ab Type	gp41 MPER (membrane proximal external region)
Neutralizing	P View neutralization details
Species (Isotype)	human(IgG1)
Patient	SC44
Immunogen	HIV-1 infection
Country	Netherlands
Keywords	antibody generation, chimeric antibody, structure

Notes

Showing 1 of 1 note.

m66G30_LCK: Crystal structure of m66 bound to its gp41 epitope and unbound structures of m66 and m66.6 are reported. To test whether residues of the m66.6 CDRL1 were the basis for its greater neutralization capacity than m66, variants were designed by substituting m66.6 CDR L1 residues into m66 CDRL1. This m66 variant Ab contained Lys30 from m66.6 CDR LC replacing Gly30 and showed very high neutralization potency against a panel of 41 virus isolates. This single substitution showed > 30% increase in neutralization. Ofek2014 (antibody generation, structure, chimeric antibody)

References

Showing 1 of 1 reference.

Displaying record number 3121

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MAb ID	m66S31_LCK
HXB2 Location	gp160(663-666) DNA(8211..8222)	gp160 Epitope Map
Author Location
Epitope	`LDKW`	Epitope Alignment
Ab Type	gp41 MPER (membrane proximal external region)
Neutralizing	P View neutralization details
Species (Isotype)	human(IgG1)
Patient	SC44
Immunogen	HIV-1 infection
Country	Netherlands
Keywords	antibody generation, chimeric antibody, structure

Notes

Showing 1 of 1 note.

m66S31_LCK: Crystal structure of m66 bound to its gp41 epitope and unbound structures of m66 and m66.6 are reported. To test whether residues of the m66.6 CDRL1 were the basis for its greater neutralization capacity than m66, variants were designed by substituting m66.6 CDR L1 residues into m66 CDRL1. This m66 variant Ab contained Lys31 from m66.6 CDR LC replacing Ser31 and could neutralize 6 viruses from a panel of 41 virus isolates. This single substitution showed 17% increase in neutralization. Ofek2014 (antibody generation, structure, chimeric antibody)

References

Showing 1 of 1 reference.

Displaying record number 3122

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MAb ID	m66Y100e_HCW
HXB2 Location	gp160(663-666) DNA(8211..8222)	gp160 Epitope Map
Author Location
Epitope	`LDKW`	Epitope Alignment
Ab Type	gp41 MPER (membrane proximal external region)
Neutralizing	P View neutralization details
Species (Isotype)	human(IgG1)
Patient	SC44
Immunogen	HIV-1 infection
Country	Netherlands
Keywords	antibody generation, chimeric antibody, structure

Notes

Showing 1 of 1 note.

m66Y100e_HCW: Crystal structure of m66 bound to its gp41 epitope and unbound structures of m66 and m66.6 are reported. To test the role of m66.6/m66 CDR H3 loop in a lipid context, gp41 MPER recognition and HIV-1 neutralization, mutants were designed to alter hydrophobicity and explore the effect on neutralization. This m66 variant Ab contained Tyr100e from m66.6 CDR HC replacing Trp and neutralized 34% of the viruses tested against a panel of 41 virus isolates. Ofek2014 (antibody generation, structure, chimeric antibody)

References

Showing 1 of 1 reference.

Displaying record number 3123

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MAb ID	m66S28_LCH-G30_LCK
HXB2 Location	gp160(663-666) DNA(8211..8222)	gp160 Epitope Map
Author Location
Epitope	`LDKW`	Epitope Alignment
Ab Type	gp41 MPER (membrane proximal external region)
Neutralizing	P View neutralization details
Species (Isotype)	human
Patient	SC44
Immunogen	HIV-1 infection
Keywords	antibody generation, chimeric antibody, structure

Notes

Showing 1 of 1 note.

m66S28_LCH-G30_LCK: Crystal structure of m66 bound to its gp41 epitope and unbound structures of m66 and m66.6 are reported. To test whether residues of the m66.6 CDRL1 were the basis for its greater neutralization capacity than m66, variants were designed by substituting m66.6 CDR L1 Serine residues into m66 CDRL1. This m66 variant Ab showed high neutralization potency against a panel of 41 virus isolates. This double substitution showed a slight detrimental effect compared to the single substitution as in m66G30_LCK as the neutralization potency didn't increase. Ofek2014 (antibody generation, structure, chimeric antibody)

References

Showing 1 of 1 reference.

Displaying record number 3124

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MAb ID	m66S28_LCH-G30_LCK-S31_LCK
HXB2 Location	gp160(663-666) DNA(8211..8222)	gp160 Epitope Map
Author Location
Epitope	`LDKW`	Epitope Alignment
Ab Type	gp41 MPER (membrane proximal external region)
Neutralizing	P View neutralization details
Species (Isotype)	human(IgG1)
Patient	SC44
Immunogen	HIV-1 infection
Country	Netherlands
Keywords	antibody generation, chimeric antibody, structure

Notes

Showing 1 of 1 note.

m66S28_LCH-G30_LCK-S31_LCK: Crystal structure of m66 bound to its gp41 epitope and unbound structures of m66 and m66.6 are reported. To test whether residues of the m66.6 CDRL1 were the basis for its greater neutralization capacity than m66, variants were designed by substituting m66.6 CDR L1 residues into m66 CDRL1. This m66 variant Ab had His28, Lys30 and Lys31 from m66.6 CDR LC replacing Ser28,Gly30 and Ser31 respectively and showed very high neutralization potency against a panel of 41 virus isolates. This triple substitution showed a very high > 40 fold increase in neutralization breath over WT m66 confirming that Lys30 of m66.6 CDR L1 plays the central role in neutralization. Ofek2014 (antibody generation, structure, chimeric antibody)

References

Showing 1 of 1 reference.

Displaying record number 3125

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MAb ID	m66 WT CDR H3
HXB2 Location	gp160(663-666) DNA(8211..8222)	gp160 Epitope Map
Author Location
Epitope	`LDKW`	Epitope Alignment
Ab Type	gp41 MPER (membrane proximal external region)
Neutralizing	P
Species (Isotype)	human(IgG1)
Patient	SC44
Immunogen	HIV-1 infection
Country	Netherlands
Keywords	antibody generation, chimeric antibody, structure

Notes

Showing 1 of 1 note.

m66 WT CDR H3: Crystal structure of m66 bound to its gp41 epitope and unbound structures of m66 and m66.6 are reported. To test the role of the m66.6/m66 CDR H3 loop in a lipid context, gp41 MPER recognition and HIV-1 neutralization, mutants were designed to alter hydrophobicity and explore the effect on neutralization. This Ab was included because m66.6 shares the same CDR H3 loop with m66. It showed moderate neutralization potency against a panel of 41 virus isolates. Ofek2014 (antibody generation, structure, chimeric antibody)

References

Showing 1 of 1 reference.

Displaying record number 3126

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MAb ID	m66.6 Y100c_HCS
HXB2 Location	gp160(663-666) DNA(8211..8222)	gp160 Epitope Map
Author Location
Epitope	`LDKW`	Epitope Alignment
Ab Type	gp41 MPER (membrane proximal external region)
Neutralizing
Species (Isotype)	human(IgG1)
Patient	SC44
Immunogen	HIV-1 infection
Country	Netherlands
Keywords	antibody generation, chimeric antibody, structure

Notes

Showing 1 of 1 note.

m66.6 Y100c_HCS: Crystal structure of m66 bound to its gp41 epitope and unbound structures of m66 and m66.6 are reported. To test the role of the m66.6/m66 CDR H3 loop in a lipid context, gp41 MPER recognition and HIV-1 neutralization, mutants were designed to alter hydrophobicity and explore the effect on neutralization. This m66.6 CDR H3 variant Ab showed moderate neutralization potency. Ofek2014 (antibody generation, structure, chimeric antibody)

References

Showing 1 of 1 reference.

Displaying record number 3127

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MAb ID	m66.6 F100d_HCS
HXB2 Location	gp160(663-666) DNA(8211..8222)	gp160 Epitope Map
Author Location
Epitope	`LDKW`	Epitope Alignment
Ab Type	gp41 MPER (membrane proximal external region)
Neutralizing	P
Species (Isotype)	human
Patient	SC44
Immunogen	HIV-1 infection
Country	United States
Keywords	antibody generation, chimeric antibody, structure

Notes

Showing 1 of 1 note.

m66.6 F100d_HCS: Crystal structure of m66 bound to its gp41 epitope and unbound structures of m66 and m66.6 are reported. To test the role of the m66.6/m66 CDR H3 loop in a lipid context, gp41 MPER recognition and HIV-1 neutralization, mutants were designed to alter hydrophobicity and explore the effect on neutralization.This m66 variant Ab contained Phe100d from m66.6 CDR HC replacing Ser and showed moderate neutralization potency. Ofek2014 (antibody generation, structure, chimeric antibody)

References

Showing 1 of 1 reference.

Displaying record number 3129

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MAb ID	m66.6 Y100c_HCS-F100d_HCS
HXB2 Location	gp160(663-666) DNA(8211..8222)	gp160 Epitope Map
Author Location
Epitope	`LDKW`	Epitope Alignment
Ab Type	gp41 MPER (membrane proximal external region)
Neutralizing	P
Species (Isotype)	human(IgG1)
Patient	SC44
Immunogen	HIV-1 infection
Country	Netherlands
Keywords	antibody generation, chimeric antibody, structure

Notes

Showing 1 of 1 note.

m66.6 Y100c_HCS-F100d_HCS: Crystal structure of m66 bound to its gp41 epitope and unbound structures of m66 and m66.6 are reported. To test the role of the m66.6/m66 CDR H3 loop in a lipid context, gp41 MPER recognition and HIV-1 neutralization, mutants were designed to alter hydrophobicity and explore the effect on neutralization. This m66 variant Ab contained Tyr100c and Phe100d from m66.6 CDR HC replacing Ser at both places.This m66.6 CDR H3 variant showed moderate neutralization potency. Ofek2014 (antibody generation, structure, chimeric antibody)

References

Showing 1 of 1 reference.

Displaying record number 3130

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MAb ID	m66.6 Y100c_HCS-Y100e_HCS
HXB2 Location	gp160(663-666) DNA(8211..8222)	gp160 Epitope Map
Author Location
Epitope	`LDKW`	Epitope Alignment
Ab Type	gp41 MPER (membrane proximal external region)
Neutralizing	P
Species (Isotype)	human(IgG1)
Patient	SC44
Immunogen	HIV-1 infection
Country	Netherlands
Keywords	antibody generation, chimeric antibody, structure

Notes

Showing 1 of 1 note.

m66.6 Y100c_HCS-Y100e_HCS: Crystal structure of m66 bound to its gp41 epitope and unbound structures of m66 and m66.6 are reported. To test the role of the m66.6/m66 CDR H3 loop in a lipid context, gp41 MPER recognition and HIV-1 neutralization, mutants were designed to alter hydrophobicity and explore the effect on neutralization. This m66 variant Ab contained Tyr100c and Tyr100e from m66.6 CDR HC replacing Ser100c and Ser100e. This m66.6 CDR H3 variant showed moderate neutralization potency. Ofek2014 (antibody generation, structure, chimeric antibody)

References

Showing 1 of 1 reference.

Displaying record number 3131

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MAb ID	m66.6 S100b_HCW
HXB2 Location	gp160(663-666) DNA(8211..8222)	gp160 Epitope Map
Author Location
Epitope	`LDKW`	Epitope Alignment
Ab Type	gp41 MPER (membrane proximal external region)
Neutralizing	P
Species (Isotype)	human(IgG1)
Patient	SC44
Immunogen	HIV-1 infection
Country	Netherlands
Keywords	antibody generation, chimeric antibody, structure

Notes

Showing 1 of 1 note.

m66.6 S100b_HCW: Crystal structure of m66 bound to its gp41 epitope and unbound structures of m66 and m66.6 are reported. To test the role of the m66.6/m66 CDR H3 loop in a lipid context, gp41 MPER recognition and HIV-1 neutralization, mutants were designed to alter hydrophobicity and explore the effect on neutralization. This m66 variant Ab contained Ser100b from m66.6 CDR HC replacing Trp and showed moderate neutralization potency. Ofek2014 (antibody generation, structure, chimeric antibody)

References

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Displaying record number 3132

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MAb ID	m66.6 Y100c_HCW
HXB2 Location	gp160(663-666) DNA(8211..8222)	gp160 Epitope Map
Author Location
Epitope	`LDKW`	Epitope Alignment
Ab Type	gp41 MPER (membrane proximal external region)
Neutralizing	P
Species (Isotype)	human(IgG1)
Patient	SC44
Immunogen	HIV-1 infection
Country	Netherlands
Keywords	antibody generation, chimeric antibody, structure

Notes

Showing 1 of 1 note.

m66.6 Y100c_HCW: Crystal structure of m66 bound to its gp41 epitope and unbound structures of m66 and m66.6 are reported. To test the role of the m66.6/m66 CDR H3 loop in a lipid context, gp41 MPER recognition and HIV-1 neutralization, mutants were designed to alter hydrophobicity and explore the effect on neutralization.This m66 variant Ab contained Tyr100c from m66.6 CDR HC replacing Trp and showed moderate neutralization potency. Ofek2014 (antibody generation, structure, chimeric antibody)

References

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Displaying record number 3133

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MAb ID	m66.6 Y100e_HCS
HXB2 Location	gp160(663-666) DNA(8211..8222)	gp160 Epitope Map
Author Location
Epitope	`LDKW`	Epitope Alignment
Ab Type	gp41 MPER (membrane proximal external region)
Neutralizing	P
Species (Isotype)	human(IgG1)
Patient	SC44
Immunogen	HIV-1 infection
Country	Netherlands
Keywords	antibody generation, chimeric antibody, structure

Notes

Showing 1 of 1 note.

m66.6 Y100e_HCS: Crystal structure of m66 bound to its gp41 epitope and unbound structures of m66 and m66.6 are reported. To test the role of the m66.6/m66 CDR H3 loop in a lipid context, gp41 MPER recognition and HIV-1 neutralization, mutants were designed to alter hydrophobicity and explore the effect on neutralization. This m66 variant Ab contained Tyr100e from m66.6 CDR HC replacing Ser and showed moderate neutralization potency. Ofek2014 (antibody generation, structure, chimeric antibody)

References

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Displaying record number 3134

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MAb ID	m66.6 Y100c_HCW-Y100e_HCW
HXB2 Location	gp160(663-666) DNA(8211..8222)	gp160 Epitope Map
Author Location
Epitope	`LDKW`	Epitope Alignment
Ab Type	gp41 MPER (membrane proximal external region)
Neutralizing
Species (Isotype)	human(IgG1)
Patient	SC44
Immunogen	HIV-1 infection
Country	Netherlands
Keywords	antibody generation, chimeric antibody, structure

Notes

Showing 1 of 1 note.

m66.6 Y100c_HCW-Y100e_HCW: Crystal structure of m66 bound to its gp41 epitope and unbound structures of m66 and m66.6 are reported. To test the role of the m66.6/m66 CDR H3 loop in a lipid context, gp41 MPER recognition and HIV-1 neutralization, mutants were designed to alter hydrophobicity and explore the effect on neutralization. This m66 variant Ab contained Tyr100c and Tyr100e from m66.6 CDR HC replacing Trp at both places. This m66.6 CDR H3 variant showed moderate neutralization potency. Ofek2014 (antibody generation, structure, chimeric antibody)

References

Showing 1 of 1 reference.