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Found 11 matching records:

Displaying record number 1840

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MAb ID	Fab 3674
HXB2 Location	Env	Env Epitope Map
Author Location	gp120
Epitope
Ab Type	gp41 six-helix bundle
Neutralizing
Species (Isotype)	human
Patient
Immunogen	in vitro stimulation or selection
Keywords	antibody binding site, binding affinity, kinetics, neutralization, review, variant cross-reactivity

Notes

Showing 4 of 4 notes.

• Fab 3674: This review discusses current understanding of Env neutralization by antibodies in relation to epitope exposure and how this insight might benefit vaccine design strategies. This MAb is in the list of current MAbs with notable cross-neutralizing activity. Pantophlet2010 (neutralization, variant cross-reactivity, review)
• Fab 3674: The potency of this MAb was improved by affinity maturation. Fab 3674 neutralized 6 out of 7 HIV strains, and only 3/10 maturated Fabs showed improved neutralization activity relative to Fab 3674. For this Ab, the bivalent format was shown to be 10-20-fold more potent than the monovalent format in terms of neutralization activity for a panel of B and C clades, corresponding to tier 2 isolates. In inhibition of viral infectivity, Fab 3674 was essentially inactive post-CD4 engagement. Gustchina2009 (neutralization, variant cross-reactivity)
• Fab 3674: The IC50 for bivalent Fab 3675 (bF-3674) in a standard neutralization assay is 88nM and is only minimally affected in the postattachment neutralization assay. The neutralization half-life for bF-3674 is 20.6 minutes and is increased 30% to 27.7 minutes in the presence of N36Mut(e,g) peptide, which is a class 3 inhibitor that prolongates temporal window of neutralization by disrupting trimerization of the N-heptad repeat (N-HR) in the prehairpin intermediate by sequestering the N-HR into N-HR/N36Mut(e,g) heterodimers. Both HXB2 and HIV-1 primary isolates of subtypes B and C were neutralized synergistically by bF-3674 and N36Mut(e,g). HXB2 was also neutralized synergistically by bF-3674 and CD4. Gustchina2008 (antibody binding site, neutralization, variant cross-reactivity, kinetics)
• Fab 3674: Fab 3674 was selected from a human phage library by panning against a chimeric construct that exposes coiled-coil of gp41 N helices. The epitope for the Fab 3674 comprises of: E560, H564, W571, K574 and Q575, and is located in the shallow groove on the N helices, exposed between two C helices in the fusiogenic six-helix bundle conformation of gp41. Fab 3674 had broadly neutralizing activity against several subtype B isolates, and also subtypes A and C, as its epitope is conserved among these subtypes. A fusion inhibitor (C34) and Fab 3674 were shown to have additive and synergistic actions on the fusion inhibition of HIV-1. Gustchina2007 (antibody binding site, neutralization, variant cross-reactivity, binding affinity)

References

Showing 4 of 4 references.

Gustchina2007 Elena Gustchina, John M. Louis, Son N. Lam, Carole A. Bewley, and G. Marius Clore. A Monoclonal Fab Derived from a Human Nonimmune Phage Library Reveals a New Epitope on gp41 and Neutralizes Diverse Human Immunodeficiency Virus Type 1 Strains. J. Virol., 81(23):12946-12953, Dec 2007. PubMed ID: 17898046. Show all entries for this paper.

Gustchina2008 Elena Gustchina, Carole A. Bewley, and G. Marius Clore. Sequestering of the Prehairpin Intermediate of gp41 by Peptide N36Mut(e,g) Potentiates the Human Immunodeficiency Virus Type 1 Neutralizing Activity of Monoclonal Antibodies Directed against the N-Terminal Helical Repeat of gp41. J. Virol., 82(20):10032-10041, Oct 2008. PubMed ID: 18667502. Show all entries for this paper.

Gustchina2009 Elena Gustchina, John M. Louis, Christian Frisch, Francisco Ylera, Annette Lechner, Carole A. Bewley, and G. Marius Clore. Affinity Maturation by Targeted Diversification of the CDR-H2 Loop of a Monoclonal Fab Derived from a Synthetic Naive Human Antibody Library and Directed against the Internal Trimeric Coiled-Coil of gp41 Yields a Set of Fabs with Improved HIV-1 Neutralization Potency and Breadth. Virology, 393(1):112-119, 10 Oct 2009. PubMed ID: 19695655. Show all entries for this paper.

Pantophlet2010 Ralph Pantophlet. Antibody Epitope Exposure and Neutralization of HIV-1. Curr. Pharm. Des., 16(33):3729-3743, 2010. PubMed ID: 21128886. Show all entries for this paper.

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Displaying record number 2053

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MAb ID	Fab 8059
HXB2 Location	Env	Env Epitope Map
Author Location	gp41
Epitope
Ab Type
Neutralizing
Species (Isotype)
Patient
Immunogen	in vitro stimulation or selection
Keywords	binding affinity, neutralization

Notes

Showing 1 of 1 note.

• 8059: 8059 was derived by affinity maturation of the parent Fab 3674. 8059 bound to the same epitope as the parental Fab and showed improved binding affinity towards the target peptide compared to the parent Fab 3674. This Ab had similar neutralization activity as the parental Fab. Gustchina2009 (neutralization, binding affinity)

References

Showing 1 of 1 reference.

Gustchina2009 Elena Gustchina, John M. Louis, Christian Frisch, Francisco Ylera, Annette Lechner, Carole A. Bewley, and G. Marius Clore. Affinity Maturation by Targeted Diversification of the CDR-H2 Loop of a Monoclonal Fab Derived from a Synthetic Naive Human Antibody Library and Directed against the Internal Trimeric Coiled-Coil of gp41 Yields a Set of Fabs with Improved HIV-1 Neutralization Potency and Breadth. Virology, 393(1):112-119, 10 Oct 2009. PubMed ID: 19695655. Show all entries for this paper.

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Displaying record number 2054

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MAb ID	Fab 8061
HXB2 Location	Env	Env Epitope Map
Author Location	gp41
Epitope
Ab Type
Neutralizing
Species (Isotype)
Patient
Immunogen	in vitro stimulation or selection
Keywords	binding affinity, neutralization

Notes

Showing 1 of 1 note.

• 8061: 8061 was derived by affinity maturation of the parent Fab 3674. 8061 bound to the same epitope as the parental Fab and showed improved binding affinity towards the target peptide compared to the parent Fab 3674. However, this Ab did not neutralize any of the laboratory adapted subtype B strains. Gustchina2009 (neutralization, binding affinity)

References

Showing 1 of 1 reference.

Gustchina2009 Elena Gustchina, John M. Louis, Christian Frisch, Francisco Ylera, Annette Lechner, Carole A. Bewley, and G. Marius Clore. Affinity Maturation by Targeted Diversification of the CDR-H2 Loop of a Monoclonal Fab Derived from a Synthetic Naive Human Antibody Library and Directed against the Internal Trimeric Coiled-Coil of gp41 Yields a Set of Fabs with Improved HIV-1 Neutralization Potency and Breadth. Virology, 393(1):112-119, 10 Oct 2009. PubMed ID: 19695655. Show all entries for this paper.

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Displaying record number 2055

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MAb ID	Fab 8062
HXB2 Location	Env	Env Epitope Map
Author Location	gp41
Epitope
Ab Type
Neutralizing
Species (Isotype)
Patient
Immunogen	in vitro stimulation or selection
Keywords	antibody binding site, binding affinity, mimotopes, neutralization, structure

Notes

Showing 3 of 3 notes.

• 8062: Mini-Abs, monovalent and bivalent Fabs targeting the conserved internal trimeric coiled-coil of the Nheptad repeat (N-HR) of gp41 has been previously reported. Crystal structures and binding of closely related monovalent Fabs, Fab 8066 and Fab 8062 to covalently stabilized chimeric trimers of N-peptides of gp41,CCIZN36)3 has been reported. Crystal structures of the complexes between 3-H and Fab 8066 and Fab 8062 were determined at 2.8 and 3.0 A° resolution, respectively. The structural data indicate that binding of three Fabs 8062 with high affinity requires more significant changes in the structure of the N-HR trimer compared to binding of Fab 8066. Gustchina2013 (mimotopes, structure)
• 8062: Crystal structure of the non-neutralizing 8062 Fab in complex with 5-Helix was compared to the crystal structure of the broadly neutralizing 8066 MAb and MAb D5. For all three Abs, binding affinity correlated with neutralization activity. Structural modeling analyses revealed relatively small differences in the interactions of this Ab with the antigen compared with 8066 and D5. CDR-H2 of 8062 was barely touching the surface of the 5-Helix while CDR-H2 of 8066 was buried in the body of the bundle. Additional interactions, and higher affinity of shared interactions of 8066 compared to 8062 were found, indicating that the difference of 8062 and 8066 in their ability to bind 5-Helix reflects the difference in the neutralization activities of these two MAbs. Gustchina2010 (antibody binding site, binding affinity, structure)
• 8062: 8062 was derived by affinity maturation of the parent Fab 3674. 8062 bound to the same epitope as the parental Fab and showed improved binding affinity towards the target peptide compared to the parent Fab 3674. However, this Ab did not neutralize any of the laboratory adapted subtype B strains. Gustchina2009 (neutralization, binding affinity)

References

Showing 3 of 3 references.

Gustchina2009 Elena Gustchina, John M. Louis, Christian Frisch, Francisco Ylera, Annette Lechner, Carole A. Bewley, and G. Marius Clore. Affinity Maturation by Targeted Diversification of the CDR-H2 Loop of a Monoclonal Fab Derived from a Synthetic Naive Human Antibody Library and Directed against the Internal Trimeric Coiled-Coil of gp41 Yields a Set of Fabs with Improved HIV-1 Neutralization Potency and Breadth. Virology, 393(1):112-119, 10 Oct 2009. PubMed ID: 19695655. Show all entries for this paper.

Gustchina2010 Elena Gustchina, Mi Li, John M. Louis, D. Eric Anderson, John Lloyd, Christian Frisch, Carole A. Bewley, Alla Gustchina, Alexander Wlodawer, and G. Marius Clore. Structural Basis of HIV-1 Neutralization by Affinity Matured Fabs Directed against the Internal Trimeric Coiled-Coil of gp41. PLoS Pathog., 6(11):e1001182, 2010. PubMed ID: 21085615. Show all entries for this paper.

Gustchina2013 Elena Gustchina, Mi Li, Rodolfo Ghirlando, Peter Schuck, John M. Louis, Jason Pierson, Prashant Rao, Sriram Subramaniam, Alla Gustchina, G. Marius Clore, and Alexander Wlodawer. Complexes of Neutralizing and Non-Neutralizing Affinity Matured Fabs with a Mimetic of the Internal Trimeric Coiled-Coil of HIV-1 gp41. PLoS One, 8(11):e78187, 2013. PubMed ID: 24244293. Show all entries for this paper.

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Displaying record number 2056

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MAb ID	Fab 8063
HXB2 Location	Env	Env Epitope Map
Author Location	gp41
Epitope
Ab Type
Neutralizing
Species (Isotype)
Patient
Immunogen	in vitro stimulation or selection
Keywords	binding affinity, neutralization

Notes

Showing 1 of 1 note.

• 8063: 8063 was derived by affinity maturation of the parent Fab 3674. 8063 bound to the same epitope as the parental Fab and showed improved binding affinity towards the target peptide compared to the parent Fab 3674. However, this Ab did not neutralize any of the laboratory adapted subtype B strains. Gustchina2009 (neutralization, binding affinity)

References

Showing 1 of 1 reference.

Gustchina2009 Elena Gustchina, John M. Louis, Christian Frisch, Francisco Ylera, Annette Lechner, Carole A. Bewley, and G. Marius Clore. Affinity Maturation by Targeted Diversification of the CDR-H2 Loop of a Monoclonal Fab Derived from a Synthetic Naive Human Antibody Library and Directed against the Internal Trimeric Coiled-Coil of gp41 Yields a Set of Fabs with Improved HIV-1 Neutralization Potency and Breadth. Virology, 393(1):112-119, 10 Oct 2009. PubMed ID: 19695655. Show all entries for this paper.

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Displaying record number 2058

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MAb ID	Fab 8064
HXB2 Location	Env	Env Epitope Map
Author Location	gp41
Epitope
Ab Type
Neutralizing
Species (Isotype)
Patient
Immunogen	in vitro stimulation or selection
Keywords	binding affinity, neutralization

Notes

Showing 1 of 1 note.

• 8064: 8064 was derived by affinity maturation of the parent Fab 3674. 8064 bound to the same epitope as the parental Fab and showed improved binding affinity towards the target peptide compared to the parent Fab 3674. This Ab had similar neutralization activity as the parental Fab. Gustchina2009 (neutralization, binding affinity)

References

Showing 1 of 1 reference.

Gustchina2009 Elena Gustchina, John M. Louis, Christian Frisch, Francisco Ylera, Annette Lechner, Carole A. Bewley, and G. Marius Clore. Affinity Maturation by Targeted Diversification of the CDR-H2 Loop of a Monoclonal Fab Derived from a Synthetic Naive Human Antibody Library and Directed against the Internal Trimeric Coiled-Coil of gp41 Yields a Set of Fabs with Improved HIV-1 Neutralization Potency and Breadth. Virology, 393(1):112-119, 10 Oct 2009. PubMed ID: 19695655. Show all entries for this paper.

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Displaying record number 2059

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MAb ID	Fab 8065
HXB2 Location	Env	Env Epitope Map
Author Location	gp41
Epitope
Ab Type
Neutralizing
Species (Isotype)
Patient
Immunogen	in vitro stimulation or selection
Keywords	binding affinity, neutralization

Notes

Showing 1 of 1 note.

• 8065: 8065 was derived by affinity maturation of the parent Fab 3674. 8065 bound to the same epitope as the parental Fab and showed improved binding affinity towards the target peptide compared to the parent Fab 3674. However, this Ab did not neutralize any of the laboratory adapted subtype B strains. Gustchina2009 (neutralization, binding affinity)

References

Showing 1 of 1 reference.

Gustchina2009 Elena Gustchina, John M. Louis, Christian Frisch, Francisco Ylera, Annette Lechner, Carole A. Bewley, and G. Marius Clore. Affinity Maturation by Targeted Diversification of the CDR-H2 Loop of a Monoclonal Fab Derived from a Synthetic Naive Human Antibody Library and Directed against the Internal Trimeric Coiled-Coil of gp41 Yields a Set of Fabs with Improved HIV-1 Neutralization Potency and Breadth. Virology, 393(1):112-119, 10 Oct 2009. PubMed ID: 19695655. Show all entries for this paper.

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Displaying record number 2060

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MAb ID	Fab 8069
HXB2 Location	Env	Env Epitope Map
Author Location	gp41
Epitope
Ab Type
Neutralizing
Species (Isotype)
Patient
Immunogen	in vitro stimulation or selection
Keywords	binding affinity, neutralization

Notes

Showing 1 of 1 note.

• 8069: 8069 was derived by affinity maturation of the parent Fab 3674. 8069 bound to the same epitope as the parental Fab and showed improved binding affinity towards the target peptide compared to the parent Fab 3674. This Ab had similar neutralization activity as the parental Fab. Gustchina2009 (neutralization, binding affinity)

References

Showing 1 of 1 reference.

Gustchina2009 Elena Gustchina, John M. Louis, Christian Frisch, Francisco Ylera, Annette Lechner, Carole A. Bewley, and G. Marius Clore. Affinity Maturation by Targeted Diversification of the CDR-H2 Loop of a Monoclonal Fab Derived from a Synthetic Naive Human Antibody Library and Directed against the Internal Trimeric Coiled-Coil of gp41 Yields a Set of Fabs with Improved HIV-1 Neutralization Potency and Breadth. Virology, 393(1):112-119, 10 Oct 2009. PubMed ID: 19695655. Show all entries for this paper.

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Displaying record number 2061

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MAb ID	Fab 8060
HXB2 Location	Env	Env Epitope Map
Author Location	gp41
Epitope
Ab Type
Neutralizing
Species (Isotype)
Patient
Immunogen	in vitro stimulation or selection
Keywords	binding affinity, neutralization

Notes

Showing 1 of 1 note.

• Fab 8060: 8060 was derived by affinity maturation of the parent Fab 3674. 8060 bound to the same epitope as the parental Fab and showed improved binding affinity towards the target peptide compared to the parent Fab 3674. This was one of three maturated Abs that showed significant increases in both breadth and potency of neutralization against primary isolates of subtypes B and C, compared to the parental Fab. The improved neutralization activity was greater for the Fabs in monovalent than in bivalent formats. Gustchina2009 (neutralization, binding affinity)

References

Showing 1 of 1 reference.

Gustchina2009 Elena Gustchina, John M. Louis, Christian Frisch, Francisco Ylera, Annette Lechner, Carole A. Bewley, and G. Marius Clore. Affinity Maturation by Targeted Diversification of the CDR-H2 Loop of a Monoclonal Fab Derived from a Synthetic Naive Human Antibody Library and Directed against the Internal Trimeric Coiled-Coil of gp41 Yields a Set of Fabs with Improved HIV-1 Neutralization Potency and Breadth. Virology, 393(1):112-119, 10 Oct 2009. PubMed ID: 19695655. Show all entries for this paper.

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Displaying record number 2062

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MAb ID	Fab 8066 (8066)
HXB2 Location	Env	Env Epitope Map
Author Location	gp41
Epitope
Ab Type
Neutralizing
Species (Isotype)
Patient
Immunogen	in vitro stimulation or selection
Keywords	ADCC, antibody binding site, binding affinity, mimotopes, neutralization, structure

Notes

Showing 4 of 4 notes.

• 8066: Isolation of human mAb, E10, from an HIV-1-infected patient sample by single B cell sorting and single cell PCR has been reported. E10 showed binding to gp140 trimer and linear peptides derived from gp41 membrane proximal external region (MPER). IgG E10 use a famous V gene segment IGHV1-69 allelic variants including Fab 8066. Fine mapping of E10 epitope may potentiate MPER-based subunit vaccine development. Yang2018 (ADCC)
• 8066: Mini-Abs, monovalent and bivalent Fabs targeting the conserved internal trimeric coiled-coil of the Nheptad repeat (N-HR) of gp41 has been previously reported. Crystal structures and binding of closely related monovalent Fabs, Fab 8066 and Fab 8062 to covalently stabilized chimeric trimers of N-peptides of gp41,CCIZN36)3 has been reported. Crystal structures of the complexes between 3-H and Fab 8066 and Fab 8062 were determined at 2.8 and 3.0 A° resolution, respectively. The structural data indicate that binding of three Fabs 8062 with high affinity requires more significant changes in the structure of the N-HR trimer compared to binding of Fab 8066. Gustchina2013 (mimotopes, structure)
• 8066: Crystal structure of the broadly neutralizing 8066 Fab in complex with 5-Helix was compared to the crystal structure of the non-neutralizing 8062 MAb and MAb D5. For all three Abs, binding affinity correlated with neutralization activity. Structural modeling analyses revealed relatively small differences in the interactions of this Ab with the antigen compared with 8062 and D5. CDR-H2 of 8062 was barely touching the surface of the 5-Helix, while CDR-H2 of 8066 was buried in the body of the bundle. Additional interactions, and higher affinity of shared interactions of 8066 compared to 8062 were found, indicating that the difference of 8062 and 8066 in their ability to bind 5-Helix reflects the difference in the neutralization activities of these two MAbs. Gustchina2010 (antibody binding site, binding affinity, structure)
• Fab 8066: 8066 was derived by affinity maturation of the parent Fab 3674. 8066 bound to the same epitope as the parental Fab and showed improved binding affinity towards the target peptide compared to the parent Fab 3674. This was one of three maturated Abs that showed significant increases in both breadth and potency of neutralization against primary isolates of subtypes B and C, compared to the parental Fab. The improved neutralization activity was greater for the Fabs in monovalent than in bivalent formats. Gustchina2009 (neutralization, binding affinity)

References

Showing 4 of 4 references.

Gustchina2009 Elena Gustchina, John M. Louis, Christian Frisch, Francisco Ylera, Annette Lechner, Carole A. Bewley, and G. Marius Clore. Affinity Maturation by Targeted Diversification of the CDR-H2 Loop of a Monoclonal Fab Derived from a Synthetic Naive Human Antibody Library and Directed against the Internal Trimeric Coiled-Coil of gp41 Yields a Set of Fabs with Improved HIV-1 Neutralization Potency and Breadth. Virology, 393(1):112-119, 10 Oct 2009. PubMed ID: 19695655. Show all entries for this paper.

Gustchina2010 Elena Gustchina, Mi Li, John M. Louis, D. Eric Anderson, John Lloyd, Christian Frisch, Carole A. Bewley, Alla Gustchina, Alexander Wlodawer, and G. Marius Clore. Structural Basis of HIV-1 Neutralization by Affinity Matured Fabs Directed against the Internal Trimeric Coiled-Coil of gp41. PLoS Pathog., 6(11):e1001182, 2010. PubMed ID: 21085615. Show all entries for this paper.

Gustchina2013 Elena Gustchina, Mi Li, Rodolfo Ghirlando, Peter Schuck, John M. Louis, Jason Pierson, Prashant Rao, Sriram Subramaniam, Alla Gustchina, G. Marius Clore, and Alexander Wlodawer. Complexes of Neutralizing and Non-Neutralizing Affinity Matured Fabs with a Mimetic of the Internal Trimeric Coiled-Coil of HIV-1 gp41. PLoS One, 8(11):e78187, 2013. PubMed ID: 24244293. Show all entries for this paper.

Yang2018 Zheng Yang, Xi Liu, Zehua Sun, Jingjing Li, Weiguo Tan, Weiye Yu, and Meiyun Zhang. Identification of a HIV gp41-Specific Human Monoclonal Antibody with Potent Antibody-Dependent Cellular Cytotoxicity. Front. Immunol., 9:2613, 2018. PubMed ID: 30519238. Show all entries for this paper.

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Displaying record number 2063

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MAb ID	Fab 8068
HXB2 Location	Env	Env Epitope Map
Author Location	gp41
Epitope
Ab Type
Neutralizing
Species (Isotype)
Patient
Immunogen	in vitro stimulation or selection
Keywords	binding affinity, neutralization

Notes

Showing 1 of 1 note.

• Fab 8068: 8068 was derived by affinity maturation of the parent Fab 3674. 8068 bound to the same epitope as the parental Fab and showed improved binding affinity towards the target peptide compared to the parent Fab 3674. This was one of three maturated Abs that showed significant increases in both breadth and potency of neutralization against primary isolates of subtypes B and C, compared to the parental Fab. The improved neutralization activity was greater for the Fabs in monovalent than in bivalent formats. Gustchina2009 (neutralization, binding affinity)

References

Showing 1 of 1 reference.

Gustchina2009 Elena Gustchina, John M. Louis, Christian Frisch, Francisco Ylera, Annette Lechner, Carole A. Bewley, and G. Marius Clore. Affinity Maturation by Targeted Diversification of the CDR-H2 Loop of a Monoclonal Fab Derived from a Synthetic Naive Human Antibody Library and Directed against the Internal Trimeric Coiled-Coil of gp41 Yields a Set of Fabs with Improved HIV-1 Neutralization Potency and Breadth. Virology, 393(1):112-119, 10 Oct 2009. PubMed ID: 19695655. Show all entries for this paper.

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