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Displaying record number 1190
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MAb ID |
A1g8 (F425 A1g8, F425A1g8) |
HXB2 Location |
Env |
Env Epitope Map
|
Author Location |
gp120 |
Research Contact |
James Robinson, Tulane University Med School, New Orleans, LA, USA |
Epitope |
|
Subtype |
B |
Ab Type |
gp120 V3 // V3 glycan (V3g) |
Neutralizing |
|
Species
(Isotype)
|
human(IgG1λ) |
Patient |
|
Immunogen |
HIV-1 infection |
Keywords |
antibody generation, antibody interactions, binding affinity, co-receptor, neutralization, variant cross-reactivity |
Notes
Showing 5 of
5 notes.
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F425A1g8: Generation and characterization of F425A1g8 isotypes and HIV neutralization activities has been described. The IgG1 variant of F425A1g8 showed little neutralization in the absence of sCD4, but the IgA1 exhibited significant independent neutralization against clade B isolates. This study emphasizes on the unique molecular structure of IgA in HIV neutralization.
Yu2013a
(antibody generation, neutralization)
-
A1g8: To test whether HIV-1 particle maturation alters the conformation of the Env proteins, a sensitive and quantitative imaging-based Ab-binding assay was used to probe the conformations of full-length and cytoplasmic tail (CT) truncated Env proteins on mature and immature HIV-1 particles. In the absence of sCD4, MAb A1g8 binding to gp120 was approximately 20% greater on immature vs. mature HIV-1 particles. 17b, A1g8, and E51 binding to immature virions was stimulated by sCD4 to a greater or equal extent vs. mature particles, with MAb 17b exhibiting the greatest increase. Truncation of the CT abolished the enhanced sCD4-induced binding of A1g8 to immature particles. This suggested that CD4 binding triggers exposure of some epitopes to an equal extent on immature and mature virions and other epitopes to a greater extent on immature virions.
Joyner2011
(binding affinity)
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F425 A1g8: This Ab neutralized infection of PBLs with various HIV-1 strains. However, it did not inhibit transcytosis of cell-free or cell-associated virus across a monolayer of epithelial cells. A mixture of 13 MAbs directed to well-defined epitopes of the HIV-1 envelope, including F425 A1g8, did not inhibit HIV-1 transcytosis, indicating that envelope epitopes involved in neutralization are not involved in mediating HIV-1 transcytosis. When the mixture of 13 MAbs and HIV-1 was incubated with polyclonal anti-human γ chain, the transcytosis was partially inhibited, indicating that agglutination of viral particles at the apical surface of cells may be critical for HIV transcytosis inhibition by HIV-specific Abs.
Chomont2008
(neutralization)
-
A1g8: The MAb B4e8 binds to the base of the V3 loop, neutralizes multiple primary isolates and was studied for interaction with other MAbs. B4e8 enhanced binding of CD4i MAbs 4.8d, 1.7b, and A1g8 to R5X4 virus 92HT593, but only of 48d to the R5 virus 92US660, and there was only a modest impact of the combination of B4e8 and CD4i MAbs on neutralization.
Cavacini2003
(antibody interactions, co-receptor)
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A1g8: This study examined antibody interactions, binding and neutralization with a B clade R5 isolate (92US660) and R5X4 isolate (92HT593). Abs generally bound and neutralized the R5X4 isolate better than the R5 isolate. Anti-V3 MAb B4a1 increased binding of CD4i MAbs 48d, 17b and A1g8, but only A1g8 binding was increased by B4a1 to the R5 isolate. Additive effects on neutralization of the R5X4 isolate with B4a1 and CD4i MAbs was observed, presumably due to increased exposure of the CD4i binding site, but not for the R5 isolate. Anti-gp41 MAb F240 had a synergistic effect on neutralization with CD4i MAbs 48d and 17b, but not with A1g8 for the R5X4 virus.
Cavacini2002
(antibody interactions, co-receptor, variant cross-reactivity)
References
Showing 5 of
5 references.
Isolation Paper
Cavacini2003
Lisa Cavacini, Mark Duval, Leslie Song, Rebecca Sangster, Shi-hua Xiang, Joseph Sodroski, and Marshall Posner. Conformational Changes in env Oligomer Induced by an Antibody Dependent on the V3 Loop Base. AIDS, 17(5):685-689, 28 Mar 2003. PubMed ID: 12646791.
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Cavacini2002
Lisa A. Cavacini, Mark Duval, James Robinson, and Marshall R. Posner. Interactions of Human Antibodies, Epitope Exposure, Antibody Binding and Neutralization of Primary Isolate HIV-1 Virions. AIDS, 16(18):2409-2417, 6 Dec 2002. Erratum in AIDS. 2003 Aug 15;17(12):1863. PubMed ID: 12461414.
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Chomont2008
Nicolas Chomont, Hakim Hocini, Jean-Chrysostome Gody, Hicham Bouhlal, Pierre Becquart, Corinne Krief-Bouillet, Michel Kazatchkine, and Laurent Bélec. Neutralizing Monoclonal Antibodies to Human Immunodeficiency Virus Type 1 Do Not Inhibit Viral Transcytosis Through Mucosal Epithelial Cells. Virology, 370(2):246-254, 20 Jan 2008. PubMed ID: 17920650.
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Joyner2011
Amanda S. Joyner, Jordan R. Willis, James E.. Crowe, Jr., and Christopher Aiken. Maturation-Induced Cloaking of Neutralization Epitopes on HIV-1 Particles. PLoS Pathog., 7(9):e1002234, Sep 2011. PubMed ID: 21931551.
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Yu2013a
Xiaocong Yu, Mark Duval, Christopher Lewis, Melissa A. Gawron, Rijian Wang, Marshall R. Posner, and Lisa A. Cavacini. Impact of IgA Constant Domain on HIV-1 Neutralizing Function of Monoclonal Antibody F425A1g8. J. Immunol., 190(1):205-210, 1 Jan 2013. PubMed ID: 23183895.
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