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Displaying record number 961

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MAb ID	1331A
HXB2 Location	gp160(503-511) DNA(7731..7757)	gp160 Epitope Map
Author Location	gp120(510-516)
Research Contact	Susan Zolla-Pazner (Zollas01@mcrcr6.med.nyu) (NYU Med. Center)
Epitope	dwVVQREKR (Discontinuous epitope)	Epitope Alignment
Ab Type	gp120 C5
Neutralizing
Species (Isotype)	human(IgG3λ)
Patient
Immunogen	HIV-1 infection
Keywords	antibody binding site, binding affinity, neutralization

Notes

Showing 10 of 10 notes.

• 1331A: 1331A bound to both SF162 wild type and SF162 mutant, carrying only the monomeric form of the Env protein, virions and transfected cells. Kimura2009 (binding affinity)
• 1331A: A significantly higher level of anti-V3 Abs (694/98D and 447-52D) and anti-C1 MAb (EH21) bound to gp120 complexed with anti-CD4bs mAbs than to gp120 alone or in complex with other non-CD4bs Abs, while no enhancement was seen with the binding of 1331A, indicating that binding of anti-CD4bs Abs to gp120 increases exposure of specific V3 and C1, but not C5, MAb epitopes. Visciano2008 (antibody binding site)
• 1331A: This Ab did not inhibit HIV-1 BaL replication in macrophages or in PHA-stimulated PBMCs. Holl2006 (neutralization)
• 1331A: scFv 4KG5 reacts with a conformational epitope. Of a panel of MAbs tested, only NAb b12 enhanced 4KG5 binding to gp120. MAbs to the V2 loop, V3 loop, V3-C4 region, and CD4BS diminished binding, while MAbs directed against C1, CD4i, C5 regions didn't impact 4KG5 binding. These results suggest that the orientation or dynamics of the V1/V2 and V3 loops restricts CD4BS access on the envelope spike, and IgG1b12 can uniquely remain unaffected. This is a C5-binding MAb that had no impact on 4KG5 binding. Zwick2003a
• 1331A: Truncation of the gp41 cytoplasmic domain of X4, R5, and X4R5 viruses forces a conformation that more closely resembles the CD4 bound state of the external Envelope, enhancing binding of CD4i MAbs 17b and 48d and of CD4BS MAbs F105, b12, and in most cases of glycosylation site dependent MAb 2G12 and the anti-gp41 MAb 246D -- in contrast, binding of the anti-V2 MAb 697D and the anti-V3 MAb 694/98D were not affected -- viruses bearing the truncation were more sensitive to neutralization by MAbs 48d, b12, and 2G12 -- the anti-C5 MAb 1331A was used to track levels of cell surface expression of the mutated proteins. EdwardsBH2002
• 1331A: Conformation-dependent anti-V3 loop Abs may be more cross-reactive, so six new V3 MAbs were generated -- the six new MAbs all bind to the tip of the V3 loop and cross-compete with the MAb 447-52D and are conformationally sensitive -- MAbs showed cross-clade binding to native, intact virions and the strength binding was highly correlated with percent neutralization using the ghost cell or PHA blast assay -- five well-characterized MAbs were used as controls: anti-V3 447-52D (anti-V3 MAb for competition and neutralization studies), 654 (anti-CD4BS used as a conformation-sensitive MAb control), 1331A (anti-C5 used as a linear binding site MAb control as binding was not diminished by treating gp120 with DTT or sodium metaperiodate to reduce disulfide bonds), and MAb 246 (anti-gp41 MAb that bound to primary isolates of all clades). Gorny2002
• 1331A: 26 HIV-1 group M isolates (clades A to H) were tested for binding to 47 MAbs, including 4 C5 MAbs, 2 bound well, 2 bound weakly -- MAb 858-D bound only 4/26, the worst of all anti-C5 MAbs tested, while MAb 1331A, which shares the same core epitope (positions 495-516), bound to 18/26. Nyambi2000
• 1331A: The Ab binding site was studied with epitope excision (protein is bound in native conformation to immobilized MAb, then digested with proteolytic enzymes) and extraction (protein is digested then allowed to react with Ab), followed by mass spectroscopy -- two non-contiguous aa in C5 were protected, E-507 and I-487, which are thought to be located on opposite sides of hydrophobic pocket involved in gp120/gp41 interaction. Hochleitner2000a
• 1331A: Core epitope dwVVQREKR maps to gp120(510-516) -- binding of panel of 21 MAbs to soluble oligomeric gp140 versus gp41 or gp120 monomers was compared -- no MAb was oligomer specific, though anti-V3 and CD4BS MAbs reacted better with the oligomer and V2 and C5 tended to favor the monomer -- C5 MAbs 858-D, 989-D and 1331A bound with a 5-10 fold preference for the monomer. Gorny2000b
• 1331A: Using a whole virion-ELISA method, 18 human MAbs were tested for their ability to bind to a panel of 9 viruses from clades A, B, D, F, G, and H -- anti-C5 Abs 670-D and 1331A bound to 3/4 B clade viruses (they don't bind to IIIB), and to subtype D MAL. Nyambi1998

References

Showing 10 of 10 references.

EdwardsBH2002 Bradley H. Edwards, Anju Bansal, Steffanie Sabbaj, Janna Bakari, Mark J. Mulligan, and Paul A. Goepfert. Magnitude of Functional CD8+ T-Cell Responses to the Gag Protein of Human Immunodeficiency Virus Type 1 Correlates Inversely with Viral Load in Plasma. J. Virol., 76(5):2298-2305, Mar 2002. PubMed ID: 11836408. Show all entries for this paper.

Gorny2000b M. K. Gorny, T. C. VanCott, C. Williams, K. Revesz, and S. Zolla-Pazner. Effects of oligomerization on the epitopes of the human immunodeficiency virus type 1 envelope glycoproteins. Virology, 267:220-8, 2000. PubMed ID: 10662617. Show all entries for this paper.

Gorny2002 Miroslaw K. Gorny, Constance Williams, Barbara Volsky, Kathy Revesz, Sandra Cohen, Victoria R. Polonis, William J. Honnen, Samuel C. Kayman, Chavdar Krachmarov, Abraham Pinter, and Susan Zolla-Pazner. Human Monoclonal Antibodies Specific for Conformation-Sensitive Epitopes of V3 Neutralize Human Immunodeficiency Virus Type 1 Primary Isolates from Various Clades. J. Virol., 76(18):9035-9045, Sep 2002. PubMed ID: 12186887. Show all entries for this paper.

Hochleitner2000a E. O. Hochleitner, M. K. Gorny, S. Zolla-Pazner, and K. B. Tomer. Mass Spectrometric Characterization of a Discontinuous Epitope of the HIV Envelope Protein HIV-gp120 Recognized by the Human Monoclonal Antibody 1331A. J. Immunol., 164:4156-4161, 2000. PubMed ID: 10754311. Show all entries for this paper.

Holl2006 Vincent Holl, Maryse Peressin, Thomas Decoville, Sylvie Schmidt, Susan Zolla-Pazner, Anne-Marie Aubertin, and Christiane Moog. Nonneutralizing Antibodies Are Able To Inhibit Human Immunodeficiency Virus Type 1 Replication in Macrophages and Immature Dendritic Cells. J. Virol., 80(12):6177-6181, Jun 2006. PubMed ID: 16731957. Show all entries for this paper.

Kimura2009 Tetsuya Kimura, Xiao-Hong Wang, Constance Williams, Susan Zolla-Pazner, and Miroslaw K. Gorny. Human Monoclonal Antibody 2909 Binds to Pseudovirions Expressing Trimers but not Monomeric HIV-1 Envelope Proteins. Hum. Antibodies, 18(1-2):35-40, 2009. PubMed ID: 19478397. Show all entries for this paper.

Nyambi1998 P. N. Nyambi, M. K. Gorny, L. Bastiani, G. van der Groen, C. Williams, and S. Zolla-Pazner. Mapping of Epitopes Exposed on Intact Human Immunodeficiency Virus Type 1 (HIV-1) Virions: A New Strategy for Studying the Immunologic Relatedness of HIV-1. J. Virol., 72:9384-9391, 1998. 18 human MAbs binding to gp120 and gp41 were tested using a novel assay to test binding to intact HIV-1 virions. The new method involves using MAbs to the host proteins incorporated into virions to bind them to ELIZA plates. Antigenic conservation in epitopes of HIV-1 in clades A, B, D, F, G, and H was studied. MAbs were selected that were directed against V2, V3, CD4bd, C5 or gp41 regions. Antibodies against V2, the CD4BS, and sp41 showed weak and sporadic reactivities, while binding strongly to gp120, suggesting these epitopes are hidden when gp120 is in its native, quaternary structure. PubMed ID: 9765494. Show all entries for this paper.

Nyambi2000 P. N. Nyambi, H. A. Mbah, S. Burda, C. Williams, M. K. Gorny, A. Nadas, and S. Zolla-Pazner. Conserved and Exposed Epitopes on Intact, Native, Primary Human Immunodeficiency Virus Type 1 Virions of Group M. J. Virol., 74:7096-7107, 2000. PubMed ID: 10888650. Show all entries for this paper.

Visciano2008 Maria Luisa Visciano, Michael Tuen, Miroslaw K. Gorny, and Catarina E. Hioe. In Vivo Alteration of Humoral Responses to HIV-1 Envelope Glycoprotein gp120 by Antibodies to the CD4-Binding Site of gp120. Virology, 372(2):409-420, 15 Mar 2008. PubMed ID: 18054978. Show all entries for this paper.

Zwick2003a Michael B. Zwick, Robert Kelleher, Richard Jensen, Aran F. Labrijn, Meng Wang, Gerald V. Quinnan, Jr., Paul W. H. I. Parren, and Dennis R. Burton. A Novel Human Antibody against Human Immunodeficiency Virus Type 1 gp120 Is V1, V2, and V3 Loop Dependent and Helps Delimit the Epitope of the Broadly Neutralizing Antibody Immunoglobulin G1 b12. J. Virol., 77(12):6965-6978, Jun 2003. PubMed ID: 12768015. Show all entries for this paper.