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MAb ID	83.1 (MAb 83.1)
HXB2 Location	gp160(309-315) DNA(7149..7169)	gp160 Epitope Map
Author Location	gp120( SF2)
Research Contact	Mary White-Scharf, Repligen Corporation, Cambridge, MA
Epitope	IYIGPGR	Epitope Alignment
Ab Type	gp120 V3 // V3 glycan (V3g)
Neutralizing	L
Species (Isotype)	mouse(IgG1)
Patient
Immunogen	vaccine
Keywords	antibody binding site, antibody generation, review, structure

Vaccine Details

Notes

Showing 9 of 9 notes.

• 83.1: Data is summarized on the X-ray crystal structures resolution and NMR studies of 83.1. Sirois2007 (review, structure)
• 83.1: Angle of interaction between 83.1 and V3 was shown by superimposing the Fab fragment of the Ab with V3. Pantophlet2008 (antibody binding site, structure)
• 83.1: The crystal structure of V3-reactive antibody-peptide complexes were examined. 83.1 completely surrounded V3, suggesting a high degree of accessibility for generating an immune response. Accessibility of V3 to this MAb is shown in a 3D figure. Huang2005 (antibody binding site, structure)
• 83.1: This review summarizes data on crystallographic structures of 83.1 binding to its V3 peptide antigens. Conformation of the V3 peptide bound to 83.1 is very similar to its conformation when bound to 447-52D. Stanfield2005 (antibody binding site, review, structure)
• 83.1: The MAbs with the broadest neutralizing activity, IgG1b12, 2G12 and 2F5, all have high affinity for the native trimer, indicating that they were raised in an immune response to the oligomer on the virion surface rather than dissociated subunits -- a disulfide linked gp120-gp41 (SOS gp140) was created to mimic the native conformation of Env and explore its potential as an immunogen -- SOS gp140 is recognized by NAbs IgG1b12, 2G12, and CD4-IgG2, and also by anti-V3 MAbs 19b and 83.1 -- SOSgp140 is not recognized by C4 region MAbs that neutralize only TCLA strains, G3-42 and G3-519 -- nor did it bind C11, 23A, and M90, MAbs that bind to gp120 C1 and C5, where it interacts with gp41 -- MAbs that bind CD4 inducible epitopes, 17b and A32 were very strongly induced by CD4 in SOS gp140 -- anti-gp41 MAbs that bind in the region that interacts with gp120, 7B2, 2.2B, T4, T15G1 and 4D4, did not bind to SOSgp140, in contrast to 2F5, which binds to the only gp41 epitope that is well exposed in native gp120-gp41 complexes. Binley2000
• 83.1: 19 day old mice injected with 83.1 have a shift in IgG1 response away from the V3 loop upon vaccination, without decreasing the total IgG anti-gp120 response, suggesting that prior treatment with a MAb can mask immunogenic sites and shift the immune response to vaccination. Keller1999
• 83.1: Maternally transferred anti-V3 loop MAb selectively inhibits the anti-V3 loop Ab component of the IgG response to rgp120 SF2 in 21 day old BALBc mice. Jelonek1996
• 83.1: Study of synergism of neutralization and binding comparing F105 and sCD4 with the V3 MAbs: 50.1, 59.1, 83.1, and 58.2 -- synergy was observed, and the data suggest that binding of one ligand (F105) can increase the binding of the second (e. g. V3 loop MAbs) due to conformational changes. Potts1993
• 83.1: Neutralizes SF2. WhiteScharf1993 (antibody generation)

References

Showing 9 of 9 references.

Isolation Paper
WhiteScharf1993 M. E. White-Scharf, B. J. Potts, L. M. Smith, K. A. Sokolowski, J. R. Rusche, and S. Silver. Broadly Neutralizing Monoclonal Antibodies to the V3 Region of HIV-1 Can Be Elicited by Peptide Immunization. Virology, 192:197-206, 1993. Using a V3 loop peptide as immunogen, a panel of 50 anti-V3 neutralizing monoclonal antibodies were generated. Four of them were characterized in detail in this paper. PubMed ID: 7685962. Show all entries for this paper.

Binley2000 J. Binley, R. Sanders, B. Clas, N. Schuelke, A. Master, Y. Guo, F. Kajumo, D. Anselma, P. Maddon, W. Olson, and J. Moore. A Recombinant Human Immunodeficiency virus type 1 envelope glycoprotein complex stabilized by an intramolecular disulfide bond between the gp120 and gp41 subunits is an antigenic mimic of the trimeric virion associated structure. J. Virol., 74:627-43, 1999. PubMed ID: 10623724. Show all entries for this paper.

Huang2005 Chih-chin Huang, Min Tang, Mei-Yun Zhang, Shahzad Majeed, Elizabeth Montabana, Robyn L. Stanfield, Dimiter S. Dimitrov, Bette Korber, Joseph Sodroski, Ian A. Wilson, Richard Wyatt, and Peter D. Kwong. Structure of a V3-Containing HIV-1 gp120 Core. Science, 310(5750):1025-1028, 11 Nov 2005. PubMed ID: 16284180. Show all entries for this paper.

Jelonek1996 M. Jelonek, J. Maskrey, K. Steimer, B. Potts, K. Higgins, and M. Kellor. Maternal Monoclonal Antibody to the V3 Loop Alters Specificity of the Response to a Human Immunodeficiency Virus Vaccine. J. Infect. Dis., 174:866-869, 1999. PubMed ID: 8843232. Show all entries for this paper.

Keller1999 M. Keller and Y. Arora. Inhibition of Anti-V3 Loop Response to a Recombinant gp120 SF2 Vaccine Be Preexisting Monoclonal Ab. AIDS Res. Hum. Retroviruses, 15:855-860, 1999. PubMed ID: 10381174. Show all entries for this paper.

Pantophlet2008 Ralph Pantophlet, Terri Wrin, Lisa A. Cavacini, James E. Robinson, and Dennis R. Burton. Neutralizing Activity of Antibodies to the V3 Loop Region of HIV-1 gp120 Relative to Their Epitope Fine Specificity. Virology, 381(2):251-260, 25 Nov 2008. PubMed ID: 18822440. Show all entries for this paper.

Potts1993 B. J. Potts, K. G. Field, Y. Wu, M. Posner, L. Cavacini, and M. White-Scharf. Synergistic Inhibition of HIV-1 by CD4 Binding Domain Reagents and V3-Directed Monoclonal Antibodies. Virology, 197:415-419, 1993. Four anti-V3 loop MAbs, (59.1, 83.1, 50.1, and 58.2), were evaluated for their affinity, neutralization potencies, and their ability to synergize F105 or sCD4 neutralization. The most important parameter for synergy was the capacity to neutralize a given virus independently. PubMed ID: 8212576. Show all entries for this paper.

Sirois2007 Suzanne Sirois, Mohamed Touaibia, Kuo-Chen Chou, and Rene Roy. Glycosylation of HIV-1 gp120 V3 Loop: Towards the Rational Design of a Synthetic Carbohydrate Vaccine. Curr. Med. Chem., 14(30):3232-3242, 2007. PubMed ID: 18220757. Show all entries for this paper.

Stanfield2005 Robyn L. Stanfield and Ian A. Wilson. Structural Studies of Human HIV-1 V3 Antibodies. Hum Antibodies, 14(3-4):73-80, 2005. PubMed ID: 16720977. Show all entries for this paper.