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Displaying record number 504

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MAb ID	58.2
HXB2 Location	gp160(310-317) DNA(7152..7175)	gp160 Epitope Map
Author Location	gp120( MN)
Research Contact	Repligen Corp.
Epitope	`HIGPGRAF`	Epitope Alignment
Ab Type	gp120 V3 // V3 glycan (V3g)
Neutralizing	L
Species (Isotype)	mouse(IgG1κ)
Patient
Immunogen	vaccine
Keywords	antibody binding site, antibody generation, neutralization, review, structure, subtype comparisons, variant cross-reactivity

Vaccine Details

Vaccine type	peptide
Vaccine strain	B clade MN
Vaccine component	Env V3

Notes

Showing 12 of 12 notes.

58.2: 58.2 complexed with sCD4 and both parental and GnTI virus (complex glycans of the neutralizing face are replaced by fully trimmed oligomannose stumps). Binley2010
58.2: Data is summarized on the X-ray crystal structures resolution and NMR studies of 58.2. Sirois2007 (review, structure)
58.2: 58.2 neutralized 5 of the 15 subtype B isolates tested, of which 4 were resistant to neutralization by MAbs 19b, 39F, CO11, F2A3, F530, LA21 and LE311. Angle of interaction between 58.2 and V3 was shown by superimposing the Fab fragment of the Ab with V3. 58.2 was shown to interact with V3 from a nearly identical angle as MAb 447D. Pantophlet2008 (antibody binding site, neutralization, variant cross-reactivity, structure)
58.2: The crystal structure of V3-reactive antibody-peptide complexes were examined. 58.2 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)
58.2: This review summarizes data on crystallographic structures of 58.2 binding to its V3 peptide antigens. Stanfield2005 (antibody binding site, review, structure)
58.2: 93 viruses from different clades were tested for their neutralization cross-reactivity using a panel of HIV antibodies. 58.2 could only neutralize B subtype viruses, and seemed to have a minimal epitope of (H/T)IGPGR(A/T)(F/L). Binley2004 (variant cross-reactivity, subtype comparisons)
58.2: 58.2's epitope was noted to be IGPGRAF -- Abs against the V3 loop (50.1, 58.2, 59.1, 257-D, 268-D, 447-52D), CD4BS (IgG1b12, 559-64D, F105), CD4i (17b), and to gp41 (2F5, F240) each showed similar binding efficiency to Env derived from related pairs of primary and TCLA lines (primary: 168P and 320SI, and TCLA: 168C and 320SI-C3.3), but the TCLA lines were much more susceptible to neutralization suggesting that the change in TCLA lines that make them more susceptible to NAbs alters some step after binding. York2001
58.2: The crystal structure of Fab 58.2 bound to V3 loop peptides was obtained -- conformational changes in the tip of the V3 loop (GPGR) were observed when different MAbs were bound -- 58.2's epitope was defined as KRKRIHIGPGRAFY. Stanfield1999
58.2: Competition ELISAs with serial deletions produced longer estimates of epitope length, RIHIGPGRAFY, than Alanine substitution, suggesting significance of non-contact residues. Seligman1996
58.2: Modest cross-reactivity among B clade gp120s, little outside B clade -- core epitope as I-IHIG. Moore1994b
58.2: Did not synergistically neutralize MN in combination with MAb F105 -- there was synergistic neutralization when combined with sCD4. Potts1993
58.2: Epitope defined by peptide reactivity and changes in affinity with amino acid substitutions -- 4/7 primarily isolates were neutralized. WhiteScharf1993 (antibody generation)

References

Showing 12 of 12 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.

Binley2004 James M. Binley, Terri Wrin, Bette Korber, Michael B. Zwick, Meng Wang, Colombe Chappey, Gabriela Stiegler, Renate Kunert, Susan Zolla-Pazner, Hermann Katinger, Christos J. Petropoulos, and Dennis R. Burton. Comprehensive Cross-Clade Neutralization Analysis of a Panel of Anti-Human Immunodeficiency Virus Type 1 Monoclonal Antibodies. J. Virol., 78(23):13232-13252, Dec 2004. PubMed ID: 15542675. Show all entries for this paper.

Binley2010 James M Binley, Yih-En Andrew Ban, Emma T. Crooks, Dirk Eggink, Keiko Osawa, William R. Schief, and Rogier W. Sanders. Role of Complex Carbohydrates in Human Immunodeficiency Virus Type 1 Infection and Resistance to Antibody Neutralization. J. Virol., 84(11):5637-5655, Jun 2010. PubMed ID: 20335257. 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.

Moore1994b J. P. Moore, F. E. McCutchan, S.-W. Poon, J. Mascola, J. Liu, Y. Cao, and D. D. Ho. Exploration of Antigenic Variation in gp120 from Clades A through F of Human Immunodeficiency Virus Type 1 by Using Monoclonal Antibodies. J. Virol., 68:8350-8364, 1994. Four of five anti-V3 MAbs were slightly cross-reactive within clade B, but not very reactive outside clade B. Two discontinuous CD4 binding site Mabs appear to be pan-reactive. Anti-V2 MAbs were only sporadically reactive inside and outside of clade B. PubMed ID: 7525988. 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.

Seligman1996 S. J. Seligman, J. M. Binley, M. K. Gorny, D. R. Burton, S. Zolla-Pazner, and K. A. Sokolowski. Characterization by Serial Deletion Competition ELISAs of HIV-1 V3 Loop Epitopes Recognized by Monoclonal Antibodies. Mol. Immunol., 33:737-745, 1996. PubMed ID: 8811069. 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.

Stanfield1999 R. Stanfield, E. Cabezas, A. Satterthwait, E. Stura, A. Profy, and I. Wilson. Dual Conformations for the HIV-1 gp120 V3 Loop in Complexes with Different Neutralizing Fabs. Structure, 7:131-142, 1999. PubMed ID: 10368281. 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.

York2001 J. York, K. E. Follis, M. Trahey, P. N. Nyambi, S. Zolla-Pazner, and J. H. Nunberg. Antibody binding and neutralization of primary and T-cell line-adapted isolates of human immunodeficiency virus type 1. J. Virol., 75(6):2741--52, Mar 2001. URL: http://jvi.asm.org/cgi/content/full/75/6/2741. PubMed ID: 11222697. Show all entries for this paper.