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MAb ID	2.1E (2.1e)
HXB2 Location	Env	Env Epitope Map
Author Location	gp120 (V3)
Research Contact	James Robinson
Epitope
Ab Type	gp120 V3 // V3 glycan (V3g)
Neutralizing
Species (Isotype)	human
Patient
Immunogen	HIV-1 infection
Keywords	antibody binding site, binding affinity, neutralization, subtype comparisons

Notes

Showing 3 of 3 notes.

2.1E: LANL database note: This monoclonal antibody is a CHAVI reagent (http://chavi.org/); Species: human; Category: V3 MAbs; Contact person: James Robinson
2.1e: Two different but genetically related viruses, CC101.19 and D1/85.16, which are resistant to small molecule CCR5 inhibitors, and two clones from their inhibitor sensitive parental strain CC1/85, were used to analyze interactions of HIV-1 with CCR5. CC101.19 had 4 substitutions in the V3 region and D1/85.16 had 3 changes in gp41. 2.1e bound detectably to gp120 of CC101.19 but this was greatly reduced compared to the binding of 2.1e to gp120 of the other three viruses. The opposite was true for 2.1e binding to the V3 peptide alone of the four viruses. 2.1e neutralized CC101.19 but did not neutralize the other three viruses. This indicates that the V3 region of CC101.19 has become unusually accessible to V3 Abs. Berro2009 (neutralization, binding affinity)
2.1E: To examine sequence and conformational differences between subtypes B and C, several experiments were performed with 11 MAbs regarding binding and neutralization. Both binding and neutralization studies revealed that the 11 MAbs could be divided in three different groups, and that the most differences between the subtypes were located in the stem and turn regions of V3. 2.1E belonged to the group 2 MAbs, which are able to bind subtype B but not subtype C gp120, and are able to bind both V3 peptides. 2.1E was able to bind subtype B V3 in the subtype C Env backbone chimera, but not the reverse, indicating that 2.1E binds to a structure created by the subtype B V3 sequence that is not impacted by the gp120 backbone. For subtype B, 2.1E required an R18 residue in order to bind, but the binding was not significantly affected by the H13R change. For subtype C, Q18R mutation did not restore binding to gp120, but the R13H-Q18R double mutation did. Peptide binding was affected only by the R13H mutation, indicating that the poor binding of Q18R gp120 mutant has a structural basis. 2.1E was not able to neutralize JR-FL isolate, and somewhat neutralized SF162. A chimeric SF162 variant with a JR-FL-like V3 sequence was hypersensitive to neutralization by this Ab. Patel2008 (antibody binding site, neutralization, binding affinity, subtype comparisons)

References

Showing 2 of 2 references.

Berro2009 Reem Berro, Rogier W. Sanders, Min Lu, Per J. Klasse, and John P. Moore. Two HIV-1 Variants Resistant to Small Molecule CCR5 Inhibitors Differ in How They Use CCR5 for Entry. PLoS Pathog., 5(8):e1000548, Aug 2009. PubMed ID: 19680536. Show all entries for this paper.

Patel2008 Milloni B Patel, Noah G. Hoffman, and Ronald Swanstrom. Subtype-Specific Conformational Differences within the V3 Region of Subtype B and Subtype C Human Immunodeficiency Virus Type 1 Env Proteins. J. Virol., 82(2):903-916, Jan 2008. PubMed ID: 18003735. Show all entries for this paper.