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Displaying record number 1485

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MAb ID	2601
HXB2 Location	Env	Env Epitope Map
Author Location
Epitope
Subtype	A, CRF02_AG
Ab Type	gp120 V3 // V3 glycan (V3g)
Neutralizing
Species (Isotype)	human
Patient
Immunogen	HIV-1 infection
Keywords	antibody binding site, antibody sequence, binding affinity, neutralization, structure, subtype comparisons, vaccine antigen design, variant cross-reactivity

Notes

Showing 5 of 5 notes.

2601: Two V3-scaffold immunogen constructs were designed and expressed using 3D structures of cholera toxin B (CTB), V3 in the gp120 context, and V3 bound to 447-52D MAb. The construct (V3-CTB) presenting the complete V3 was not recognized by 2601. 2601 also did not bind to the short V3-CTB construct, presenting a V3 fragment in conformation observed in complex with 447-52D. Totrov2010 (vaccine antigen design, binding affinity, structure)
2601: The Ig usage for variable heavy chain of this Ab was as follows: IGHV:3-30*02, IGHD:2-2, D-RF:2, IGHJ:4. There was a preferential usage of the VH5-51 gene segment for V3 Abs. The usage of the VH4 family for the V3 Abs was restricted to only one gene segment, VH4-59, and the VH3 gene family was used at a significantly lower level by these Abs. The V3 Abs preferentially used the JH3 and D2-15 gene segments. Gorny2009 (antibody sequence)
2601: This Ab did not neutralize SF162 but the neutralization sensitivity increased in the SF162 variant with a JR-FL V3 loop, SF162(JR-FL V3). In contrast, no neutralization was observed of the SF162(JR-FL V1/V2) and the SF162(JR-FL V1/V2/V3) variants. This Ab was shown to neutralize viruses with V3 sequences from several different subtypes (B, F, A1, H, C and CRF02_AG) except CRF01_AE. This Ab failed to neutralize SF162(JR-FL V1/V2) with V3 derived from different clades except A1, indicating effective V1/V2-mediated masking of some HIV-1 clades. The effect on the neutralization sensitivity of the residue at the crown of the V3 loop (position 18) was shown to be low for this Ab. Krachmarov2006 (neutralization, variant cross-reactivity, subtype comparisons)
2601: This MAb was derived from plasma from a patient with env clade A virus with the GPGQ V3 motif. When cross-reactivity was tested, this Ab bound to the V3subtypeA-fusion protein containing GPGQ motif and not to V3subtypeB-fusion protein containing GPGR motif. This Ab was also shown to be able to neutralize clade C psMW965 (GPGQ) but not clade B psSF162 (GPGR) virus and only one subtype B and three non-B primary isolates. Gorny2006 (neutralization, variant cross-reactivity, binding affinity, subtype comparisons)
2601: Sera from subtype A infected individuals from Cameroon have antibodies that react strongly with subtype A and subtype B V3 loops in fusion proteins, and neutralize SF162 pseudotypes, while sera from 47 subtype B infected individuals reacted only with subtype B V3s. Sera from Cameroon did not neutralize primary A or B isolates, due to indirect masking by the V1/V2 domain rather than due to loss of the target epitope. 2601 was derived from a person infected with a clade A or CRF02 virus, and binds to A but not to B V3 loops. Neutralization of JR-FL and SF162(UG V3) by anti-V3 MAbs 2557, 2558, 2601, but not subtype A primary isolates despite binding to the subtype A V3 loops, suggested masking by V1V2 blocking of neutralization by these antibodies. Krachmarov2005 (antibody binding site, variant cross-reactivity, subtype comparisons)

References

Showing 5 of 5 references.

Krachmarov2005 Chavdar Krachmarov, Abraham Pinter, William J. Honnen, Miroslaw K. Gorny, Phillipe N. Nyambi, Susan Zolla-Pazner, and Samuel C. Kayman. Antibodies That Are Cross-Reactive for Human Immunodeficiency Virus Type 1 Clade A and Clade B V3 Domains Are Common in Patient Sera from Cameroon, but Their Neutralization Activity Is Usually Restricted by Epitope Masking. J. Virol., 79(2):780-790, Jan 2005. PubMed ID: 15613306. Show all entries for this paper.

Gorny2006 Miroslaw K. Gorny, Constance Williams, Barbara Volsky, Kathy Revesz, Xiao-Hong Wang, Sherri Burda, Tetsuya Kimura, Frank A. J. Konings, Arthur Nádas, Christopher A. Anyangwe, Phillipe Nyambi, Chavdar Krachmarov, Abraham Pinter, and Susan Zolla-Pazner. Cross-Clade Neutralizing Activity of Human Anti-V3 Monoclonal Antibodies Derived from the Cells of Individuals Infected with Non-B Clades of Human Immunodeficiency Virus Type 1. J. Virol., 80(14):6865-6872, Jul 2006. PubMed ID: 16809292. Show all entries for this paper.

Krachmarov2006 C. P. Krachmarov, W. J. Honnen, S. C. Kayman, M. K. Gorny, S. Zolla-Pazner, and Abraham Pinter. Factors Determining the Breadth and Potency of Neutralization by V3-Specific Human Monoclonal Antibodies Derived from Subjects Infected with Clade A or Clade B Strains of Human Immunodeficiency Virus Type 1. J. Virol., 80(14):7127-7135, Jul 2006. PubMed ID: 16809318. Show all entries for this paper.

Gorny2009 Miroslaw K. Gorny, Xiao-Hong Wang, Constance Williams, Barbara Volsky, Kathy Revesz, Bradley Witover, Sherri Burda, Mateusz Urbanski, Phillipe Nyambi, Chavdar Krachmarov, Abraham Pinter, Susan Zolla-Pazner, and Arthur Nadas. Preferential Use of the VH5-51 Gene Segment by the Human Immune Response to Code for Antibodies against the V3 Domain of HIV-1. Mol. Immunol., 46(5):917-926, Feb 2009. PubMed ID: 18952295. Show all entries for this paper.

Totrov2010 Maxim Totrov, Xunqing Jiang, Xiang-Peng Kong, Sandra Cohen, Chavdar Krachmarov, Aidy Salomon, Constance Williams, Michael S. Seaman, Ruben Abagyan, Timothy Cardozo, Miroslaw K. Gorny, Shixia Wang, Shan Lu, Abraham Pinter, and Susan Zolla-Pazner. Structure-Guided Design and Immunological Characterization of Immunogens Presenting the HIV-1 gp120 V3 Loop on a CTB Scaffold. Virology, 405(2):513-523, 30 Sep 2010. PubMed ID: 20663531. Show all entries for this paper.