Localization of the HIV-1 gp120 conformational epitope recognized by virus-neutralizing monoclonal antibodies 2G12

被引:5
|
作者
Tumanova, OY [1 ]
Kuvshinov, VN
Il'ichev, AA
Nekrasov, BG
Ivanisenko, VA
Kozlov, AP
Sandakhchiev, LS
机构
[1] VECTOR State Res Ctr Virol & Biotechnol, Inst Bioengn, Koltsov 630559, Novosibirsk Reg, Russia
[2] Biomed Ctr, Inst Highly Purified Preparat, St Petersburg 197110, Russia
关键词
HIV-1; gp120; virus-neutralizing monoclonal antibody 2G12; conformational epitope; localization; phage peptide library;
D O I
10.1023/A:1019804511163
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
A phage peptide library was used to select peptides interacting with virus-neutralizing monoclonal antibodies (mAb) 2G12 which recognize a discontinuous surface epitope of HIV-1 gp120. With the published X-ray data, gp 120 regions involved in the antigenic determinant were predicted. Binding with mAb 2G12 was ascribed to Thr297, Phe383, Tyr384, Arg419, Ile240, Thr415, Leu416, Pro417, Lys421, and Trp112. Though distant in the gp 120 sequence, these residues are close in space and form the 2G12 epitope on the gp 120 surface.
引用
收藏
页码:517 / 521
页数:5
相关论文
共 50 条
  • [31] Distinct conformational states of HIV-1 gp41 are recognized by neutralizing and non-neutralizing antibodies
    Gary Frey
    Jia Chen
    Sophia Rits-Volloch
    Michael M Freeman
    Susan Zolla-Pazner
    Bing Chen
    Nature Structural & Molecular Biology, 2010, 17 : 1486 - 1491
  • [32] NEUTRALIZING ANTIBODIES TO HIV-1 IN SERONEGATIVE VOLUNTEERS IMMUNIZED WITH RECOMBINANT GP120 FROM THE MN STRAIN OF HIV-1
    BELSHE, RB
    GRAHAM, BS
    KEEFER, MC
    GORSE, GJ
    WRIGHT, P
    DOLIN, R
    MATTHEWS, T
    WEINHOLD, K
    BOLOGNESI, DP
    SPOSTO, R
    STABLEIN, DM
    TWADDELL, T
    BERMAN, PW
    GREGORY, T
    IZU, AE
    WALKER, MC
    FAST, P
    JAMA-JOURNAL OF THE AMERICAN MEDICAL ASSOCIATION, 1994, 272 (06): : 475 - 480
  • [33] Human Anti-HIV-1 gp120 Monoclonal Antibodies with Neutralizing Activity Cloned from Humanized Mice Infected with HIV-1
    Gawron, Melissa A.
    Duval, Mark
    Carbone, Claudia
    Jaiswal, Smita
    Wallace, Aaron
    Martin, Joseph C., III
    Dauphin, Ann
    Brehm, Michael A.
    Greiner, Dale L.
    Shultz, Leonard D.
    Luban, Jeremy
    Cavacini, Lisa A.
    JOURNAL OF IMMUNOLOGY, 2019, 202 (03): : 799 - 804
  • [34] Characterization of the conformational state and flexibility of HIV-1 gp120
    Pan, YP
    Ma, BY
    Keskin, O
    Nussinov, R
    BIOPHYSICAL JOURNAL, 2005, 88 (01) : 34A - 34A
  • [35] Structural Basis of HIV-1 gp120 Conformational Mobility
    Kwong, Peter D.
    Pancera, Marie
    Majeed, Shahzad
    Ban, Yih-En Andrew
    Chen, Lei
    Huang, Chihchin
    Kong, Leopold
    Kwon, Young Do
    Stuckey, Jonathan
    Zhou, Tongqing
    Robinson, James E.
    Schief, William R.
    Sodroski, Joseph
    Wyatt, Richard
    ACTA CRYSTALLOGRAPHICA A-FOUNDATION AND ADVANCES, 2009, 65 : S24 - S24
  • [36] RELATIONSHIP BETWEEN FUNCTIONAL DOMAINS OF THE HIV-1 SURFACE GLYCOPROTEIN GP120 AND NEUTRALIZING ANTIBODIES
    BRAND, D
    TRUONG, C
    BARIN, F
    M S-MEDECINE SCIENCES, 1994, 10 (04): : 417 - 424
  • [37] The carbohydrate epitope of the neutralizing anti-HIV-1 antibody 2G12
    Scanlan, CN
    Pantophlet, R
    Wormald, MR
    Saphire, EO
    Calarese, D
    Stanfield, R
    Wilson, IA
    Katinger, H
    Dwek, RA
    Burton, DR
    Rudd, PM
    GLYCOBIOLOGY AND MEDICINE, 2003, 535 : 205 - 218
  • [38] Potency of HIV-1 envelope glycoprotein gp120 antibodies to inhibit the interaction of DC-SIGN with HIV-1 gp120
    Lekkerkerker, AN
    Ludwig, IS
    van Vliet, SJ
    van Kooyk, Y
    Geijtenbeek, TBH
    VIROLOGY, 2004, 329 (02) : 465 - 476
  • [39] Characterization of CD4-induced epitopes on the HIV type 1 gp120 envelope glycoprotein recognized by neutralizing human monoclonal antibodies
    Xiang, SH
    Doka, N
    Choudhary, RK
    Sodroski, J
    Robinson, JE
    AIDS RESEARCH AND HUMAN RETROVIRUSES, 2002, 18 (16) : 1207 - 1217