Effects of mutations on HIV-1 infectivity and neutralization involving the conserved NNNT amino acid sequence in the gp120 V3 loop

被引：5

作者：

Polzer, Svenja ^{[1
]}

Mueller, Harm ^{[1
]}

Schreiber, Michael ^{[1
]}

机构：

[1] Bernhard Nocht Inst Trop Med, Dept Virol, D-20359 Hamburg, Germany

来源：

FEBS LETTERS | 2009年 / 583卷 / 07期

关键词：

HIV; V3; loop; Neutralization; N-linked glycosylation; Viral infectivity; IMMUNODEFICIENCY-VIRUS TYPE-1; N-LINKED GLYCOSYLATION; ANTIBODY NEUTRALIZATION; ENVELOPE GLYCOPROTEIN; CCR5; GLYCAN; DOMAIN; CD4; INDIVIDUALS; RESISTANCE;

D O I：

10.1016/j.febslet.2009.03.010

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：

The N-glycan g15 within the HIV-1 gp120 V3 loop efficiently blocks antibodies to facilitate viral escape from humoral immune responses. However, we have isolated primary viruses all lacking the N-glycosylation site g15 due to mutations (NNNT > YRNA, HNTV, SIQK), which showed resistance to neutralizing antibodies present in autologous or heterologous HIV-1 positive sera. When introduced into the NL4-3 background, the sequences YRNA, HNTV and SIQK caused an increase of viral infectivity and resistance to neutralization. Thus, despite the lack of g15, primary isolates can escape from neutralization because of specific mutations of the NNNT sequence altering coreceptor usage. (C) 2009 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.

引用

页码：1201 / 1206

页数：6

共 30 条

[21] Loss of N-linked glycans in the V3-loop region of gp120 is correlated to an enhanced infectivity of HIV-1 [J].

Polzer, S ;

Dittmar, MT ;

Schmitz, H ;

Meyer, B ;

Müller, H ;

Kräusslich, HG ;

Schreiber, M .

GLYCOBIOLOGY, 2001, 11 (01) :11-19

[22] Rapid selection for an N-linked oligosaccharide by monoclonal antibodies directed against the V3 loop of human immunodeficiency virus type 1 [J].

Schonning, K ;

Jansson, B ;

Olofsson, S ;

Hansen, JES .

JOURNAL OF GENERAL VIROLOGY, 1996, 77 :753-758

[23]

Schonning Kristian, 2003, APMIS, V111, P1

[24] Loss of antibody reactivity directed against the V3 domain of certain human immunodeficiency virus type 1 variants during disease progression [J].

Schreiber, M ;

Wachsmuth, C ;

Muller, H ;

Hagen, C ;

Schmitz, H ;

vanLunzen, J .

JOURNAL OF GENERAL VIROLOGY, 1996, 77 :2403-2414

[25] Escape of HIV-1 is associated with lack of V3 domain-specific antibodies in vivo [J].

Schreiber, M ;

Muller, H ;

Wachsmuth, C ;

Laue, T ;

Hufert, FT ;

VanLaer, MD ;

Schmitz, H .

CLINICAL AND EXPERIMENTAL IMMUNOLOGY, 1997, 107 (01) :15-20

[26] ANTIBODIES OF SYMPTOMATIC HUMAN-IMMUNODEFICIENCY-VIRUS TYPE 1-INFECTED INDIVIDUALS ARE DIRECTED TO THE V3 DOMAIN OF NONINFECTIOUS AND NOT OF INFECTIOUS VIRIONS PRESENT IN AUTOLOGOUS SERUM [J].

SCHREIBER, M ;

PETERSEN, H ;

WACHSMUTH, C ;

MULLER, H ;

HUFERT, FT ;

SCHMITZ, H .

JOURNAL OF VIROLOGY, 1994, 68 (06) :3908-3916

[27] CCR5, CXCR4, and CD4 are clustered and closely apposed on microvilli of human macrophages and T cells [J].

Singer, II ;

Scott, S ;

Kawka, DW ;

Chin, J ;

Daugherty, BL ;

DeMartino, JA ;

DiSalvo, J ;

Gould, SL ;

Lineberger, JE ;

Malkowitz, L ;

Miller, MD ;

Mitnaul, L ;

Siciliano, SJ ;

Staruch, MJ ;

Williams, HR ;

Zweerink, HJ ;

Springer, MS .

JOURNAL OF VIROLOGY, 2001, 75 (08) :3779-3790

[28] Sequence variation and consensus sequence of V3 loop on HIV-1 gp120 [J].

Tian, HJ ;

Lan, CH ;

Chen, YH .

IMMUNOLOGY LETTERS, 2002, 83 (03) :231-233

[29] Antibody neutralization and escape by HIV-1 [J].

Wei, XP ;

Decker, JM ;

Wang, SY ;

Hui, HX ;

Kappes, JC ;

Wu, XY ;

Salazar-Gonzalez, JF ;

Salazar, MG ;

Kilby, JM ;

Saag, MS ;

Komarova, NL ;

Nowak, MA ;

Hahn, BH ;

Kwong, PD ;

Shaw, GM .

NATURE, 2003, 422 (6929) :307-312

[30] N-Glycans in the gp120 V1N2 domain of the HIV-1 strain NL4-3 are indispensable for viral infectivity and resistance against antibody neutralization [J].

Wolk, Tobias ;

Schreiber, Michael .

MEDICAL MICROBIOLOGY AND IMMUNOLOGY, 2006, 195 (03) :165-172

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