The HIV-inactivating protein, cyanovirin-N, does not block gp120-mediated virus-to-cell binding

被引:29
作者
Mariner, JM
McMahon, JB
O'Keefe, BR
Nagashima, K
Boyd, MR [1 ]
机构
[1] NCI, Lab Drug Discovery Res & Dev, Dev Therapeut Program,Div Canc Treatment & Diag, Frederick Canc Res & Dev Ctr, Frederick, MD 21702 USA
[2] Frederick Canc Res & Dev Ctr, Lab Cell & Mol Struct, SAIC, Frederick, MD 21702 USA
关键词
D O I
10.1006/bbrc.1998.9060
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
Concentrations of the potent, HN(human immunodeficiency virus) inactivating protein, cyanovirin-N (CV-N), which completely inhibit HIV-1 infectivity, do not block the binding of soluble CD4-receptor (sCD4) to HIV-1 lysates nor the attachment of intact HIV-1 virions to several target T-cell lines. Furthermore, in contrast to the known disassociative effects of sCD4 on viral envelope glycoproteins, treatment of HIVRF with high concentrations of CV-N results in complete viral inactivation but without apparent shedding of gp120 or other ultrastructural changes. These results are consistent with the view that the virucidal effects of CV-N result from interference with step(s) in the fusion process subsequent to the initial binding of the virus to target cells. (C) 1998 Academic Press.
引用
收藏
页码:841 / 845
页数:5
相关论文
共 30 条
[1]   Chemokine receptors and HIV-1: An attractive pair? [J].
Bates, P .
CELL, 1996, 86 (01) :1-3
[2]  
Berger EA, 1997, AIDS, V11, pS3
[3]  
BEWLEY CA, 1998, IN RPESS NATURE STRU
[4]   Discovery of cyanovirin-N, a novel human immunodeficiency virus-inactivating protein that binds viral surface envelope glycoprotein gp120: Potential applications to microbicide development [J].
Boyd, MR ;
Gustafson, KR ;
McMahon, JB ;
Shoemaker, RH ;
OKeefe, BR ;
Mori, T ;
Gulakowski, RJ ;
Wu, L ;
Rivera, MI ;
Laurencot, CM ;
Currens, MJ ;
Cardellina, JH ;
Buckheit, RW ;
Nara, PL ;
Pannell, LK ;
Sowder, RC ;
Henderson, LE .
ANTIMICROBIAL AGENTS AND CHEMOTHERAPY, 1997, 41 (07) :1521-1530
[5]   A SEMIAUTOMATED MULTIPARAMETER APPROACH FOR ANTI-HIV DRUG SCREENING [J].
GULAKOWSKI, RJ ;
MCMAHON, JB ;
STALEY, PG ;
MORAN, RA ;
BOYD, MR .
JOURNAL OF VIROLOGICAL METHODS, 1991, 33 (1-2) :87-100
[6]   BINDING OF SOLUBLE CD4 PROTEINS TO HUMAN-IMMUNODEFICIENCY-VIRUS TYPE-1 AND INFECTED-CELLS INDUCES RELEASE OF ENVELOPE GLYCOPROTEIN-GP120 [J].
HART, TK ;
KIRSH, R ;
ELLENS, H ;
SWEET, RW ;
LAMBERT, DM ;
PETTEWAY, SR ;
LEARY, J ;
BUGELSKI, PJ .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1991, 88 (06) :2189-2193
[7]   Envelope glycoproteins from human immunodeficiency virus types 1 and 2 and simian immunodeficiency virus can use human CCR5 as a coreceptor for viral entry and make direct CD4-dependent interactions with this chemokine receptor [J].
Hill, CM ;
Deng, HK ;
Unutmaz, D ;
Kewalramani, VN ;
Bastiani, L ;
Gorny, MK ;
ZollaPazner, S ;
Littman, DR .
JOURNAL OF VIROLOGY, 1997, 71 (09) :6296-6304
[8]   MORPHOMETRIC ANALYSIS OF RECOMBINANT SOLUBLE CD4-MEDIATED RELEASE OF THE ENVELOPE GLYCOPROTEIN GP120 FROM HIV-1 [J].
KIRSH, R ;
HART, TK ;
ELLENS, H ;
MILLER, J ;
PETTEWAY, SA ;
LAMBERT, DM ;
LEARY, J ;
BUGELSKI, PJ .
AIDS RESEARCH AND HUMAN RETROVIRUSES, 1990, 6 (10) :1209-1212
[9]   Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody [J].
Kwong, PD ;
Wyatt, R ;
Robinson, J ;
Sweet, RW ;
Sodroski, J ;
Hendrickson, WA .
NATURE, 1998, 393 (6686) :648-659
[10]   Evidence for cell-surface association between fusin and the CD4-gp120 complex in human cell lines [J].
Lapham, CK ;
Ouyang, J ;
Chandrasekhar, B ;
Nguyen, NY ;
Dimitrov, DS ;
Golding, H .
SCIENCE, 1996, 274 (5287) :602-605