Heparin-like structures on respiratory syncytial virus are involved in its infectivity in vitro

被引:64
作者
Bourgeois, C
Bour, JB
Lidholt, K
Gauthray, C
Pothier, P
机构
[1] Fac Med Dijon, Lab Microbiol Med & Mol, F-21033 Dijon, France
[2] Univ Uppsala, Ctr Biomed, Dept Med & Physiol Chem, S-75123 Uppsala, Sweden
关键词
D O I
10.1128/JVI.72.9.7221-7227.1998
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Addition of heparin to the virus culture inhibited syncytial plaque formation due to respiratory syncytial virus (RSV), Moreover, pretreatment of the virus,vith heparinase or an inhibitor of heparin, protamine, greatly reduced virus infectivity, Two anti-heparan sulfate antibodies stained RSV-infected cells, but not noninfected cells, by immunofluorescence, One of the antibodies was capable of neutralizing RSV infection in vitro. These results prove that heparin-like structures identified on RSV play a major role in early stages of infection. The RSV G protein is the attachment protein. Both anti-heparan sulfate antibodies specifically bound to this protein. Enzymatic digestion of polysaccharides in the G protein reduced the binding, which indicates that heparin-like structures are on the G protein. Such oligosaccharides may therefore participate in the attachment of the virus.
引用
收藏
页码:7221 / 7227
页数:7
相关论文
共 36 条
[1]   POLYLACTOSAMINOGLYCAN MODIFICATION OF THE RESPIRATORY SYNCYTIAL VIRUS SMALL HYDROPHOBIC (SH) PROTEIN - A CONSERVED FEATURE AMONG HUMAN AND BOVINE RESPIRATORY SYNCYTIAL VIRUSES [J].
ANDERSON, K ;
KING, AMQ ;
LERCH, RA ;
WERTZ, GW .
VIROLOGY, 1992, 191 (01) :417-430
[2]   CELLULAR MUCINS - TARGETS FOR IMMUNOTHERAPY [J].
APOSTOLOPOULOS, V ;
MCKENZIE, IFC .
CRITICAL REVIEWS IN IMMUNOLOGY, 1994, 14 (3-4) :293-309
[3]   USE OF SYNTHETIC PEPTIDES TO LOCATE NEUTRALIZING ANTIGENIC DOMAINS ON THE FUSION PROTEIN OF RESPIRATORY SYNCYTIAL VIRUS [J].
BOURGEOIS, C ;
CORVAISIER, C ;
BOUR, JB ;
KOHLI, E ;
POTHIER, P .
JOURNAL OF GENERAL VIROLOGY, 1991, 72 :1051-1058
[4]   Recombinant respiratory syncytial virus from which the entire SH gene has been deleted grows efficiently in cell culture and exhibits site-specific attenuation in the respiratory tract of the mouse [J].
Bukreyev, A ;
Whitehead, SS ;
Murphy, BR ;
Collins, PL .
JOURNAL OF VIROLOGY, 1997, 71 (12) :8973-8982
[5]  
CHOPPIN PW, 1980, REV INFECT DIS, V2, P40
[6]   NUCLEOTIDE-SEQUENCE OF THE GENE ENCODING THE FUSION (F) GLYCOPROTEIN OF HUMAN RESPIRATORY SYNCYTIAL VIRUS [J].
COLLINS, PL ;
HUANG, YT ;
WERTZ, GW .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA-BIOLOGICAL SCIENCES, 1984, 81 (24) :7683-7687
[7]   OLIGOMERIZATION AND POSTTRANSLATIONAL PROCESSING OF GLYCOPROTEIN-G OF HUMAN RESPIRATORY SYNCYTIAL VIRUS - ALTERED O-GLYCOSYLATION IN THE PRESENCE OF BREFELDIN-A [J].
COLLINS, PL ;
MOTTET, G .
JOURNAL OF GENERAL VIROLOGY, 1992, 73 :849-863
[8]   POSTTRANSLATIONAL PROCESSING AND OLIGOMERIZATION OF THE FUSION GLYCOPROTEIN OF HUMAN RESPIRATORY SYNCYTIAL VIRUS [J].
COLLINS, PL ;
MOTTET, G .
JOURNAL OF GENERAL VIROLOGY, 1991, 72 :3095-3101
[9]   SPECIFICITY STUDIES ON THE HEPARIN LYASES FROM FLAVOBACTERIUM-HEPARINUM [J].
DESAI, UR ;
WANG, HM ;
LINHARDT, RJ .
BIOCHEMISTRY, 1993, 32 (32) :8140-8145
[10]  
GARCIABARRENO B, 1989, J VIROL, V63, P925