A HETEROLOGOUS HEPARIN-BINDING DOMAIN CAN PROMOTE FUNCTIONAL ATTACHMENT OF A PSEUDORABIES VIRUS GC MUTANT TO CELL-SURFACES

被引:25
作者
FLYNN, SJ [1 ]
RYAN, P [1 ]
机构
[1] UNIV TENNESSEE, DEPT MICROBIOL & IMMUNOL, MEMPHIS, TN 38163 USA
关键词
D O I
10.1128/JVI.69.2.834-839.1995
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
The efficient attachment of pseudorabies virus to cultured cells is dependent on an electrostatic interaction between negatively charged cell surface heparan sulfate and the viral envelope glycoprotein gC. Deletion of the first one-third of gC severely impairs virus attachment, but the mutant virions are still capable of entering cells and establishing an infection via a gC-independent pathway. This region of gC contains three clusters of positively charged amino acids that exactly or nearly conform to proposed consensus motifs for heparin-binding domains (HBDs), and the loss of one or more of these potential HBDs may be responsible for the observed attachment defect. To more directly show the involvement of HBDs in pseudorabies virus attachment to cells, we replaced the first one-third of gC with a single, biochemically defined HBD from apolipoprotein B-100. On the basis of the results of attachment, penetration, and heparin competition assays, the heterologous HBD mediated heparan sulfate-dependent virus attachment, but not to fully mild-type levels. Although the intermediate phenotype is not understood, the apolipoprotein B-100 HBD may represent the smallest defined amino acid sequence that promotes functional herpesvirus attachment to cultured cells.
引用
收藏
页码:834 / 839
页数:6
相关论文
共 35 条
[1]   MOLECULAR MODELING OF PROTEIN-GLYCOSAMINOGLYCAN INTERACTIONS [J].
CARDIN, AD ;
WEINTRAUB, HJR .
ARTERIOSCLEROSIS, 1989, 9 (01) :21-32
[2]  
Chou P Y, 1978, Adv Enzymol Relat Areas Mol Biol, V47, P45
[3]   A COMPREHENSIVE SET OF SEQUENCE-ANALYSIS PROGRAMS FOR THE VAX [J].
DEVEREUX, J ;
HAEBERLI, P ;
SMITHIES, O .
NUCLEIC ACIDS RESEARCH, 1984, 12 (01) :387-395
[4]   AN AMINO-TERMINAL DELETION MUTATION OF PSEUDORABIES VIRUS GLYCOPROTEIN-GIII AFFECTS PROTEIN LOCALIZATION AND RNA ACCUMULATION [J].
ENQUIST, LW ;
KEELER, CL ;
ROBBINS, AK ;
RYAN, JP ;
WHEALY, ME .
JOURNAL OF VIROLOGY, 1988, 62 (10) :3565-3573
[5]  
FLYNN S, UNPUB
[6]   THE AMINO-TERMINAL 1/3 OF PSEUDORABIES VIRUS GLYCOPROTEIN GIII CONTAINS A FUNCTIONAL ATTACHMENT DOMAIN, BUT THIS DOMAIN IS NOT REQUIRED FOR THE EFFICIENT PENETRATION OF VERO CELLS [J].
FLYNN, SJ ;
BURGETT, BL ;
STEIN, DS ;
WILKINSON, KS ;
RYAN, P .
JOURNAL OF VIROLOGY, 1993, 67 (05) :2646-2654
[7]   HERPES-SIMPLEX VIRUS TYPE-1 ENTRY THROUGH A CASCADE OF VIRUS-CELL INTERACTIONS REQUIRES DIFFERENT ROLES OF GD AND GH IN PENETRATION [J].
FULLER, AO ;
LEE, WC .
JOURNAL OF VIROLOGY, 1992, 66 (08) :5002-5012
[8]   NEW TECHNIQUE FOR ASSAY OF INFECTIVITY OF HUMAN ADENOVIRUS 5 DNA [J].
GRAHAM, FL ;
VANDEREB, AJ .
VIROLOGY, 1973, 52 (02) :456-467
[9]   GLYCOPROTEIN-C-INDEPENDENT BINDING OF HERPES-SIMPLEX VIRUS TO CELLS REQUIRES CELL-SURFACE HEPARAN-SULFATE AND GLYCOPROTEIN-B [J].
HEROLD, BC ;
VISALLI, RJ ;
SUSMARSKI, N ;
BRANDT, CR ;
SPEAR, PG .
JOURNAL OF GENERAL VIROLOGY, 1994, 75 :1211-1222
[10]   GLYCOPROTEIN-C OF HERPES-SIMPLEX VIRUS TYPE-1 PLAYS A PRINCIPAL ROLE IN THE ADSORPTION OF VIRUS TO CELLS AND IN INFECTIVITY [J].
HEROLD, BC ;
WUDUNN, D ;
SOLTYS, N ;
SPEAR, PG .
JOURNAL OF VIROLOGY, 1991, 65 (03) :1090-1098