TRUNCATION OF THE CARBOXY-TERMINAL 28 AMINO-ACIDS OF GLYCOPROTEIN-B SPECIFIED BY HERPES-SIMPLEX VIRUS TYPE-1 MUTANT AMB1511-7 CAUSES EXTENSIVE CELL-FUSION

被引：70

作者：

BAGHIAN, A ^{[1
]}

HUANG, L ^{[1
]}

NEWMAN, S ^{[1
]}

JAYACHANDRA, S ^{[1
]}

KOUSOULAS, KG ^{[1
]}

机构：

[1] LOUISIANA STATE UNIV, SCH VET MED, DEPT VET MICROBIOL & PARASITOL, BATON ROUGE, LA 70803 USA

来源：

JOURNAL OF VIROLOGY | 1993年 / 67卷 / 04期

关键词：

D O I：

10.1128/JVI.67.4.2396-2401.1993

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

Three amber mutations were introduced proximal to the syn3 locus of the herpes simplex virus type 1 glycoprotein B (gB) gene specifying gB derivatives lacking the carboxy-terminal 28, 49, or 64 amino acids. A complementation system that utilized gBs expressed in COS cells to complement gB-null virus KDELTAT was established. The 49- or 64-amino-acid-truncated gBs failed to complement gB-null virus KDELTAT, while the 28-amino-acid-truncated gB complemented KDELTAT efficiently. Mutant herpes simplex virus type 1 KOS (amb1511-7) specifying the 28-amino-acid-truncated gB fused Vero cells extensively.

引用

页码：2396 / 2401

页数：6

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