Analysis of human parainfluenza virus 3 receptor binding variants: Evidence for the use of a specific sialic acid-containing receptor

被引：15

作者：

Moscona, A

Peluso, RW

机构：

[1] CUNY MT SINAI SCH MED,DEPT CELL BIOL ANAT,NEW YORK,NY 10029

[2] CUNY MT SINAI SCH MED,DEPT MICROBIOL,NEW YORK,NY 10029

来源：

MICROBIAL PATHOGENESIS | 1996年 / 20卷 / 03期

关键词：

human parainfluenza virus type 3; virus receptors; haemagglutinin-neuraminidase; viral fusion; sialic acid receptors;

D O I：

10.1006/mpat.1996.0016

中图分类号：

R392 [医学免疫学]; Q939.91 [免疫学];

学科分类号：

100102 ;

摘要：

In order for the fusion protein (F) of the human parainfluenza virus type 3 (HPF3) to promote membrane fusion and viral entry, the haemagglutinin-neuraminidase (HN) glycoprotein must interact with its receptor. Sialoglycoconjugates are known to be the receptors for the HPF3 HN, however specific attachment factors or receptors for HPF3 have not been identified. In this report we describe the analysis of variants of HPF3 with increased fusion-promoting phenotypes that were selected by treatment with viral neuraminidase. The results suggest that for HPF3, the virus is specific in its use of sialic acid receptors; the majority of sialic-acid containing molecules are not targets for HPF3. (C) 1996 Academic Press Limited

引用

页码：179 / 184

页数：6

共 18 条

[1] THE RELEASE OF N-ACETYLNEURAMINIC AND N-GLYCOLLOYL-NEURAMINIC ACID FROM SOLUBLE COMPLEX CARBOHYDRATES AND ERYTHROCYTES BY BACTERIAL, VIRAL AND MAMMALIAN SIALIDASES [J].