2A PROTEINASES OF COXSACKIE-VIRUS AND RHINOVIRUS CLEAVE PEPTIDES DERIVED FROM ELF-4-GAMMA VIA A COMMON RECOGNITION MOTIF

被引：81

作者：

SOMMERGRUBER, W ^{[1
]}

AHORN, H ^{[1
]}

KLUMP, H ^{[1
]}

SEIPELT, J ^{[1
]}

ZOEPHEL, A ^{[1
]}

FESSL, F ^{[1
]}

KRYSTEK, E ^{[1
]}

BLAAS, D ^{[1
]}

KUECHLER, E ^{[1
]}

LIEBIG, HD ^{[1
]}

SKERN, T ^{[1
]}

机构：

[1] UNIV VIENNA, FAC MED, INST BIOCHEM, A-1030 VIENNA, AUSTRIA

来源：

VIROLOGY | 1994年 / 198卷 / 02期

关键词：

D O I：

10.1006/viro.1994.1089

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

The cleavage specificities of the 2A proteinases from coxsackievirus B4 (CVB4) and human rhinovirus 2 (HRV2) on oligopeptide substrates have been determined. Comparison of the specificity of CVB4 2A proteinase with that of HRV2 2A proteinase allowed clearable peptides to be designed using the common motif Ile/Leu-X-Thr-X*Gly; little resemblance to the viral cleavage site remained. The data also allowed the prediction of three possible cleavage sites for 2A proteinases on eIF-4γ; two peptides derived from these sequences were cleaved by both 2A proteinases. One of these peptides corresponds to the cleavage site for 2A proteinases mapped on eIF-4γ [B. J. Lamphear et al. (1993) J. Biol. Chem. 268, 19200-19203]. This supports the hypothesis that cleavage of eIF-4γ by picornaviral 2A proteinases occurs directly. © 1994 Academic Press. All rights reserved.

引用

页码：741 / 745

页数：5

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