Human Rhinovirus 2A Proteinase Cleavage Sites in Eukaryotic Initiation Factors (eIF) 4GI and eIF4GII Are Different-Reference-Cited by-同舟云学术

Human Rhinovirus 2A Proteinase Cleavage Sites in Eukaryotic Initiation Factors (eIF) 4GI and eIF4GII Are Different

Published:2003-04-15 Issue:8 Volume:77 Page:5026-5029
ISSN:0022-538X
Container-title:Journal of Virology
language:en
Short-container-title:J Virol

Author:

Gradi Alessandra¹,Svitkin Yuri V.¹,Sommergruber Wolfgang²,Imataka Hiroaki¹,Morino Shigenobu¹,Skern Tim³,Sonenberg Nahum¹

Affiliation:

1. Department of Biochemistry and McGill Cancer Center, McGill University, Montreal, Quebec, Canada H3G 1Y6

2. Department of Exploratory Research, Boehringer Ingelheim

3. Institute of Medical Biochemistry, Division of Biochemistry, Vienna Bio Center, University of Vienna, Vienna, Austria

Abstract

ABSTRACT Several picornaviruses shut down host cellular protein synthesis by proteolytic cleavage of the eukaryotic initiation factor (eIF) 4GI and eIF4GII isoforms. Viral RNA translation is maintained by a cap-independent mechanism. Here, we identify the human rhinovirus 2 2A pro cleavage site in eIF4GII in vitro as PLLNV 699 *GSR; this sequence lies seven amino acids C-terminal to the cleavage site previously identified in eIF4GI (LSTR681*GPP).

Publisher

American Society for Microbiology

Subject

Virology,Insect Science,Immunology,Microbiology

Link

https://journals.asm.org/doi/pdf/10.1128/JVI.77.8.5026-5029.2003

Reference32 articles.

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