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Journal of Virology, April 2003, p. 5026-5029, Vol. 77, No. 8
0022-538X/03/$08.00+0 DOI: 10.1128/JVI.77.8.5026-5029.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.
Human Rhinovirus 2A Proteinase Cleavage Sites in Eukaryotic Initiation Factors (eIF) 4GI and eIF4GII Are Different
Alessandra Gradi,1,
Yuri V. Svitkin,1 Wolfgang Sommergruber,2 Hiroaki Imataka,1,
Shigenobu Morino,1,
Tim Skern,3 and Nahum Sonenberg1*
Department of Biochemistry and McGill Cancer Center, McGill University, Montreal, Quebec, Canada H3G 1Y6 ,1
Department of Exploratory Research, Boehringer Ingelheim,2
Institute of Medical Biochemistry, Division of Biochemistry, Vienna Bio Center, University of Vienna, Vienna, Austria3
Received 27 August 2002/
Accepted 30 January 2003
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 2Apro cleavage site in eIF4GII in vitro as PLLNV699*GSR; this sequence lies seven amino acids C-terminal to the cleavage site previously identified in eIF4GI (LSTR681*GPP).
* Corresponding author. Mailing address: Department of Biochemistry, McGill University, 3655 Promenade Sir William Osler, Montreal, Quebec, Canada H3G 1Y6. Phone: (514) 398-7274. Fax: (514) 398-1287. E-mail:
nahum.sonenberg{at}mcgill.ca.
Present address: Institute for Animal Health, Pirbright, Surrey GU24 ONF, United Kingdom.
Present address: RIKEN Genomic Sciences Center, Tsurumi-ku, Yokohama 230-0045, Japan.
Present address: Research Center Kyoto, Soraku-gun, Kyoto 619-0216, Japan.
Journal of Virology, April 2003, p. 5026-5029, Vol. 77, No. 8
0022-538X/03/$08.00+0 DOI: 10.1128/JVI.77.8.5026-5029.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.
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