Unique characteristics of a picornavirus internal ribosome entry site from the porcine teschovirus-1 talfan.
The teschoviruses constitute a recently defined picornavirus genus. Most of the genome sequence of the porcine teschovirus-1 (PTV) Talfan and several other strains is known. We now demonstrate that initiation of protein synthesis occurs at nucleotide (nt) 412 on the PTV Talfan RNA and that nt 1 to 405 contains an internal ribosome entry site (IRES) that functions efficiently in vitro and within mammalian cells. In comparison with other picornavirus IRES elements, the PTV IRES is relatively short and lacks a significant polypyrimidine tract near the 3' end. Expression of an enterovirus 2A protease, which induces cleavage of eIF4G within the translation initiation complex eIF4F, has little effect on the PTV IRES activity within BHK cells. The PTV IRES has a unique set of properties and represents a new class of picornavirus IRES element.
Kaku
Yoshihiro
Y
Department of Infectious Diseases, National Institute of Animal Health, Tsukuba, Ibaraki 305-0856, Japan.
Chard
Louisa S
LS
Inoue
Toru
T
Belsham
Graham J
GJ
D020121:5' Untranslated Regions; D000818:Animals; D018387:Codon, Initiator / Q000737:chemistry; D006224:Cricetinae; D003546:Cysteine Endopeptidases / Q000378:metabolism; D004770:Enterovirus / Q000201:enzymology; D010849:Picornaviridae / Q000235:genetics / Q000472:pathogenicity*; D012367:RNA, Viral / Q000737:chemistry* / Q000378:metabolism; D012270:Ribosomes / Q000378:metabolism*; D013552:Swine / Q000821:virology*
D020121:5' Untranslated Regions; D018387:Codon, Initiator; D012367:RNA, Viral; D003546:Cysteine Endopeptidases