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Structure and genetic analysis of the arterivirus nonstructural protein 7alpha.


ABSTRACT: Arterivirus replicase polyproteins are cleaved into at least 13 mature nonstructural proteins (nsps), and in particular the nsp5-to-nsp8 region is subject to a complex processing cascade. The function of the largest subunit from this region, nsp7, which is further cleaved into nsp7? and nsp7?, is unknown. Using nuclear magnetic resonance (NMR) spectroscopy, we determined the solution structure of nsp7? of equine arteritis virus, revealing an interesting unique fold for this protein but thereby providing little clue to its possible functions. Nevertheless, structure-based reverse genetics studies established the importance of nsp7/nsp7? for viral RNA synthesis, thus providing a basis for future studies.

SUBMITTER: Manolaridis I 

PROVIDER: S-EPMC3126611 | biostudies-literature | 2011 Jul

REPOSITORIES: biostudies-literature

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Structure and genetic analysis of the arterivirus nonstructural protein 7alpha.

Manolaridis Ioannis I   Gaudin Cyril C   Posthuma Clara C CC   Zevenhoven-Dobbe Jessika C JC   Imbert Isabelle I   Canard Bruno B   Kelly Geoff G   Tucker Paul A PA   Conte Maria R MR   Snijder Eric J EJ  

Journal of virology 20110511 14


Arterivirus replicase polyproteins are cleaved into at least 13 mature nonstructural proteins (nsps), and in particular the nsp5-to-nsp8 region is subject to a complex processing cascade. The function of the largest subunit from this region, nsp7, which is further cleaved into nsp7α and nsp7β, is unknown. Using nuclear magnetic resonance (NMR) spectroscopy, we determined the solution structure of nsp7α of equine arteritis virus, revealing an interesting unique fold for this protein but thereby p  ...[more]

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2022-11-17 | GSE217848 | GEO