Key result
Structure-based reverse genetics establishes nsp7/nsp7α as critical for equine arteritis virus RNA synthesis.
The determination of the nsp7α structure and its role in viral RNA synthesis provides a basis for future studies on arterivirus replication.
Caution against clinical translation from this equine model; leaves open nsp7 targeting for arterivirus replication studies.
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 providing little clue to its possible functions. Nevertheless, structure-based reverse genetics studies established the importance of nsp7/nsp7α for viral RNA synthesis, thus providing a basis for future studies.
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Manolaridis et al. (2011) studied Equine arteritis virus. Structure-based reverse genetics of nsp7/nsp7α was evaluated on Viral RNA synthesis. Structure-based reverse genetics studies established the importance of nsp7/nsp7α for viral RNA synthesis in equine arteritis virus.
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