Active foamy virus proteinase is essential for virus infectivity but not for formation of a Pol polyprotein.

To analyze proteolytic processing of foamy (spuma) retroviruses, two mutations were generated in the presumed active-site triplet Asp-Ser-Gly in the predicted proteinase (PR) region of the human foamy virus (HSRV). The mutations changed either the presumed catalytic aspartic acid residue to a cataly...

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Pubblicato in:	J Virol
Autori principali:	Konvalinka, J, Löchelt, M, Zentgraf, H, Flügel, R M, Kräusslich, H G
Natura:	Artigo
Lingua:	Inglês
Pubblicazione:	American Society for Microbiology (ASM) 1995
Soggetti:	Research Article
Accesso online:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC189650/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/7474150/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/jvi.69.11.7264-7268.1995
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