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Integrase C-terminal residues determine the efficiency of feline foamy viral DNA integration
Kim, Jinsun,Lee, Ga-Eun,Lochelt, Martin,Shin, Cha-Gyun 3M Company 2018 Virology Vol.514 No.-
<P><B>Abstract</B></P> <P>Integrase (IN) is an essential enzyme in retroviral life cycle. It mediates viral cDNA integration into host cellular DNA. Feline foamy virus (FFV) is a member of the Spumavirus subfamily of Retroviridae. Recently, its life cycle has been proposed to be different from other retroviruses. Despite this important finding, FFV IN is not understood clearly. Here, we constructed point mutations in FFV IN C-terminal domain (CTD) to obtain a clear understanding of its integration mechanism. Mutation of the amino acid residues in FFV IN CTD interacting with target DNA reduced both IN enzymatic activities <I>in vitro</I> and viral productions in infected cells. Especially, the mutants, R307 and K340, made viral DNA integration less efficient and allowed accumulation of more unintegrated viral DNA, thereby suppressing viral replication. Therefore, we suggest that the CTD residues interacting with the target DNA play a significant role in viral DNA integration and replication.</P> <P><B>Highlights</B></P> <P> <UL> <LI> Mutation in FFV IN CTD reduced three representative enzymatic activities <I>in vitro</I>. </LI> <LI> Viruses with a mutation in CTD showed a significant reduction in viral infectivity. </LI> <LI> The mutation at R307 and K340 made viral DNA integration less efficient. </LI> <LI> The mutation at R307 and K340 leaded to accumulation of unintegrated viral DNA. </LI> </UL> </P>