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      저자 : LOMMEL, STEVEN A. (검색결과 1 건)
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      • The <i>Red clover necrotic mosaic virus</i> capsid protein N‐terminal lysine‐rich motif is a determinant of symptomatology and virion accumulation

        PARK, SANG‐,HO,SIT, TIM L.,KIM, KOOK‐,HYUNG,LOMMEL, STEVEN A. Blackwell Publishing Ltd 2012 Molecular plant pathology Vol.13 No.7

        <P><B>SUMMARY</B></P><P>The interaction between viral capsid protein (CP) and its cognate viral RNA modulates many steps in the virus infection cycle, such as replication, translation and assembly. The N‐terminal 50 amino acids of the <I>Red clover necrotic mosaic virus</I> (RCNMV) CP are rich in basic residues (especially lysine) and are essential for the core functions of the CP, namely RNA binding and virion assembly. To further elucidate additional biological roles for these basic residues, a series of alanine substitution mutations was introduced into infectious clones of RCNMV RNA‐1 and assayed for symptomatology, virion formation and systemic infection. Infectivity assays conducted in <I>Nicotiana benthamiana</I> revealed that all nine alanine substitution mutants (ASMs) were competent for systemic infection. Two ASMs (K4A and K7A/K8A) induced severe symptoms and delayed the systemic spread of viral genomes when compared with wild‐type RCNMV. However, these ASMs were still competent for virion formation. Three other ASMs (K25A, K33A and K38A) displayed milder symptoms and significant reductions in virion accumulation when compared with wild‐type RCNMV, but retained the ability to spread systemically. Evidence from these last three ASMs, as well as a CP null mutant, showed that RCNMV is able to move systemically in <I>N. benthamiana</I> as a nonvirion form. These observations reaffirm the necessity of the N‐terminal lysine‐rich residues of the RCNMV CP for efficient virion accumulation. They also reveal additional roles for the CP in the modulation of host symptomatology, independent of its role in virion assembly and the rate of systemic viral movement in <I>N. benthamiana</I>.</P>

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