L-domain flanking sequences are important for host interactions and efficient budding of vesicular stomatitis virus recombinants
L-domain flanking sequences are important for host interactions and efficient budding of vesicular stomatitis virus recombinants
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DOI：
10.1128/jvi.79.20.12617-12622.2005
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发表时间：
2005-10-01
影响因子：
5.4
通讯作者：
Harty, RN
中科院分区：
文献类型：
--
作者：
Irie, T;Harty, RN
水泡性口炎病毒（VSV）在基质（M）蛋白内具有PPPY和PSAP基序。PPPY基序在BHK-21细胞中具有显著的L结构域活性，而PSAP基序则没有。由于单独的核心PSAP基序不足以提供L-结构域活性，我们修饰了PSAP核心基序侧翼的上游或下游氨基酸以确定它们对L-结构域活性的影响。回收在PSAP核心侧翼的上游或下游序列中含有单个或多个氨基酸突变的VSV重组体。检查重组病毒的生长动力学、出芽效率和与宿主蛋白的功能相互作用。我们表明，L-结构域核心基序周围的氨基酸组成是有效的L-结构域的活动和与宿主蛋白质的相互作用的背景下的VSV感染的关键。
Vesicular stomatitis virus (VSV) possesses a PPPY and a PSAP motif within the matrix (M) protein. The PPPY motif has significant L-domain activity in BHK-21 cells, whereas the PSAP motif does not. Since the core PSAP motif alone is insufficient to provide L-domain activity, we modified upstream or downstream amino acids flanking the PSAP core motif to determine their effect on L-domain activity. VSV recombinants were recovered that contained single or multiple amino acid mutations in upstream or downstream sequences flanking the PSAP core. Recombinant viruses were examined for growth kinetics, budding efficiency, and functional interactions with host proteins. We demonstrate that the composition of amino acids surrounding the L-domain core motifs are critical for efficient L-domain activity and for interactions with host proteins in the context of a VSV infection.