Identification of a dynein interacting domain in the papillomavirus minor capsid protein L2
Identification of a dynein interacting domain in the papillomavirus minor capsid protein L2
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DOI：
10.1128/jvi.00057-06
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发表时间：
2006-07-01
影响因子：
5.4
通讯作者：
Sapp, Martin
中科院分区：
文献类型：
--
作者：
Florin, Luise;Becker, Katrin A.;Sapp, Martin
乳头瘤病毒通过内吞作用进入细胞（H. C. Selinka等人，Virology 299：279-287，2002）。从内体排出后，次要衣壳蛋白L2伴随病毒DNA进入细胞核，随后进入亚核早幼粒细胞白血病蛋白体（P.M. Day等人，Proc. Natl. Acad. Sci. USA 101：14252-14257，2004），表明该蛋白质可能参与病毒基因组的胞质内转运。我们现在证明，L2蛋白能够通过马达蛋白动力蛋白与微管网络相互作用。L2蛋白被发现附着在微管后，进入人乳头瘤病毒假病毒粒子的涂层。基于免疫荧光和免疫共沉淀分析，与动力蛋白相互作用的L2区被映射到C-末端40个氨基酸。该区域内的突变废除L2/动力蛋白相互作用强烈降低假病毒的感染性，表明这种相互作用介导负端定向运输的病毒基因组沿着微管向细胞核。
Papillomaviruses enter cells via endocytosis (H. C. Selinka et al., Virology 299:279-287, 2002). After egress from endosomes, the minor capsid protein L2 accompanies the viral DNA to the nucleus and subsequently to the subnuclear promyelocytic leukemia protein bodies (P. M. Day et al., Proc. Natl. Acad. Sci. USA 101:14252-14257, 2004), suggesting that this protein may be involved in the intracytoplasmic transport of the viral genome. We now demonstrate that the L2 protein is able to interact with the microtubule network via the motor protein dynein. L2 protein was found attached to microtubules after uncoating of incoming human papillomavirus pseudovirions. Based on immunofluorescence and coimmunoprecipitation analyses, the L2 region interacting with dynein is mapped to the C-terminal 40 amino acids. Mutations within this region abrogating the L2/dynein interaction strongly reduce the infectivity of pseudoviruses, indicating that this interaction mediates the minus-end-directed transport of the viral genome along microtubules towards the nucleus.