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dc.contributor.authorLin, Yizh_CN
dc.contributor.authorXu, Limei(SOA, Inst Oceanog 3, Key Lab Marine Biogenet Resources, Xiamen 361005, Peoples R China)zh_CN
dc.contributor.authorYang, Fengzh_CN
dc.contributor.author杨丰zh_CN
dc.date.accessioned2011-04-26T08:02:33Z
dc.date.available2011-04-26T08:02:33Z
dc.date.issued2010-06zh_CN
dc.identifier.citationARCHIVES OF VIROLOGY,2010,155(6):833-838zh_CN
dc.identifier.issn0304-8608zh_CN
dc.identifier.urihttp://dx.doi.org/doi:10.1007/s00705-010-0650-zzh_CN
dc.identifier.urihttps://dspace.xmu.edu.cn/handle/2288/1919
dc.description.abstractVP33, also termed VP281, VP37 or VP36B, is a minor envelope protein of white spot syndrome virus (WSSV). Because of its low abundance and lack of a transmembrane domain, we hypothesized that VP33 is likely to be attached to the viral envelope by interaction with other envelope proteins. In this study, we employed far-western blotting and pull-down assays to demonstrate that VP33 interacts with itself, as well as with VP24, which is one of the four major viral envelope proteins. Moreover, a gel-filtration analysis was performed to show that this self-interaction led to the formation of stable VP33 tetramers. These results implied that VP33 tetramers were anchored to the viral envelope through interaction with VP24, suggesting that VP33 may participate in the formation of the WSSV envelope.zh_CN
dc.description.sponsorshipNatural Science Foundation of China [3077164035]; National "863" Program of China [2006AA100312, 2006AA09Z445]zh_CN
dc.language.isoenzh_CN
dc.publisherSPRINGER WIENzh_CN
dc.titleTetramerization of white spot syndrome virus envelope protein VP33 and its interaction with VP24zh_CN
dc.typeArticlezh_CN


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