C-terminal domain on the outer surface of the Macrobrachium rosenbergii nodavirus capsid is required for Sf9 cell binding and internalization

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• 作者：Monsicha Somrit^a ; ¹ ; Atthaboon Watthammawut^a ; ^e ; ¹ ; Charoonroj Chotwiwatthanakun^c ; ^d ; Puey Ounjai^b ; ^f ; Wanida Suntimanawong^c ; Wattana Weerachatyanukul^a ; ^{wattana.wee@mahidol.ac.th} (Assoc. Prof.)
• 关键词：Shrimp ; Nodavirus ; Virus-host interaction ; Internalization ; VLP
• 刊名：Virus Research
• 出版年：2017
• 出版时间：2 January 2017
• 年：2017
• 卷：227
• 期：Complete
• 页码：41-48
• 全文大小：2466 K
• 卷排序：227

文摘

Enzyme hydrolysis or genetic truncation of C-terminal domain of MrNV VLP is still able to form VLP icosahedral conformation. Chymotryptic removal of a C-terminal peptide from MrNV VLP and its F344 truncated variant exhibited a drastically reduced ability to interact and internalize into Sf9 cells. C-terminal domain is not only exposed on the capsid surface, but also constitutes the central core of the viral capsid protrusion.