标题:Mutations in the HRB linker of human parainfluenza virus type 3 fusion protein reveal its importance for fusion activity
作者:Liu, Ying; Xie, Wenyan; Chi, Miaomiao; Wen, Hongling; Zhao, Li; Song, Yanyan; Liu, Na; Chi, Lianli; Wang, Zhiyu
作者机构:[Liu, Ying; Chi, Miaomiao; Wen, Hongling; Zhao, Li; Song, Yanyan; Liu, Na; Wang, Zhiyu] Shandong Univ, Dept Virol, Sch Publ Hlth, 44 Wenhua Xi Rd, Jin 更多
通讯作者:Wang, ZY
通讯作者地址:[Wang, ZY]Shandong Univ, Dept Virol, Sch Publ Hlth, 44 Wenhua Xi Rd, Jinan 250012, Shandong, Peoples R China.
来源:VIRUS RESEARCH
出版年:2020
卷:275
DOI:10.1016/j.virusres.2019.197791
关键词:Human parainfluenza virus type 3; Fusion protein; HRB linker; Mutation; analysis fusogenicity
摘要:Human parainfluenza virus type 3 (HPIV3) fuses the viral envelope with the host cell membrane through the concerted action of the fusion (F) protein and the hemagglutinin-neuraminidase (HN). Upon HN binding to sialic acid (SA), the F protein in a metastable prefusion form is activated to undergo a series of structural rearrangements into a stable postfusion form to actuate the fusion between membranes. Various domains of F protein of some other paramyxoviruses, including HPIV3, have been reported to be differently functional. However, it is not yet clear what roles HRB linker plays. To clarify the roles that HRB linker might play in the F-mediated membrane fusion process, here we examined the effects of mutations introduced into the HRB linker of HPIV3 F protein. Six Single amino acid mutants, three chimeric mutants, and one deletion mutant were obtained and analyzed for membrane fusion activity and cell surface expression. The results showed that the membrane fusion activity of mutants changed to varying degrees in comparison with wild-type (wt) F, and some mutants even forfeited fusogenicity absolutely. It is indicated that the HRB linker domain plays an important role in the F-mediated membrane fusion process.
收录类别:SCOPUS;SCIE
资源类型:期刊论文
原文链接:https://www.scopus.com/inward/record.uri?eid=2-s2.0-85074334099&doi=10.1016%2fj.virusres.2019.197791&partnerID=40&md5=5689127248f6bf1d9ec9e590629115ca
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