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	Conserved leucines in n-terminal heptad repeat hr1 of envelope fusion protein f of group ii nucleopolyhedroviruses are important for correct processing and essential for fusogenicity
	Long, Gang1,2,3; Pan, Xiaoyu2,3; Vlak, Just M.1
刊名	Journal of virology
	2008-03-01
卷号	82期号:5页码:2437-2447
ISSN号	0022-538X
DOI	10.1128/jvi.01885-07
通讯作者	Vlak, just m.(just.vlak@wur.nl)
英文摘要	The heptad repeat (hr), a conserved structural motif of class i viral fusion proteins, is responsible for the formation of a six-helix bundle structure during the envelope fusion process. the insect baculovirus f protein is a newly found budded virus envelope fusion protein which possesses common features to class i fusion proteins, such as proteolytic cleavage and the presence of an n-terminal open fusion peptide and multiple hr domains on the transmembrane subunit f-1. similar to many vertebrate viral fusion proteins, a conserved leucine zipper motif is predicted in this hr region proximal to the fusion peptide in baculovirus f proteins. to facilitate our understanding of the functional role of this leucine zipper-like hr1 domain in baculovirus f protein synthesis, processing, and viral infectivity, key leucine residues (leu209, leu216, and leu223) were replaced by alanine (a) or arginine (r), respectively. by using autographa californica multicapsid nucleopolyhedrovirus (acmnpv) as a pseudotype expression system, we demonstrated that all mutant f proteins incorporated into budded virus, indicating that leucine substitutions did not affect intercellular trafficking of f. furin-like protease cleavage was not affected by any of the leucine substitutions; however, the disulfide bridging and n-linked glycosylation patterns were partly altered. single substitutions in hr1 showed that the three leucine residues were critical for f fusogenicity and the rescue of acmnpv infectivity. our results support the view that the leucine zipper-like hr1 domain is important to safeguard the proper folding, glycosylation, and fusogenicity of baculovirus f proteins.
WOS关键词	VIRUS TYPE-1 GP41 ; VIRAL MEMBRANE-FUSION ; CORONAVIRUS SPIKE PROTEIN ; CRYSTAL-STRUCTURE ; MULTICAPSID NUCLEOPOLYHEDROVIRUS ; INFLUENZA HEMAGGLUTININ ; MUTATIONAL ANALYSIS ; FUNCTIONAL-ANALYSIS ; STRUCTURAL BASIS ; COILED COILS
WOS研究方向	Virology
WOS类目	Virology
语种	英语
出版者	AMER SOC MICROBIOLOGY
WOS记录号	WOS:000253481000039
内容类型	期刊论文
URI标识	http://www.corc.org.cn/handle/1471x/2375518
专题	武汉病毒研究所
通讯作者	Vlak, Just M.
作者单位	1.Univ Wageningen & Res Ctr, Virol Lab, NL-6709 PD Wageningen, Netherlands 2.Chinese Acad Sci, Wuhan Inst Virol, State Key Lab Virol, Key Lab Mol Virol, Wuhan 430070, Peoples R China 3.Chinese Acad Sci, Wuhan Inst Virol, Joint Lab Invertebrate Virol, Wuhan 430070, Peoples R China
推荐引用方式 GB/T 7714	Long, Gang,Pan, Xiaoyu,Vlak, Just M.. Conserved leucines in n-terminal heptad repeat hr1 of envelope fusion protein f of group ii nucleopolyhedroviruses are important for correct processing and essential for fusogenicity[J]. Journal of virology,2008,82(5):2437-2447.
APA	Long, Gang,Pan, Xiaoyu,&Vlak, Just M..(2008).Conserved leucines in n-terminal heptad repeat hr1 of envelope fusion protein f of group ii nucleopolyhedroviruses are important for correct processing and essential for fusogenicity.Journal of virology,82(5),2437-2447.
MLA	Long, Gang,et al."Conserved leucines in n-terminal heptad repeat hr1 of envelope fusion protein f of group ii nucleopolyhedroviruses are important for correct processing and essential for fusogenicity".Journal of virology 82.5(2008):2437-2447.

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