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Function, oligomerization and n-linked glycosylation of the helicoverpa armigera single nucleopolyhedrovirus envelope fusion protein

文献类型:期刊论文

作者Long, G; Westenberg, M; Wang, HL; Vlak, JM; Hut, ZH
刊名Journal of general virology
出版日期2006-04-01
卷号87页码:839-846
ISSN号0022-1317
DOI10.1099/vir.0.81592-0
通讯作者Vlak, jm(just.vlak@wur.nl)
英文摘要In the family baculoviridae, two distinct envelope fusion proteins are identified in budded virions (bvs). gp64 is the major envelope fusion protein of group i nucleopolyhedrovirus (npv) bvs. an unrelated type of envelope fusion protein, named f, is encoded by group 11 npvs. the genome of helicoverpa armigera (hear) npv, a group 11 npv of the single nucleocapsid or s type, also encodes an f-like protein: open reading frame 133 (ha133). it was demonstrated by n-terminal sequencing of the major 59 kda protein present in hearnpv bv that this protein is one of the two f subunits: f(1) (transmembrane subunit of 59 kda) and f(2) (surface subunit of 20 kda), both the result of cleavage by a proprotein convertase and disulfide-linked. the hearnpv f protein proved to be a functional analogue of gp64, as the infectivity of an acmnpv gp64-deletion mutant was rescued by the introduction of the hearnpv f gene. it was also demonstrated by chemical cross-linking that hearnpv f is present in bvs as an oligomer whereby, unlike gp64, disulfide bonds are not involved. deglycosylation assays indicated that both f, and f2 possess n-linked glycans. however, when f was made in hz2e5 cells, these glycans did not have an alpha-1-3 core fucose modification that usually occurs in insect cells. as alpha-1-3 core fucose is a major inducer of an allergic response in humans, the present observation makes the hearnpv-hz2e5 system an attractive alternative for the production of recombinant glycoproteins for therapeutic use in humans.
WOS关键词CALIFORNICA MULTICAPSID NUCLEOPOLYHEDROVIRUS ; NUCLEAR POLYHEDROSIS-VIRUS ; VIRAL MEMBRANE-FUSION ; BACULOVIRUS GP64 ; CELL-LINES ; CROSS-LINKING ; INSECT ; GENOME ; GLYCOPROTEINS ; ACTIVATION
WOS研究方向Biotechnology & Applied Microbiology ; Virology
WOS类目Biotechnology & Applied Microbiology ; Virology
语种英语
WOS记录号WOS:000236446400013
出版者SOC GENERAL MICROBIOLOGY
URI标识http://www.irgrid.ac.cn/handle/1471x/2375281
专题武汉病毒研究所
通讯作者Vlak, JM
作者单位1.Wageningen Univ, Virol Lab, NL-6709 PD Wageningen, Netherlands
2.Chinese Acad Sci, State Key Lab Virol, Key Lab Mol Virol, Wuhan 430071, Peoples R China
3.Chinese Acad Sci, Joint Lab Invertebrate Virol, Wuhan Inst Virol, Wuhan 430071, Peoples R China
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GB/T 7714
Long, G,Westenberg, M,Wang, HL,et al. Function, oligomerization and n-linked glycosylation of the helicoverpa armigera single nucleopolyhedrovirus envelope fusion protein[J]. Journal of general virology,2006,87:839-846.
APA Long, G,Westenberg, M,Wang, HL,Vlak, JM,&Hut, ZH.(2006).Function, oligomerization and n-linked glycosylation of the helicoverpa armigera single nucleopolyhedrovirus envelope fusion protein.Journal of general virology,87,839-846.
MLA Long, G,et al."Function, oligomerization and n-linked glycosylation of the helicoverpa armigera single nucleopolyhedrovirus envelope fusion protein".Journal of general virology 87(2006):839-846.

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来源:武汉病毒研究所

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