中国科学院机构知识库网格
Chinese Academy of Sciences Institutional Repositories Grid
Proteomics analysis of helicoverpa armigera single nucleocapsid nucleopolyhedrovirus identified two new occlusion-derived virus-associated proteins, ha44 and ha100

文献类型:期刊论文

作者Deng, Fei; Wang, Ranran; Fang, Minggang; Jiang, Yue; Xu, Xushi; Wang, Hanzhong; Chen, Xinwen; Arif, Basil M.; Guo, Lin; Wang, Hualin
刊名Journal of virology
出版日期2007-09-01
卷号81期号:17页码:9377-9385
ISSN号0022-538X
DOI10.1128/jvi.00632-07
通讯作者Hu, zhihong(huzh@wh.iov.cn)
英文摘要Sodium dodecyl sulfate-polyacrylamide gel electrophoresis and mass spectrometry were used to analyze the structural proteins of the occlusion-derived virus (odv) of helicoverpa armigera single nucleocapsid nucleopolyhedrovirus (hearnpv), a group ii npv. twenty-three structural proteins of hearnpv odv were identified, 21 of which have been reported previously as structural proteins or odv-associated proteins in other baculoviruses. these include polyhedrin, p78/83, p49, odv-e18, odv-ec27, odv-e56, p74, lef-3, ha66 (ac66), dna polymerase, gp41, vp39, p33, odv-e25, helicase, p6.9, odv/bv-c42, vp80, odv-ec43, odv-e66, and pif-1. two proteins encoded by hearnpv orf44 (ha44) and orf100 (ha100) were discovered as odv-associated proteins for the first time. ha44 encodes a protein of 378 aa with a predicted mass of 42.8 kda. ha100 encodes a protein of 510 aa with a predicted mass of 58.1 kda and is a homologue of the gene for poly (adp- ribose) glycohydrolase (parg). western blot analysis and immunoelectron microscopy confirmed that ra44 is associated with the nucleocapsid and ha100 is associated with both the nucleocapsid and the envelope of hearnpv odv. ha44 is conserved in group h npvs and granuloviruses but does not exist in group i npvs, while ha100 is conserved only in group ii npvs.
WOS关键词NUCLEAR POLYHEDROSIS-VIRUS ; AUTOGRAPHA-CALIFORNICA NUCLEOPOLYHEDROVIRUS ; ENVELOPE FUSION PROTEIN ; MULTIPLE SEQUENCE ALIGNMENT ; PER-OS-INFECTIVITY ; OPEN READING FRAME ; STRUCTURAL PROTEIN ; POLY(ADP-RIBOSE) GLYCOHYDROLASE ; TRANSCRIPTIONAL ANALYSIS ; NUCLEOTIDE-SEQUENCE
WOS研究方向Virology
WOS类目Virology
语种英语
WOS记录号WOS:000248923700050
出版者AMER SOC MICROBIOLOGY
URI标识http://www.irgrid.ac.cn/handle/1471x/2375407
专题武汉病毒研究所
通讯作者Hu, Zhihong
作者单位1.Chinese Acad Sci, Wuhan Inst Virol, State Key Lab Virol, Wuhan 430071, Peoples R China
2.Chinese Acad Sci, Wuhan Inst Virol, Joint Lab Invertebrate Virol, Wuhan 430071, Peoples R China
3.Great Lakes Forestry Ctr, Mol Virol Lab, Sault Ste Marie, ON, Canada
4.Wuhan Univ, State Key Lab Virol, Wuhan 430072, Peoples R China
5.Coll Life Sci, Wuhan 430072, Peoples R China
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GB/T 7714
Deng, Fei,Wang, Ranran,Fang, Minggang,et al. Proteomics analysis of helicoverpa armigera single nucleocapsid nucleopolyhedrovirus identified two new occlusion-derived virus-associated proteins, ha44 and ha100[J]. Journal of virology,2007,81(17):9377-9385.
APA Deng, Fei.,Wang, Ranran.,Fang, Minggang.,Jiang, Yue.,Xu, Xushi.,...&Hu, Zhihong.(2007).Proteomics analysis of helicoverpa armigera single nucleocapsid nucleopolyhedrovirus identified two new occlusion-derived virus-associated proteins, ha44 and ha100.Journal of virology,81(17),9377-9385.
MLA Deng, Fei,et al."Proteomics analysis of helicoverpa armigera single nucleocapsid nucleopolyhedrovirus identified two new occlusion-derived virus-associated proteins, ha44 and ha100".Journal of virology 81.17(2007):9377-9385.

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来源:武汉病毒研究所

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