中国科学院机构知识库网格
Chinese Academy of Sciences Institutional Repositories Grid
Removal of two high-mannose n-linked glycans on gp120 renders human immunodeficiency virus 1 largely resistant to the carbohydrate-binding agent griffithsin

文献类型:期刊论文

作者Huang, Xin1,2; Jin, Wei1,2; Griffin, George E.3; Shattock, Robin J.3; Hu, Qinxue1,3
刊名Journal of general virology
出版日期2011-10-01
卷号92页码:2367-2373
ISSN号0022-1317
DOI10.1099/vir.0.033092-0
通讯作者Hu, qinxue(qhu@wh.iov.cn)
英文摘要High-mannose n-linked glycans recognized by carbohydrate-binding agents (cbas) are potential targets for topical microbicides. to better understand the mechanisms by which cbas inhibit human immunodeficiency virus (hiv)-1 infection at the molecular level, we systematically analysed the contribution of site-specific glycans to the anti-hiv activity of cbas by site-directed mutagenesis. our results demonstrate that a single deglycosylation at n295 or n448 in a range of primary and t-cell-line-adapted hiv-1 isolates resulted in marked resistance to griffithsin (grft) but maintained the sensitivity to cyanovirin (cv-n), galanthus nivalis agglutinin (gna) and a range of neutralizing antibodies. unlike cv-n and gna, the interaction between grft and gp120 appeared to be dependent on the specific trimeric 'sugar tower' including n295 and n448. this was further strengthened by the results of grft-env binding experiments. our study identifies grft-specific gp120 glycans and may provide information for the design of novel cba antiviral strategies.
WOS关键词ANTIVIRAL PROTEIN GRIFFITHSIN ; ENVELOPE GLYCOPROTEIN GP120 ; CYANOVIRIN-N ; ANTIBODY 2G12 ; ENTRY INHIBITOR ; TYPE-1 ; HIV-1 ; MICROBICIDE ; AIDS ; NEUTRALIZATION
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:000295856000016
出版者SOC GENERAL MICROBIOLOGY
URI标识http://www.irgrid.ac.cn/handle/1471x/2376024
专题武汉病毒研究所
通讯作者Hu, Qinxue
作者单位1.Chinese Acad Sci, Wuhan Inst Virol, State Key Lab Virol, Wuhan 430071, Peoples R China
2.Chinese Acad Sci, Grad Sch, Beijing 100049, Peoples R China
3.St Georges Univ London, Ctr Infect & Immun, London SW17 0RE, England
推荐引用方式
GB/T 7714
Huang, Xin,Jin, Wei,Griffin, George E.,et al. Removal of two high-mannose n-linked glycans on gp120 renders human immunodeficiency virus 1 largely resistant to the carbohydrate-binding agent griffithsin[J]. Journal of general virology,2011,92:2367-2373.
APA Huang, Xin,Jin, Wei,Griffin, George E.,Shattock, Robin J.,&Hu, Qinxue.(2011).Removal of two high-mannose n-linked glycans on gp120 renders human immunodeficiency virus 1 largely resistant to the carbohydrate-binding agent griffithsin.Journal of general virology,92,2367-2373.
MLA Huang, Xin,et al."Removal of two high-mannose n-linked glycans on gp120 renders human immunodeficiency virus 1 largely resistant to the carbohydrate-binding agent griffithsin".Journal of general virology 92(2011):2367-2373.

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来源:武汉病毒研究所

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