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
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出版日期 | 2011-10-01 |
卷号 | 92页码:2367-2373 |
ISSN号 | 0022-1317 |
DOI | 10.1099/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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