The deletion of residues 268-292 of E1 impairs the ability of HCV envelope proteins to induce pore formation
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- 作者：Laura Lombanaa ; Sara Ortega-Atienzaa ; 1 ; Juliá ; n Gó ; mez-Gutié ; rreza ; Belé ; n Yé ; lamosa ; Darrell L. Petersonb ; Francisco Gavilanesa ; pacog@bbm1.ucm.es" class="auth_mail" title="E-mail the corresponding author
- 关键词：HCV ; hepatitis C virus ; HCVpp ; hepatitis C virus pseudoparticles ; E2E1 ; chimeric protein containing the ectodomains of E2 and E1 HCV envelope proteins ; E2E1Δ268-292 ; chimeric protein containing the ectodomains of E2 and E1 but lacking the region 268-292 of E1 ; CCA ; convex constraint analysis ; PG ; egg yolk phosphatidylglycerol ; NBD-PE ; N-(7-nitro-2 ; 1 ; 3-benzoxadiazol-4-yl)dimyristoylphosphatidyl-ethanolamine ; Rh-PE ; N-(lissamine rhodamine B sulphonyl) diacylphosphatidyl-ethanolamine ; ANTS ; 8-amino
- 刊名：Virus Research
- 出版年：2016
- 出版时间：2 June 2016
- 年：2016
- 卷：217
- 期：Complete
- 页码：63-70
- 全文大小：1092 K
文摘
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HCV E2E1Δ268-292 chimera, lacking the E1 putative fusion peptide, has been obtained.
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The mutant chimera has the conformational features of the full length one.
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HCVpp containing deleted E1 are not able to infect Huh7 cells.
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The involvement of the region 268-292 in membrane pore formation is suggested.