A highly unusual palindromic transmembrane helical hairpin formed by SARS coronavirus E protein

JOURNAL OF MOLECULAR BIOLOGY

卷:341

Article

Arbely, E ; Khattari, Z ; Brotons, G ; Akkawi, M ; Salditt, T ; Arkin, IT

关键词: membrane proteins;    SARS coronavirus;    transmembrane helices;    viral budding;   

DOI  :  10.1016/j.jmb.2004.06.044

来源: Elsevier

【 摘 要 】

The agent responsible for the recent severe acute respiratory syndrome (SARS) outbreak is a previously unidentified coronavirus. While there is a wealth of epidemiological studies, little if any molecular characterization of SARS coronavirus (SCoV) proteins has been carried out. Here we describe the molecular characterization of SCoV E protein, a critical component of the virus responsible for virion envelope morphogenesis. We conclusively show that SCoV E protein contains an unusually short, palindromic transmembrane helical hairpin around a previously unidentified pseudo-center of symmetry, a structural feature which seems to be unique to SCoV The hairpin deforms lipid bilayers by way of increasing their curvature, providing for the first time a molecular explanation of E protein's pivotal role in viral budding. The molecular understanding of this critical component of SCoV may represent the beginning of a concerted effort aimed at inhibiting its function, and consequently, viral infectivity. (C) 2004 Elsevier Ltd. All rights reserved.

【 授权许可】

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