Evidence for the role of His-142 of protein 1C in the acid-induced disassembly of foot-and-mouth disease virus capsids.

Journal article

Foot-and-mouth disease virus (FMDV) capsids are inherently labile under mildly acidic conditions, dissociating to pentamers at pH values in the region of 6.5, with the release of protein 1A and the viral RNA. This acid-induced disassembly is thought to be required for the entry of the virus genome into the host cell. Previous work has highlighted a histidine-alpha-helix charge-dipole interaction at the twofold axes of symmetry between pentamers and has suggested that this interaction plays a ...

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Authors: Ellard, F; Drew, J; Blakemore, W; Stuart, D; King, A

• Publication status: Published
• Journal: Journal of general virology
• Volume: 80 ( Pt 8)
• Issue: 8
• Pages: 1911-1918
• Publication date: 1999-08-01
• EISSN: 1465-2099
• ISSN: 0022-1317
• Language: English
• Keywords: Cell Line; Cricetinae; Capsid Proteins; Aphthovirus; Mutagenesis, Site-Directed; Hydrogen-Ion Concentration; Histidine; Capsid; Virus Assembly; Animals