A single amino acid substitution in the measles virus F₂ protein reciprocally modulates membrane fusion activity in pathogenic and oncolytic strains

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• 作者：Sabine Heidmeier ; Jan R.H. Hanauer ; Katrin Friedrich ; Steffen Pr眉fer ; Irene C. Schneider ; Christian J. Buchholz ; Klaus Cichutek ; Michael D. M眉hlebach
• 关键词：Measles virus ; Fusion protein ; Membrane fusion ; Receptor usage
• 刊名：Virus Research
• 出版年：13 February, 2014
• 年：2014
• 卷：180
• 期：Complete
• 页码：43-48
• 全文大小：2334 K

文摘

Differences in fusion activity between measles virus (MV) attenuated, oncolytic strain MV_NSe and pathogenic MV_wt323 are reflected in amino acid 94 of the fusion (F) proteins. A valine 94 in F_NSe (naturally) or F_wt323 (introduced) correlated with enhanced cell-cell fusion activity during transient glycoprotein expression or recombinant MV infections irrespective of the strains鈥?targeted receptors, whereas the reverse effect was found for methionine 94. Enhanced fusogenicity was determined by weaker glycoprotein interaction and correlated positively with cytotoxicity in both virus strains. Amino acid 94 of F can be used to tailor fusogenicity and cytotoxicity of recombinant MV, while the cellular receptor triggering fusion is not decisive.