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

Autor:	Irene C. Schneider, Katrin Friedrich, Jan R.H. Hanauer, Steffen Prüfer, Sabine Heidmeier, Michael D. Mühlebach, Klaus Cichutek, Christian J. Buchholz
Rok vydání:	2014
Předmět:	chemistry.chemical_classification Cancer Research Methionine biology biology.organism_classification Molecular biology Virus Oncolytic virus Amino acid Measles virus chemistry.chemical_compound Infectious Diseases Biochemistry chemistry Valine Virology Glycoprotein Membrane Fusion Activity
Zdroj:	Virus Research. 180:43-48
ISSN:	0168-1702
Popis:	Differences in fusion activity between measles virus (MV) attenuated, oncolytic strain MVNSe and pathogenic MVwt323 are reflected in amino acid 94 of the fusion (F) proteins. A valine 94 in FNSe (naturally) or Fwt323 (introduced) correlated with enhanced cell–cell fusion activity during transient glycoprotein expression or recombinant MV infections irrespective of the strains’ 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.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::87bf6f8666d1256c051a6192d02857f7 https://doi.org/10.1016/j.virusres.2013.12.016 Zobrazit plný text záznamu Full Text from ScienceDirect