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• W2096587816 abstract "To understand the molecular determinants of measles virus (MV) cytopathicity, we have characterized mutant viruses exhibiting a more-extensive cell-to-cell fusion while maintaining efficient replication to high titers. A virus which is modified by the addition of an 8-amino-acid Flag epitope tag at the cytoplasmic tail of its H (for MV hemagglutinin) envelope glycoprotein replicates efficiently, has an increased cytopathicity, possesses a greater infectivity per particle, and has an altered protein composition compared with that of unmodified MV. The mutant phenotype is not specifically linked to the epitope sequence, since an alternatively added HA (for influenza virus-derived hemagglutinin) epitope tag caused similar effects. We demonstrate that both epitope tags weaken the interaction between the H and fusion (F) glycoproteins in virus-infected cells. This reduction in strength of H/F interaction is independent of the presence of the viral matrix (M) protein. Viruses with this less stable complex are more sensitive to neutralization by a soluble octameric form of the CD46 receptor, consistent with their increased fusogenicity. Similar analyses of glycoproteins derived from MV strains with reduced cytopathicities confirm that the strength of H and F glycoprotein interaction is a modulator of viral fusogenicity." @default.
• W2096587816 created "2016-06-24" @default.
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• W2096587816 date "2002-05-15" @default.
• W2096587816 modified "2023-09-25" @default.
• W2096587816 title "Strength of Envelope Protein Interaction Modulates Cytopathicity of Measles Virus" @default.
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• W2096587816 doi "https://doi.org/10.1128/jvi.76.10.5051-5061.2002" @default.
• W2096587816 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/136138" @default.
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