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- W2035138045 startingPage "3576" @default.
- W2035138045 abstract "In polarized epithelial cells measles virus (MV) is predominantly released at the apical cell surface, irrespective of the sorting of its two envelope glycoproteins F and H. It has been reported previously that the viral matrix (M) protein modulates the fusogenic capacity of the viral envelope glycoproteins. Here, extant MV mutants and chimeras were used to determine the role of M protein in the transport of viral glycoproteins and release of progeny virions in polarized epithelial CaCo2 cells. In the absence of M, envelope glycoproteins are sorted to the basolateral surface, suggesting that they possess intrinsic basolateral sorting signals. However, interactions of M with the glycoprotein cytoplasmic tails allow M-glycoprotein co-segregation to the apical surface, suggesting a vectorial function of M to retarget the glycoproteins for apical virion release. Whereas this may allow virus airway shedding, the intrinsic sorting of the glycoproteins to the basolateral surface may account for systemic host infection by allowing efficient cell-cell fusion." @default.
- W2035138045 created "2016-06-24" @default.
- W2035138045 creator A5001086890 @default.
- W2035138045 creator A5062353668 @default.
- W2035138045 creator A5064342193 @default.
- W2035138045 date "2000-07-17" @default.
- W2035138045 modified "2023-10-16" @default.
- W2035138045 title "Measles virus matrix protein specifies apical virus release and glycoprotein sorting in epithelial cells" @default.
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- W2035138045 doi "https://doi.org/10.1093/emboj/19.14.3576" @default.
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