Article ID Journal Published Year Pages File Type
6142248 Virus Research 2015 11 Pages PDF
Abstract
The Paramyxovirus membrane associated proteins are composed of two integral membrane glycoproteins, HN (H, G) and F, and of a matrix protein (M) carpeting the membrane inner layer. For Sendai virus (SeV), F and M have been proposed to form a complex at the endoplasmic reticulum that further migrates to the cell periphery where it represents a nucleation site for viral assembly completion (Essaidi-Laziosi et al., 2013). HN is recruited in the assembly complex once expressed at the cell surface. In contrast to F and M, HN appears dispensable for virus particle production. However, upon F suppression, concomitant HN suppression restricts viral particle production much more severely than F suppression alone, suggesting that HN plays a role as well. In this study, we demonstrate that the transmembrane and cytoplasmic regions of F are sufficient to promote virus particle production and incorporation of a foreign protein in viral particles. We further identify in the F cytoplasmic tail the site of interaction with M. We next confirm HN participation in viral particle production and we provide genetic evidence for a participation of M in the process. We finally derive observations that may provide a mechanism by which the viral C protein participates in viral particle production by mediating HN-M interaction.
Related Topics
Life Sciences Immunology and Microbiology Virology
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