Sakai T, Takagi H, Muraki Y, Saito M, et al. Unique directional motility of influenza C virus controlled by its filamentous morphology and short-range motions. J Virol 2017 Nov 8
Influenza virus motility is based on cooperation between two viral spike proteins, hemagglutinin (HA) and neuraminidase (NA), and is a major determinant of virus infectivity. To translocate a virus particle on the cell surface, HA molecules exchange viral receptors and NA molecules accelerate the receptor exchange of HA. This type of virus motility was recently identified in influenza A virus (IAV). To determine if other influenza virus types have a similar receptor-exchange mechanism-driven motility, we investigated influenza C virus (ICV) motility on a receptor-fixed glass surface. This system excludes receptor mobility, which makes it more optimal than a cell surface for demonstrating virus motility by receptor-exchange. Like IAV, ICV was observed to move across the receptor-fixed surface. However, in contrast with the random movement of IAV, a filamentous ICV strain, Ann Arbor/1/50 (AA), moved straight, in a directed manner, and at a constant rate, whereas a spherical ICV strain, Taylor/1233/47 (Taylor), moved randomly, similar to IAV. The AA and Taylor viruses each moved with a combination of gradual (crawling) and rapid (gliding) motions, but the lengths of crawling and gliding for the AA virus were shorter than those of the Taylor virus. Our findings indicate that, like IAV, ICV also has a motility that is driven by the receptor-exchange mechanism. However, compared with IAV movement, filamentous ICV movement is highly regulated in both direction and speed. Control of ICV movement is based on its specific motility employing short crawling and gliding motions as well as its own filamentous morphology.IMPORTANCE Influenza virus enters into a host cell for infection via cellular endocytosis. Human influenza virus infects epithelial cells of the respiratory tract, the surfaces of which are hidden by abundant cilia that are inactive in endocytosis. An open question is the manner by which the virus migrates to endocytosis-active domains. In analyzing individual virus behaviors through single-virus tracking, we identified a novel function of the hemagglutinin and esterase of influenza C virus (ICV) as motility machinery. Hemagglutinin iteratively exchanges a viral receptor, causing virus movement. Esterase degrades the receptors along the trajectory traveled by the virus and prevents the virus from moving backward, causing directional movement. We propose that ICV has unique motile machinery directionally controlled via hemagglutinin sensing the receptor density manipulated by esterase.
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