Paramyxovirus matrix (M) proteins organize virus assembly, functioning as adapters that link together viral ribonucleoprotein complexes and viral glycoproteins at infected cell plasma membranes. M proteins may also function to recruit and manipulate host factors to assist virus budding, similar to retroviral Gag proteins. By yeast two-hybrid screening, angiomotin-like 1 (AmotL1) was identified as a host factor that interacts with the M protein of parainfluenza virus 5 (PIV5). AmotL1-M protein interaction was observed in yeast, in transfected mammalian cells, and in virus-infected cells. Binding was mapped to a 83-amino acid region derived from the C-terminal portion of AmotL1. Overexpression of M-binding AmotL1-derived polypeptides potently inhibited production of PIV5 VLPs and impaired virus budding. Expression of these polypeptides moderately inhibited production of mumps VLPs, but had no effect on production of Nipah VLPs. siRNA-mediated depletion of AmotL1 protein reduced PIV5 budding, suggesting that this interaction is beneficial to paramyxovirus infection.
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