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Characterization of Sendai virus M protein mutants that can partially interfere with virus particle production

Department of Genetics and Microbiology, University of Geneva Medical School, CMU, 9 avenue de Champel, 1211 Geneva 4, Switzerland ¹

Author for correspondence: Laurent Roux.Fax +41 22 702 57 02. e-mail Laurent.Roux{at}medecine.unige.ch

Substitution of Val¹¹³ in Sendai virus (SeV) M protein generates non-functional polypeptides, characterized by their exclusion from virus particles and by their ability to interfere with virus particle production. These phenotypic traits correlate with a single-band PAGE migration profile, in contrast to wild-type M (M^wt ), which separates into two species, one of which is a phosphorylated form. The single-band migration is likely to result from a conformational change, as evidenced by the lack of maturation of a native epitope and by a particular tryptic digestion profile, and not from the phosphorylation of all M molecules, an assumption consistent with the PAGE migration feature. One of the M mutants (HA–M³⁰ , an M protein carrying Thr¹¹²Met and Val¹¹³ Glu substitutions tagged with an influenza virus haemagglutinin epitope) was characterized further in the context of SeV infection, i.e. under conditions of co-expression with M^wt. HA–M ³⁰ is shown (i) to bind mainly to membrane fractions, (ii) not to co-precipitate M^wt, as HA–M^wt does, (iii) to interfere with the binding of nucleocapsids to membranes and (iv) to accumulate in perinuclear regions, in contrast to HA-M^wt , which is also found at the cell periphery. Such mutants constitute potential tools for the identification of critical steps in paramyxovirus assembly and budding.

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