Recruitment of Alix/AIP1 to the plasma membrane by Sendai virus C protein facilitates budding of virus-like particles.
Sendai virus (SeV) is unique in that one of the viral accessory proteins, C, enhances budding of virus-like particles (VLPs) formed by SeV matrix protein M by physically interacting with Alix/AIP1. C protein itself does not have the ability to form VLPs, while M protein provides viral budding force, like other enveloped viruses. Here we show that SeV C protein recruits Alix/AIP1 to the plasma membrane (PM) to facilitate VLP budding. SeV M-VLP budding is sensitive to overexpression of a dominant-negative (DN) form of VPS4A only in the presence of the C proteins, which is able to recruit Alix/AIP1 to the PM. Our results indicate that SeV M and C proteins play separate roles in the budding process: M protein drives budding and C protein enhances the efficiency of the utilization of cellular MVB sorting machinery for efficient VLP budding.
Irie
Takashi
T
Department of Virology, Graduate School of Biomedical Sciences, Hiroshima University, 1-2-3 Kasumi, Hiroshima 734-8551, Japan. tirie@hiroshima-u.ac.jp
Nagata
Natsuko
N
Yoshida
Tetsuya
T
Sakaguchi
Takemasa
T
D002135:Calcium-Binding Proteins / Q000502:physiology*; D002352:Carrier Proteins / Q000502:physiology*; D018797:Cell Cycle Proteins / Q000502:physiology*; D002462:Cell Membrane / Q000502:physiology*; D056827:Endosomal Sorting Complexes Required for Transport; D008954:Models, Biological; D029082:Sendai virus / Q000502:physiology*; D014763:Viral Matrix Proteins / Q000502:physiology; D014764:Viral Proteins / Q000502:physiology*; D014771:Virion / Q000502:physiology*
D002135:Calcium-Binding Proteins; D002352:Carrier Proteins; D018797:Cell Cycle Proteins; D056827:Endosomal Sorting Complexes Required for Transport; C097020:M protein, Sendai virus; C117020:PDCD6IP protein, human; D014763:Viral Matrix Proteins; D014764:Viral Proteins; C051221:nonstructural C protein, Sendai virus