[Paramyxovirus budding].
Our knowledge about envelope virus budding has been dramatically increased, since L-domain motifs were identified within their matrix and retroviral Gag proteins which drive virus budding. These viral proteins have been shown to interact with host cellular proteins involved in endocytosis and/or multi-vesicular body (MVB) sorting via their L-domains. Since budding of many enveloped viruses have been reported to be dependent on the activity of cellular Vps4, which catalyzes the disassembly of ESCRT machinery in the final step of protein sorting, this cellular function is believed to be utilized for efficient virus budding. However, for many enveloped viruses, L-domain motifs have not yet been identified, and the involvement of MVB sorting machinery in virus budding is still unknown. In this review, we will focus on paramyxoviruses among such viruses, and discuss their budding with the latest information.
Department of Virology, Graduate School of Biomedical Sciences, Hiroshima University, Hiroshima 734-8551, Japan. tirie@hiroshima-u.ac.jp
Takashi
T
Irie
Takemasa
T
Sakaguchi
D000818:Animals; D002462:Cell Membrane / Q000821:virology; D003593:Cytoplasm / Q000821:virology; D004705:Endocytosis; D006801:Humans; D010252:Paramyxoviridae / Q000254:growth & development / Q000502:physiology*; D017434:Protein Structure, Tertiary; D021381:Protein Transport; D014764:Viral Proteins / Q000737:chemistry / Q000502:physiology; D019065:Virus Assembly; D014779:Virus Replication
D014764:Viral Proteins