Critical role of Rab11a-mediated recycling endosomes in the assembly of type I parainfluenza viruses.
Paramyxoviruses replicate in the cytoplasm of infected cells and newly synthesized viral nucleocapsids (vRNPs) are transported to the plasma membrane to be incorporated into progeny virions. In this study, we analyzed the impact of the Rab11-mediated recycling pathway in Sendai virus (SeV) and human parainfluenza virus type 1 (hPIV1) vRNP transport. We found that suppression of Rab11 expression caused vRNP aggregation in the cytoplasm and reduced progeny virion formation. Overexpression of constitutively active Rab11Q70L, but not dominant negative Rab11S25N co-localized with vRNP, showing that vRNP specifically recognizes the GTP-bound active form of Rab11. Moreover, Rab11Q70L co-localized with the dominant negative tails of all three subtypes of myosins, Va, Vb, and Vc, while SeV and hPIV1 vRNPs co-localized with only myosin Vb and Vc. These results highlight the critical role of Rab11 in vRNP trafficking, and suggest a specificity in the recycling endosomes parainfluenza viruses utilize for virus assembly.
Department of Microbiology and Immunology, University of Rochester School of Medicine and Dentistry, 601 Elmwood Avenue, Box 672 Rochester, NY 14642, USA.
Raychel
R
Stone
Department of Microbiology and Immunology, University of Rochester School of Medicine and Dentistry, 601 Elmwood Avenue, Box 672 Rochester, NY 14642, USA.
Tsuyoshi
T
Hayashi
Department of Microbiology and Immunology, University of Rochester School of Medicine and Dentistry, 601 Elmwood Avenue, Box 672 Rochester, NY 14642, USA.
Shringkhala
S
Bajimaya
Department of Microbiology and Immunology, University of Rochester School of Medicine and Dentistry, 601 Elmwood Avenue, Box 672 Rochester, NY 14642, USA.
Erin
E
Hodges
Department of Microbiology and Immunology, University of Rochester School of Medicine and Dentistry, 601 Elmwood Avenue, Box 672 Rochester, NY 14642, USA. Electronic address: toru_takimoto@urmc.rochester.edu.
Toru
T
Takimoto
D000818:Animals; D002460:Cell Line; D011992:Endosomes / Q000378:metabolism; D006367:HeLa Cells; D006801:Humans; D008253:Macaca mulatta; D024701:Myosin Type V / Q000378:metabolism*; D019251:Nucleocapsid / Q000378:metabolism; D010222:Parainfluenza Virus 1, Human / Q000235:genetics / Q000378:metabolism*; D018184:Paramyxoviridae Infections; D021381:Protein Transport / Q000235:genetics / Q000502:physiology; D034622:RNA Interference; D034741:RNA, Small Interfering; D029082:Sendai virus / Q000235:genetics / Q000378:metabolism*; D019065:Virus Assembly / Q000235:genetics*; D020691:rab GTP-Binding Proteins / Q000096:biosynthesis / Q000235:genetics*; D020695:rab4 GTP-Binding Proteins / Q000378:metabolism; D000099193:rab11 GTP-Binding Proteins
D024701:Myosin Type V; D034741:RNA, Small Interfering; D020691:rab GTP-Binding Proteins; D020695:rab4 GTP-Binding Proteins; D000099193:rab11 GTP-Binding Proteins
Myosins; Parainfluenza virus; Rab; Virus assembly