Your browser doesn't support javascript.
loading
The C-terminal amyloidogenic peptide contributes to self-assembly of Avibirnavirus viral protease.
Zheng, Xiaojuan; Jia, Lu; Hu, Boli; Sun, Yanting; Zhang, Yina; Gao, Xiangxiang; Deng, Tingjuan; Bao, Shengjun; Xu, Li; Zhou, Jiyong.
Afiliação
  • Zheng X; Key Laboratory of Animal Virology of Ministry of Agriculture, Zhejiang University, Hangzhou 310058, PR China.
  • Jia L; State Key Laboratory and Collaborative Innovation Center for Diagnosis and Treatment of Infectious Diseases, First Affiliated Hospital, Zhejiang University, Hangzhou 310003, PR China.
  • Hu B; Key Laboratory of Animal Virology of Ministry of Agriculture, Zhejiang University, Hangzhou 310058, PR China.
  • Sun Y; College of Veterinary Medicine, Nanjing Agricultural University, Nanjing 210095, PR China.
  • Zhang Y; Key Laboratory of Animal Virology of Ministry of Agriculture, Zhejiang University, Hangzhou 310058, PR China.
  • Gao X; Key Laboratory of Animal Virology of Ministry of Agriculture, Zhejiang University, Hangzhou 310058, PR China.
  • Deng T; Key Laboratory of Animal Virology of Ministry of Agriculture, Zhejiang University, Hangzhou 310058, PR China.
  • Bao S; Key Laboratory of Animal Virology of Ministry of Agriculture, Zhejiang University, Hangzhou 310058, PR China.
  • Xu L; Key Laboratory of Animal Virology of Ministry of Agriculture, Zhejiang University, Hangzhou 310058, PR China.
  • Zhou J; Key Laboratory of Animal Virology of Ministry of Agriculture, Zhejiang University, Hangzhou 310058, PR China.
Sci Rep ; 5: 14794, 2015 Oct 06.
Artigo em Inglês | MEDLINE | ID: mdl-26440769
ABSTRACT
Unlike other viral protease, Avibirnavirus infectious bursal disease virus (IBDV)-encoded viral protease VP4 forms unusual intracellular tubule-like structures during viral infection. However, the formation mechanism and potential biological functions of intracellular VP4 tubules remain largely elusive. Here, we show that VP4 can assemble into tubules in diverse IBDV-infected cells. Dynamic analysis show that VP4 initiates the assembly at early stage of IBDV infection, and gradually assembles into larger size of fibrils within the cytoplasm and nucleus. Intracellular assembly of VP4 doesn't involve the host cytoskeleton, other IBDV-encoded viral proteins or vital subcellular organelles. Interestingly, the last C-terminal hydrophobic and amyloidogenic stretch (238)YHLAMA(243) with two "aggregation-prone" alanine residues was found to be essential for its intracellular self-assembly. The assembled VP4 fibrils show significantly low solubility, subsequently, the deposition of highly assembled VP4 structures ultimately deformed the host cytoskeleton and nucleus, which was potentially associated with IBDV lytic infection. Importantly, the assembly of VP4 significantly reduced the cytotoxicity of protease activity in host cells which potentially prevent the premature cell death and facilitate viral replication. This study provides novel insights into the formation mechanism and biological functions of the Avibirnavirus protease-related fibrils.
Assuntos

Similares

MEDLINE

...
LILACS

LIS

Texto completo: Disponível Coleções: Bases de dados internacionais Base de dados: MEDLINE Assunto principal: Proteínas Virais / Serina Endopeptidases / Proteínas Estruturais Virais / Avibirnavirus / Interações Hospedeiro-Patógeno Limite: Animais / Humanos Idioma: Inglês Revista: Sci Rep Ano de publicação: 2015 Tipo de documento: Artigo