Hepatitis C virus-like particle budding: role of the core protein and importance of its Asp111.
In the absence of a hepatitis C virus (HCV) culture system, the use of a Semliki Forest virus replicon expressing genes encoding HCV structural proteins that assemble into HCV-like particles provides an opportunity to study HCV morphogenesis. Using this system, we showed that the HCV core protein constitutes the budding apparatus of the virus and that its targeting to the endoplasmic reticulum by means of the signal sequence of E1 protein is essential for budding. In addition, the aspartic acid at position 111 in the HCV core protein sequence was found to be crucial for virus assembly, demonstrating the usefulness of this system for mapping amino acids critical to HCV morphogenesis.
Blanchard
Emmanuelle
E
Laboratoire de Virologie, Faculté de Médecine et Centre Hospitalier Universitaire, 2 bis Boulevard Tonnellé, 37032 Tours, France.
Hourioux
Christophe
C
Brand
Denys
D
Ait-Goughoulte
Malika
M
Moreau
Alain
A
Trassard
Sylvie
S
Sizaret
Pierre-Yves
PY
Dubois
Frederic
F
Roingeard
Philippe
P
D000818:Animals; D001224:Aspartic Acid; D002460:Cell Line; D006224:Cricetinae; D018274:Electroporation; D016174:Hepacivirus / Q000502:physiology*; D012672:Semliki forest virus / Q000235:genetics; D014758:Viral Core Proteins / Q000737:chemistry / Q000235:genetics / Q000502:physiology*; D014771:Virion / Q000502:physiology*; D019065:Virus Assembly
D014758:Viral Core Proteins; D001224:Aspartic Acid