The paramyxovirus SV5 V protein binds two atoms of zinc and is a structural component of virions.
The paramyxovirus simian virus 5 (SV5) cysteine-rich V protein has been shown to be a virus structural protein by analysis of the polypeptides of purified SV5 virions. In addition, the V protein has been identified as a component of the virus nucleocapsid core both by the analysis of the polypeptides present in radioactively labeled preparations of purified nucleocapsids and by immunoelectron microscopy. Quantitative autoradiography was used to determine that there are approximately 350 molecules of the V protein in virions. The V protein has been purified from V recombinant baculovirus-infected insect cells and by using inductively coupled argon plasma atomic emission spectroscopy it was found that each molecule of V binds two zinc atoms.
Paterson
R G
RG
Department of Biochemistry, Molecular Biology and Cell Biology, Northwestern University, Evanston, Illinois 60208-3500, USA. r-paterson@nwu.edu
Leser
G P
GP
Shaughnessy
M A
MA
Lamb
R A
RA
D000818:Animals; D002417:Cattle; D002460:Cell Line; D004285:Dogs; D016253:Microscopy, Immunoelectron; D011485:Protein Binding; D018108:Respirovirus / Q000502:physiology* / Q000648:ultrastructure; D015678:Viral Structural Proteins / Q000378:metabolism* / Q000648:ultrastructure; D014771:Virion / Q000378:metabolism* / Q000648:ultrastructure; D019065:Virus Assembly / Q000502:physiology; D015032:Zinc / Q000378:metabolism
C097019:V protein, Simian parainfluenza virus 5; D015678:Viral Structural Proteins; D015032:Zinc