In vitro assembly of the outer capsid of bovine rotavirus is calcium-dependent.
The nucleocapsid protein (VP6) and outer capsid glycoprotein (VP7) of bovine rotavirus (BRV) assemble in vitro, in 0.01 M Tris-HCl, pH 8.0, 50 mM CaCl2, into smooth particles resembling double-shelled BRV. That the two proteins interact is demonstrated by the immunoprecipitation of both by antibody directed against either VP6 or VP7. The calcium-dependence, particle morphology, and immunoreactivity in ELISA suggest that VP7 is presented authentically on the outer capsid. The implications for rotavirus morphogenesis are discussed.
Ready
K F
KF
Veterinary Infectious Disease Organization, Saskatoon, Saskatchewan, Canada.
Sabara
M I
MI
Babiuk
L A
LA
D000818:Animals; D000956:Antigens, Viral / Q000032:analysis; D015153:Blotting, Western; D002118:Calcium / Q000494:pharmacology*; D002213:Capsid / Q000096:biosynthesis* / Q000276:immunology; D002417:Cattle; D004797:Enzyme-Linked Immunosorbent Assay; D008854:Microscopy, Electron; D011233:Precipitin Tests; D012401:Rotavirus / Q000187:drug effects / Q000276:immunology / Q000648:ultrastructure*; D014758:Viral Core Proteins / Q000096:biosynthesis* / Q000276:immunology
D000956:Antigens, Viral; D014758:Viral Core Proteins; D002118:Calcium