The African swine fever virus nonstructural protein pB602L is required for formation of the icosahedral capsid of the virus particle.
African swine fever virus (ASFV) protein pB602L has been described as a molecular chaperone for the correct folding of the major capsid protein p72. We have studied the function of protein pB602L during the viral assembly process by using a recombinant ASFV, vB602Li, which inducibly expresses the gene coding for this protein. We show that protein pB602L is a late nonstructural protein, which, in contrast with protein p72, is excluded from the viral factory. Repression of protein pB602L synthesis inhibits the proteolytic processing of the two viral polyproteins pp220 and pp62 and leads to a decrease in the levels of protein p72 and a delocalization of the capsid protein pE120R. As shown by electron microscopy analysis of cells infected with the recombinant virus vB602Li, the viral assembly process is severely altered in the absence of protein pB602L, with the generation of aberrant "zipper-like" structures instead of icosahedral virus particles. These "zipper-like" structures are similar to those found in cells infected under restrictive conditions with the recombinant virus vA72 inducibly expressing protein p72. Immunoelectron microscopy studies show that the abnormal forms generated in the absence of protein pB602L contain the inner envelope protein p17 and the two polyproteins but lack the capsid proteins p72 and pE120R. These findings indicate that protein pB602L is essential for the assembly of the icosahedral capsid of the virus particle.
Epifano
Carolina
C
Centro de Biología Molecular Severo Ochoa (CSIC-UAM), Facultad de Ciencias, Universidad Autónoma de Madrid, Cantoblanco, 28049 Madrid, Spain.
Krijnse-Locker
Jacomine
J
Salas
María L
ML
Rodríguez
Javier M
JM
Salas
José
J
D000358:African Swine Fever Virus / Q000235:genetics / Q000502:physiology* / Q000648:ultrastructure; D000818:Animals; D015152:Blotting, Northern; D015153:Blotting, Western; D002213:Capsid / Q000502:physiology*; D002522:Chlorocebus aethiops; D017931:DNA Primers; D019084:Fluorescent Antibody Technique, Indirect; D047468:Immunoprecipitation; D016253:Microscopy, Immunoelectron; D010957:Plasmids / Q000235:genetics; D020815:Polyproteins / Q000378:metabolism; D014709:Vero Cells; D017361:Viral Nonstructural Proteins / Q000235:genetics / Q000378:metabolism* / Q000502:physiology; D019065:Virus Assembly / Q000502:physiology*
D017931:DNA Primers; D020815:Polyproteins; D017361:Viral Nonstructural Proteins