Generation of filamentous instead of icosahedral particles by repression of African swine fever virus structural protein pB438L.
The mechanisms involved in the construction of the icosahedral capsid of the African swine fever virus (ASFV) particle are not well understood at present. Capsid formation requires protein p72, the major capsid component, but other viral proteins are likely to play also a role in this process. We have examined the function of the ASFV structural protein pB438L, encoded by gene B438L, in virus morphogenesis. We show that protein pB438L associates with membranes during the infection, behaving as an integral membrane protein. Using a recombinant ASFV that inducibly expresses protein pB438L, we have determined that this structural protein is essential for the formation of infectious virus particles. In the absence of the protein, the virus assembly sites contain, instead of icosahedral particles, large aberrant tubular structures of viral origin as well as bilobulate forms that present morphological similarities with the tubules. The filamentous particles, which possess an aberrant core shell domain and an inner envelope, are covered by a capsid-like layer that, although containing the major capsid protein p72, does not acquire icosahedral morphology. This capsid, however, is to some extent functional, as the filamentous particles can move from the virus assembly sites to the plasma membrane and exit the cell by budding. The finding that, in the absence of protein pB438L, the viral particles formed have a tubular structure in which the icosahedral symmetry is lost supports a role for this protein in the construction or stabilization of the icosahedral vertices 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
Salas
José
J
Rodríguez
Javier M
JM
D000358:African Swine Fever Virus / Q000235:genetics* / Q000502:physiology / Q000648:ultrastructure; D000818:Animals; D002213:Capsid / Q000737:chemistry / Q000378:metabolism; D002522:Chlorocebus aethiops; D003673:Defective Viruses / Q000502:physiology*; D015967:Gene Expression Regulation, Viral; D020868:Gene Silencing / Q000502:physiology*; D008854:Microscopy, Electron; D014709:Vero Cells; D015678:Viral Structural Proteins / Q000737:chemistry / Q000502:physiology*
D015678:Viral Structural Proteins