Characterization of the African swine fever virion protein j18L.
The African swine fever virus (ASFV) open reading frame (ORF) that is named jl8L in the Malawi (LIL20/1) isolate and E199L in the Ba71V isolate encodes a cysteine rich protein of 195 amino acids with a predicted molecular mass of 21.7 kDa and a hydrophobic domain near the C terminus. There are several possible motifs for glycosylation, phosphorylation and myristoylation. Rabbit antisera and monoclonal antibodies raised against a recombinant ASFV j18L protein expressed as a fusion protein with glutathione S-transferase (GST) identified proteins of 19.0-20 kDa in cells infected with different ASFV strains and with a recombinant vaccinia virus expressing j18L. The monoclonal antibodies detected a protein of 20.0 kDa whereas rabbit antisera detected two proteins with relative molecular masses of 15.0 and 20.0 kDa in purified extracellular ASF virions. In ASFV-infected cells, the j18L protein was expressed late post-infection and was localized mainly in the viral factories.
Sun
H
H
Institute for Animal Health, Pirbright Laboratory, Surrey, UK.
Jenson
J
J
Dixon
L K
LK
Parkhouse
M E
ME
D000358:African Swine Fever Virus / Q000737:chemistry*; D000818:Animals; D001483:Base Sequence; D008969:Molecular Sequence Data; D008970:Molecular Weight; D011817:Rabbits; D013552:Swine; D014764:Viral Proteins / Q000032:analysis* / Q000502:physiology; D014771:Virion / Q000737:chemistry*
D014764:Viral Proteins