Polyprotein processing protease of African swine fever virus: purification and biochemical characterization.
The purified recombinant African swine fever virus polyprotein processing protease cleaves the two GG-X sites in polyprotein pp62 with the same efficiency. Cleavage at the site that is first recognized in vivo is not a requisite for cleavage at the second site, suggesting the existence of mechanisms that control the ordered processing of the polyprotein during infection.
Rubio
Daniel
D
Centro de Biología Molecular Severo Ochoa (Consejo Superior de Investigaciones Científicas-Universidad Autónoma de Madrid), Universidad Autónoma de Madrid, Cantoblanco, Spain.
Alejo
Alí
A
Rodríguez
Irene
I
Salas
María L
ML
D000358:African Swine Fever Virus / Q000201:enzymology* / Q000235:genetics / Q000472:pathogenicity; D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D010450:Endopeptidases / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism; D005814:Genes, Viral; D066298:In Vitro Techniques; D009154:Mutation; D020815:Polyproteins / Q000378:metabolism; D011499:Protein Processing, Post-Translational; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D025842:SUMO-1 Protein / Q000378:metabolism; D013379:Substrate Specificity; D014764:Viral Proteins / Q000378:metabolism
D020815:Polyproteins; D011994:Recombinant Proteins; D025842:SUMO-1 Protein; D014764:Viral Proteins; D010450:Endopeptidases