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Polyprotein Processing Protease of African Swine Fever Virus: Purification and Biochemical Characterization
Author(s) -
Daniel Rubio,
Alı́ Alejo,
Irene Rodrı́guez,
María Salas
Publication year - 2003
Publication title -
journal of virology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.617
H-Index - 292
eISSN - 1070-6321
pISSN - 0022-538X
DOI - 10.1128/jvi.77.7.4444-4448.2003
Subject(s) - biology , protease , cleavage (geology) , virology , recombinant dna , african swine fever virus , virus , ns3 , polyproteins , enzyme , biochemistry , paleontology , fracture (geology) , gene
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.

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