Cleavage of vimentin by different retroviral proteases.
Proteases (PRs) of retroviruses cleave viral polyproteins into their mature structural proteins and replication enzymes. Besides this essential role in the replication cycle of retroviruses, PRs also cleave a variety of host cell proteins. We have analyzed the in vitro cleavage of mouse vimentin by proteases of human immunodeficiency virus type 1 (HIV-1) and type 2 (HIV-2), bovine leukemia virus (BLV), Mason-Pfizer monkey virus (M-PMV), myeloblastosis-associated virus (MAV), and two active-site mutants of MAV PR. Retroviral proteases display significant differences in specificity requirements. Here, we show a comparison of substrate specificities of several retroviral proteases on vimentin as a substrate. Vimentin was cleaved by all the proteases at different sites and with different rates. The results show that the physiologically important cellular protein vimentin can be degraded by different retroviral proteases.
Snásel
J
J
Department of Biochemistry, Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, Prague.
Shoeman
R
R
Horejsí
M
M
Hrusková-Heidingsfeldová
O
O
Sedlácek
J
J
Ruml
T
T
Pichová
I
I
D000818:Animals; D016282:Aspartic Acid Endopeptidases / Q000378:metabolism; D001665:Binding Sites / Q000235:genetics; D004591:Electrophoresis, Polyacrylamide Gel; D010450:Endopeptidases / Q000378:metabolism*; D016333:HIV Protease; D006863:Hydrogen-Ion Concentration; D001909:Leukemia Virus, Bovine / Q000201:enzymology; D016093:Mason-Pfizer monkey virus / Q000201:enzymology; D051379:Mice; D009154:Mutation; D012190:Retroviridae / Q000201:enzymology*; D012965:Sodium Chloride / Q000378:metabolism; D013379:Substrate Specificity; D014746:Vimentin / Q000737:chemistry / Q000378:metabolism*
D014746:Vimentin; D012965:Sodium Chloride; D010450:Endopeptidases; D016282:Aspartic Acid Endopeptidases; D016333:HIV Protease; C065184:p16 protease, Human immunodeficiency virus 2; C036946:protease p15