Cleavage of vimentin by different retroviral proteases.

Abstract:

: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.

journal_name

Arch Biochem Biophys

authors

Snásel J,Shoeman R,Horejsí M,Hrusková-Heidingsfeldová O,Sedlácek J,Ruml T,Pichová I

doi

10.1006/abbi.2000.1776

subject

Has Abstract

pub_date

2000-05-15 00:00:00

pages

241-5

issue

2

eissn

0003-9861

issn

1096-0384

pii

S0003986100917764

journal_volume

377

pub_type

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