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Human monocytes possess a serine protease activity capable of degrading HIV-1 reverse transcriptase in vitro.

Abstract：

:Human immunodeficiency virus type-1 (HIV-1) reverse transcriptase (RT) plays a central role in the virus replication cycle. We found that HIV-1 RT was rapidly degraded when incubated with cell extracts obtained from human peripheral blood cells. The proteolytic activity responsible for the in vitro degradation of RT was present in monocytes and their precursors. Interestingly, this activity was downregulated upon cell activation or differentiation along the macrophage pathway. The proteolytic process appears specific for HIV-1 RT since other HIV-1 proteins were not degraded upon incubation in the same extracts. Although the degradation of RT was unaffected by specific proteasome inhibitors, it could be inhibited by PMSF and aprotinin, suggesting the involvement of a serine protease. Upon cell fractionation, this serine protease was found to be associated with the microsomal fraction and displayed an apparent molecular weight of approximately 2000 kDa, as determined by gel filtration. Our results suggest that a giant serine protease, different from tripeptidyl peptidase II, is involved in the in vitro degradation of HIV-1 RT. The possibility of an in vivo interaction between HIV-1 RT and a cell-type-specific serine protease is discussed.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Château MT,Robert-Hebmann V,Devaux C,Lazaro JB,Canard B,Coux O

doi

10.1006/bbrc.2001.5252

subject

Has Abstract

pub_date

2001-07-27 00:00:00

pages

863-72

issue

4

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(01)95252-0

journal_volume

285

pub_type

杂志文章

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