Adenovirus protease expressed in insect cells cleaves adenovirus proteins, ovalbumin and baculovirus protease in the absence of activating peptide.

Abstract:

:The adenovirus type 2 protease (EP) was expressed by infecting insect cells with a recombinant baculovirus. Immunoblot and activity analysis showed EP to be present in both the nucleus and cytoplasm. While the insect cell expressed EP was more soluble than the Escherichia coli expressed EP, its activity was one quarter of the latter, suggesting that eukaryotic postsynthetic modifications are not essential for enzyme activity. EP inactivated a cytoplasmic cathepsin-like baculovirus-encoded cysteine protease which carries a single EP cleavage site and which was capable of digesting most adenovirus structural proteins in vitro. In addition to cleavage of the baculovirus protease, the adenovirus EP was also able to cleave ovalbumin and canine adenovirus protein pre-VII, in the absence of activating peptide. EP activation therefore may occur by means of factors other than the specific activating peptide.

journal_name

Virus Res

journal_title

Virus research

authors

Keyvani-Amineh H,Labrecque P,Cai F,Carstens EB,Weber JM

doi

10.1016/0168-1702(95)00018-l

subject

Has Abstract

pub_date

1995-07-01 00:00:00

pages

87-97

issue

2

eissn

0168-1702

issn

1872-7492

pii

0168-1702(95)00018-L

journal_volume

37

pub_type

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