PROSITE logo

PROSITE documentation PDOC51875 [for PROSITE entry PS51875]
Hypovirulence-associated virus (HAV) papain-like proteases p29 and p48 domains profiles


Description

Hypoviruses are positive-strand RNA mycoviruses that attenuate virulence of their pathogenic fungal hosts [E1]. They employ a gene expression strategy that involves the autocatalytic processing of the N-terminal portion of encoded polyproteins by papain-like protease domains. The prototypic hypovirus CHV-1/EP713, responsible for virulence attenuation (hypovirulence) of the chestnut blight fungus Cryphonectria parasitica, encodes two contiguous open reading frames (ORFs) designated ORF A and ORF B, which contain N-terminal proteases p29 and p48, respectively. Protease p29 functions as a suppressor of the RNA silencing defense response, while p48 is required for viral RNA replication [1,2,3,4].

The HAV papain-like protease p29 is a cysteine protease, which forms the peptidase family C7 [E2]. A Cys and a His catalytic residue are essential for autocatalytic cleavage at a glycine dipeptide clevage site located at the C-terminus of the domain [1,2,4].

The HAV papain-like protease p48 is a cysteine protease, which forms the peptidase family C8 [E3]. A Cys and a His catalytic residue are essential for autocatalytic cleavage between the cleavage site residues Gly and Ala located at the C-terminus of the domain [1,2,4].

The profiles we developed cover the entire HAV papain-like proteases p48 and p29 domains.

Last update:

November 2018 / First entry.

-------------------------------------------------------------------------------


Technical section

PROSITE methods (with tools and information) covered by this documentation:

HAV_P48_PRO, PS51875; Hypovirus-associated virus (HAV) papain-like protease p48 domain profile  (MATRIX)

HAV_P29_PRO, PS51877; Hypovirulence-associated virus (HAV) papain-like protease p29 domain profile  (MATRIX)


References

1AuthorsShapira R. Nuss D.L.
TitleGene expression by a hypovirulence-associated virus of the chestnut blight fungus involves two papain-like protease activities. Essential residues and cleavage site requirements for p48 autoproteolysis.
SourceJ. Biol. Chem. 266:19419-19425(1991).
PubMed ID1918054

2AuthorsChoi G.H. Pawlyk D.M. Nuss D.L.
TitleThe autocatalytic protease p29 encoded by a hypovirulence-associated virus of the chestnut blight fungus resembles the potyvirus-encoded protease HC-Pro.
SourceVirology 183:747-752(1991).
PubMed ID1853573

3AuthorsDeng F. Nuss D.L.
TitleHypovirus papain-like protease p48 is required for initiation but not for maintenance of virus RNA propagation in the chestnut blight fungus Cryphonectria parasitica.
SourceJ. Virol. 82:6369-6378(2008).
PubMed ID18448523
DOI10.1128/JVI.02638-07

4AuthorsJensen K.S. Nuss D.L.
TitleMutagenesis of the catalytic and cleavage site residues of the hypovirus papain-like proteases p29 and p48 reveals alternative processing and contributions to optimal viral RNA accumulation.
SourceJ. Virol. 88:11946-11954(2014).
PubMed ID25100848
DOI10.1128/JVI.01489-14

E1Titlehttps://viralzone.expasy.org/594

E2Titlehttps://www.ebi.ac.uk/merops/cgi-bin/famsum?family=C7

E3Titlehttps://www.ebi.ac.uk/merops/cgi-bin/famsum?family=C8



PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.

Miscellaneous

View entry in original PROSITE document format
View entry in raw text format (no links)