The autocatalytic protease p29 encoded by a hypovirulence-associated virus of the chestnut blight fungus resembles the potyvirus-encoded protease HC-Pro

Choi, Gil H.; Pawlyk, Diane M.; Nuss, Donald L.

doi:10.1016/0042-6822(91)91004-z

Cited by 87 publications

(71 citation statements)

References 14 publications

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“…There are also significant differences in the predicted physical characteristics of the two proteins. p29 has a significant level of similarity to the multifunctional potyvirus papain-like protease protein HCPro (11,27). These similarities include conserved amino acid sequences flanking the cysteine and histidine residues that are essential for proteolytic cleavage, the nature of the cleavage site, the distance between the essential residues and the cleavage site, and the conservation of a number of cysteine residues within the N-terminal portions of the two proteins.…”

Section: Vol 77 2003mentioning

confidence: 99%

“…The N-terminal 24 codons are essential for virus viability, perhaps serving as part of an internal ribosome entry site-like sequence (43), whereas the C-terminal half, including the catalytic Cys 162 and His 215 residues, is responsible for the cotranslational self-cleavage from polyprotein p69 (11,12). The third p29 domain was initially suggested from studies in which p29 was shown to suppress pigmentation and asexual sporulation regardless of whether it was expressed in the absence of virus infection or within the context of the infectious CHV1-EP713 cDNA clone, presumably through interactions with host factors (13,16).…”

Section: Vol 77 2003mentioning

confidence: 99%

“…ORF A encodes a papain-like protease, p29, and a highly basic protein, p40, derived, respectively, from the N terminus and C terminus of polyprotein, p69, by a p29-mediated autocatalytic cleavage event (11,12). Craven et al (16) subsequently used a similar transformation approach to map the suppressive activity to p29.…”

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confidence: 99%

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Hypovirus Papain-Like Protease p29 Functions in trans To Enhance Viral Double-Stranded RNA Accumulation and Vertical Transmission

Suzuki

Maruyama

Moriyama

et al. 2003

J Virol

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The prototypic hypovirus CHV1-EP713 attenuates virulence (hypovirulence) and alters several physiological processes of the chestnut blight fungus Cryphonectria parasitica. The papain-like protease, p29, and the highly basic protein, p40, derived, respectively, from the N-terminal and C-terminal portions of the CHV1-EP713-encoded open reading frame (ORF) A polyprotein, p69, both contribute to reduced pigmentation and sporulation. The p29 coding region was shown to suppress pigmentation and asexual sporulation in the absence of virus infection in transformed C. parasitica, whereas transformants containing the p40-coding domain exhibited a wild-type, untransformed phenotype. Deletion of either p29 or p40 from the viral genome also results in reduced accumulation of viral RNA. We now show that p29, but not p40, functions in trans to enhance genomic RNA accumulation and vertical transmission of p29 deletion mutant viruses. The frequency of virus transmission through conidia was found to decrease with reduced accumulation of viral genomic double-stranded RNA (dsRNA): from almost 100% for wild-type virus to ϳ50% for ⌬p29, and 10 to 20% for ⌬p69. When expressed from a chromosomally integrated cDNA copy, p29 elevated viral dsRNA accumulation and transmission for ⌬p29 mutant virus to the level shown by wild-type virus. Increased viral RNA accumulation levels were also observed for a ⌬p69 mutant lacking almost the entire ORF A sequence. Such enhancements were not detected in transgenic fungal colonies expressing p40. Mutation of p29 residues Cys 70 or Cys 72 , strictly conserved in hypovirus p29 and potyvirus HC-Pro, resulted in the loss of both p29-mediated suppressive activity in virus-free transgenic C. parasitica and in trans enhancement of RNA accumulation and transmission, suggesting a linkage between these functional activities. These results suggest that p29 is an enhancer of viral dsRNA accumulation and vertical virus transmission through asexual spores.Members of the virus family Hypoviridae (22) persistently attenuate virulence (hypovirulence) and stably alter complex biological processes upon infection of their fungal host, the chestnut blight fungus, Cryphonectria parasitica. Infection-related phenotypic changes can include suppressed pigment production and asexual sporulation, altered colony morphology, loss of female fertility and modified expression of specific host genes (1,18,28,31). Infectious hypovirus cDNA clones (8, 10) and a robust transformation protocol for C. parasitica (15) provide a versatile system for identifying virus-encoded symptom determinants and modulators of hypovirus replication.Choi and Nuss (13) showed that transformation of virus-free C. parasitica with the 5Ј-proximal coding domain, open reading frame (ORF) A, resulted in suppressed conidiation and pigmentation but no change in fungal virulence. ORF A encodes a papain-like protease, p29, and a highly basic protein, p40, derived, respectively, from the N terminus and C terminus of polyprotein, p69, by a p29-mediated autocatalytic cl...

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Section: Vol 77 2003mentioning

confidence: 99%

Section: Vol 77 2003mentioning

confidence: 99%

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Hypovirus Papain-Like Protease p29 Functions in trans To Enhance Viral Double-Stranded RNA Accumulation and Vertical Transmission

Suzuki

Maruyama

Moriyama

et al. 2003

J Virol

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“…In TYMV a Thr is present in PI'. This is unusual, since hydrolysis by most papain-like viral proteinases occurs between small amino acids (Choi et at., 1991 ;Shapira & Nuss, 1991 ;Carrington & Herndom 1992;Snijder et al, 1992;Dong & Baker, 1994; for review see Strauss & Strauss, 1990) except for nsP2 of alphaviruses, which cleaves before a Tyr at the nsP3/P4 site. The insensitivity of the latter proteinase to the residue in PI' was confirmed by various mutations in this position (see Strauss & Strauss, 1990).…”

confidence: 99%

Expression of the turnip yellow mosaic virus proteinase in Escherichia coli and determination of the cleavage site within the 206 kDa protein

Kadaré¹,

Rozanov²,

Haenni

1995

Journal of General Virology

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The large non-structural polyprotein (206 kDa) of turnip yellow mosaic tymovirus (TYMV) undergoes autocleavage, producing N-and C-terminal proteins. Here we show that the viral proteinase responsible for this event is active when produced in Escherichia coli, as monitored in Western blots by examining the generation of the C-terminal cleavage product after induction by IPTG. The outer boundaries and critical amino acids of the proteinase domain were characterized by deletion analysis and site-directed mutagenesis. A miniproteinase of 273 residues resulting from combined N-and Cterminal deletions still performed efficient cleavage.

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“…The structural similarity between HC-Pro and nsP2 CPD may be a manifestation of common evolutionary origin or a result of convergent evolution. Clan CN may also include p29 and p48 cysteine proteases from Cryphonectria hypoviruses which show short similar sequences with HC-Pro around the catalytic dyad residues and cleavage site (55,56).…”

Section: Discussionmentioning

confidence: 99%

Structure of the Autocatalytic Cysteine Protease Domain of Potyvirus Helper-component Proteinase

Guo

Lin

2011

Journal of Biological Chemistry

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The helper-component proteinase (HC-Pro) of potyvirus is involved in polyprotein processing, aphid transmission, and suppression of antiviral RNA silencing. There is no high resolution structure reported for any part of HC-Pro, hindering mechanistic understanding of its multiple functions. We have determined the crystal structure of the cysteine protease domain of HC-Pro from turnip mosaic virus at 2.0 Å resolution. As a protease, HC-Pro only cleaves a Gly-Gly dipeptide at its own C terminus. The structure represents a postcleavage state in which the cleaved C terminus remains tightly bound at the active site cleft to prevent trans activity. The structure adopts a compact ␣/␤-fold, which differs from papain-like cysteine proteases and shows weak similarity to nsP2 protease from Venezuelan equine encephalitis alphavirus. Nevertheless, the catalytic cysteine and histidine residues constitute an active site that is highly similar to these in papain-like and nsP2 proteases. HC-Pro recognizes a consensus sequence YXVGG around the cleavage site between the two glycine residues. The structure delineates the sequence specificity at sites P1-P4. Structural modeling and covariation analysis across the Potyviridae family suggest a tryptophan residue accounting for the glycine specificity at site P1 . Moreover, a surface of the protease domain is conserved in potyvirus but not in other genera of the Potyviridae family, likely due to extra functional constrain. The structure provides insight into the catalysis mechanism, cis-acting mode, cleavage site specificity, and other functions of the HC-Pro protease domain.

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The autocatalytic protease p29 encoded by a hypovirulence-associated virus of the chestnut blight fungus resembles the potyvirus-encoded protease HC-Pro

Cited by 87 publications

References 14 publications

Hypovirus Papain-Like Protease p29 Functions in trans To Enhance Viral Double-Stranded RNA Accumulation and Vertical Transmission

Hypovirus Papain-Like Protease p29 Functions in trans To Enhance Viral Double-Stranded RNA Accumulation and Vertical Transmission

Expression of the turnip yellow mosaic virus proteinase in Escherichia coli and determination of the cleavage site within the 206 kDa protein

Structure of the Autocatalytic Cysteine Protease Domain of Potyvirus Helper-component Proteinase

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