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Inhibitory effects of cystatins on proteolytic activities of the Plum pox potyvirus cysteine proteinases.
Virus Res. 2004 Oct; 105(2):175-82.VR

Abstract

In an effort to develop new antiviral strategies effective against potyviruses, several cystatins were evaluated for their ability to inhibit the cysteine proteinases of Plum pox potyvirus (PPV) using in vitro proteolytic assays. The following cystatins were purified as GST fusion proteins and shown to be active against papain:oryzacystatins I and II (OCI and OCII), corn cystatin II (CCII), human stefin A (HSA), the domain 8 of tomato multicystatin (TMC-8) and a large 24kDa tomato cystatin (LTCyst). These cystatins did not inhibit the activity of purified recombinant PPV NIa proteinase, a serine-like cysteine proteinases related to the 3C proteinases of picornaviruses and to chymotrypsin. The cystatins were shown to inhibit slightly the activity of the PPV HC-Pro proteinase with CCII being the best inhibitor. However a large excess of the cystatins was required to observe any inhibition. Based on these results and on the documented pleiotropic effects of cystatins on the metabolism of plants, we conclude that they are not the best candidates for antiviral strategies targeted to viral cysteine proteinases. The availability of soluble active recombinant PPV NIa proteinase will be instrumental for the selection of other proteinase inhibitors with increased affinity and specificity for this proteinase.

Authors+Show Affiliations

Wen R
Pacific Agri-Food Research Centre, 4200 Highway 97, Summerland, BC, Canada V0H 1Z0.
Zhang SC
No affiliation info available
Michaud D
No affiliation info available
Sanfaçon H
No affiliation info available

MeSH

CystatinsCysteine EndopeptidasesCysteine Proteinase InhibitorsEndopeptidasesMicrobial Sensitivity TestsPapainPlum Pox VirusRecombinant Fusion ProteinsViral Proteins

Pub Type(s)

Journal Article

Language

eng

PubMed ID

15351491

Citation

Wen, Rui, et al. "Inhibitory Effects of Cystatins On Proteolytic Activities of the Plum Pox Potyvirus Cysteine Proteinases." Virus Research, vol. 105, no. 2, 2004, pp. 175-82.
Wen R, Zhang SC, Michaud D, et al. Inhibitory effects of cystatins on proteolytic activities of the Plum pox potyvirus cysteine proteinases. Virus Res. 2004;105(2):175-82.
Wen, R., Zhang, S. C., Michaud, D., & Sanfaçon, H. (2004). Inhibitory effects of cystatins on proteolytic activities of the Plum pox potyvirus cysteine proteinases. Virus Research, 105(2), 175-82.
Wen R, et al. Inhibitory Effects of Cystatins On Proteolytic Activities of the Plum Pox Potyvirus Cysteine Proteinases. Virus Res. 2004;105(2):175-82. PubMed PMID: 15351491.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Inhibitory effects of cystatins on proteolytic activities of the Plum pox potyvirus cysteine proteinases. AU - Wen,Rui, AU - Zhang,Shuo Cheng, AU - Michaud,Dominique, AU - Sanfaçon,Hélène, PY - 2004/04/06/received PY - 2004/05/28/revised PY - 2004/05/28/accepted PY - 2004/9/8/pubmed PY - 2005/3/12/medline PY - 2004/9/8/entrez SP - 175 EP - 82 JF - Virus research JO - Virus Res VL - 105 IS - 2 N2 - In an effort to develop new antiviral strategies effective against potyviruses, several cystatins were evaluated for their ability to inhibit the cysteine proteinases of Plum pox potyvirus (PPV) using in vitro proteolytic assays. The following cystatins were purified as GST fusion proteins and shown to be active against papain:oryzacystatins I and II (OCI and OCII), corn cystatin II (CCII), human stefin A (HSA), the domain 8 of tomato multicystatin (TMC-8) and a large 24kDa tomato cystatin (LTCyst). These cystatins did not inhibit the activity of purified recombinant PPV NIa proteinase, a serine-like cysteine proteinases related to the 3C proteinases of picornaviruses and to chymotrypsin. The cystatins were shown to inhibit slightly the activity of the PPV HC-Pro proteinase with CCII being the best inhibitor. However a large excess of the cystatins was required to observe any inhibition. Based on these results and on the documented pleiotropic effects of cystatins on the metabolism of plants, we conclude that they are not the best candidates for antiviral strategies targeted to viral cysteine proteinases. The availability of soluble active recombinant PPV NIa proteinase will be instrumental for the selection of other proteinase inhibitors with increased affinity and specificity for this proteinase. SN - 0168-1702 UR - https://www.unboundmedicine.com/medline/citation/15351491/Inhibitory_effects_of_cystatins_on_proteolytic_activities_of_the_Plum_pox_potyvirus_cysteine_proteinases_ DB - PRIME DP - Unbound Medicine ER -