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Pro domain peptide of HGCP-Iv cysteine proteinase inhibits nematode cysteine proteinases.
Genet Mol Res. 2004 Sep 30; 3(3):342-55.GM

Abstract

Cysteine proteinases (CPs) are synthesized as zymogens and converted to mature proteinase forms by proteolytic cleavage and release of their pro domain peptides. A cDNA encoding a papain-like CP, called hgcp-Iv, was isolated from a Heterodera glycines J2 cDNA library, expressed and utilized to assess the ability of its propeptide to inhibit proteinase in its active form. The hgcp-Iv cDNA sequence encodes a polypeptide of 374 amino acids with the same domain organization as other cathepsin L-like CPs, including a hydrophobic signal sequence and a pro domain region. HGCP-Iv, produced in Escherichia coli as a fusion protein with thioredoxin, degrades the synthetic peptide benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin and is inhibited by E-64, a substrate and inhibitor commonly used for functional characterization of CPs. Recombinant propeptides of HGCP-Iv, expressed in E. coli, presented high inhibitory activity in vitro towards its cognate enzyme and proteinase activity of Meloidogyne incognita females, suggesting its usefulness in inhibiting nematode CPs in biological systems. Cysteine proteinases from other species produced no noticeable activity.

Authors+Show Affiliations

Silva FB
Departamento de Biologia Celular, Universidade de Brasília, Brasília, DF, Brasil.
Batista JA
No affiliation info available
Marra BM
No affiliation info available
Fragoso RR
No affiliation info available
Monteiro AC
No affiliation info available
Figueira EL
No affiliation info available
Grossi-de-Sá MF
No affiliation info available

MeSH

Amino Acid SequenceAnimalsBase SequenceCysteine EndopeptidasesCysteine Proteinase InhibitorsDNA, ComplementaryDNA, HelminthFemaleMolecular Sequence DataPeptidesPlant DiseasesPolymerase Chain ReactionTylenchoidea

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

15614726

Citation

Silva, Francine B., et al. "Pro Domain Peptide of HGCP-Iv Cysteine Proteinase Inhibits Nematode Cysteine Proteinases." Genetics and Molecular Research : GMR, vol. 3, no. 3, 2004, pp. 342-55.
Silva FB, Batista JA, Marra BM, et al. Pro domain peptide of HGCP-Iv cysteine proteinase inhibits nematode cysteine proteinases. Genet Mol Res. 2004;3(3):342-55.
Silva, F. B., Batista, J. A., Marra, B. M., Fragoso, R. R., Monteiro, A. C., Figueira, E. L., & Grossi-de-Sá, M. F. (2004). Pro domain peptide of HGCP-Iv cysteine proteinase inhibits nematode cysteine proteinases. Genetics and Molecular Research : GMR, 3(3), 342-55.
Silva FB, et al. Pro Domain Peptide of HGCP-Iv Cysteine Proteinase Inhibits Nematode Cysteine Proteinases. Genet Mol Res. 2004 Sep 30;3(3):342-55. PubMed PMID: 15614726.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Pro domain peptide of HGCP-Iv cysteine proteinase inhibits nematode cysteine proteinases. AU - Silva,Francine B, AU - Batista,João A N, AU - Marra,Brener M, AU - Fragoso,Rodrigo R, AU - Monteiro,Ana Carolina S, AU - Figueira,Edson L Z, AU - Grossi-de-Sá,Maria Fátima, Y1 - 2004/09/30/ PY - 2004/12/23/pubmed PY - 2005/3/15/medline PY - 2004/12/23/entrez SP - 342 EP - 55 JF - Genetics and molecular research : GMR JO - Genet Mol Res VL - 3 IS - 3 N2 - Cysteine proteinases (CPs) are synthesized as zymogens and converted to mature proteinase forms by proteolytic cleavage and release of their pro domain peptides. A cDNA encoding a papain-like CP, called hgcp-Iv, was isolated from a Heterodera glycines J2 cDNA library, expressed and utilized to assess the ability of its propeptide to inhibit proteinase in its active form. The hgcp-Iv cDNA sequence encodes a polypeptide of 374 amino acids with the same domain organization as other cathepsin L-like CPs, including a hydrophobic signal sequence and a pro domain region. HGCP-Iv, produced in Escherichia coli as a fusion protein with thioredoxin, degrades the synthetic peptide benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin and is inhibited by E-64, a substrate and inhibitor commonly used for functional characterization of CPs. Recombinant propeptides of HGCP-Iv, expressed in E. coli, presented high inhibitory activity in vitro towards its cognate enzyme and proteinase activity of Meloidogyne incognita females, suggesting its usefulness in inhibiting nematode CPs in biological systems. Cysteine proteinases from other species produced no noticeable activity. SN - 1676-5680 UR - https://www.unboundmedicine.com/medline/citation/15614726/Pro_domain_peptide_of_HGCP_Iv_cysteine_proteinase_inhibits_nematode_cysteine_proteinases_ DB - PRIME DP - Unbound Medicine ER -