Inhibition of Plant-Pathogenic Fungi by the Barley Cystatin Hv-CPI (Gene Icy) Is Not Associated with Its Cysteine-Proteinase Inhibitory Properties

Martinez Muñoz, Manuel and Lopez Solanilla, Emilia and Rodriguez Palenzuela, Pablo and Carbonero Zalduegui, Pilar and Diaz Rodriguez, Isabel (2003). Inhibition of Plant-Pathogenic Fungi by the Barley Cystatin Hv-CPI (Gene Icy) Is Not Associated with Its Cysteine-Proteinase Inhibitory Properties. "Molecular Plant-Microbe Interactions", v. 16 (n. 10); pp. 876-883. ISSN 0894-0282. https://doi.org/10.1094/MPMI.2003.16.10.876.

Description

Title: Inhibition of Plant-Pathogenic Fungi by the Barley Cystatin Hv-CPI (Gene Icy) Is Not Associated with Its Cysteine-Proteinase Inhibitory Properties
Author/s:
  • Martinez Muñoz, Manuel
  • Lopez Solanilla, Emilia
  • Rodriguez Palenzuela, Pablo
  • Carbonero Zalduegui, Pilar
  • Diaz Rodriguez, Isabel
Item Type: Article
Título de Revista/Publicación: Molecular Plant-Microbe Interactions
Date: October 2003
ISSN: 0894-0282
Volume: 16
Subjects:
Faculty: E.T.S. de Ingeniería Agronómica, Alimentaria y de Biosistemas (UPM)
Department: Biotecnología - Biología Vegetal
Creative Commons Licenses: Recognition - No derivative works - Non commercial

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Abstract

The recombinant barley cystatin Hv-CPI inhibited the growth of three phytopathogenic fungi (Botrytis cinerea, Colletotrichum graminicola, and Plectosphaerella cucumerina) and the saprotrophic fungus Trichoderma viride. Several mutants of barley cystatin were generated by polymerase chain reaction approaches and both their antifungal and their cysteine-proteinase inhibitory properties investigated. Point mutants R38-G, Q63-L, and Q63-P diminished their capacity for inhibiting papain and cathepsin B, retaining their antifungal properties. However, mutant C68-G was more active for papain and cathepsin B than the wild type. These results indicate that in addition to the consensus cystatin-reactive site, Q63-V64-V65-A66-G67, the A37-R38-F39-A40-V41 region, common to all cereal cystatins, and the C68 residue are important for barley cystatin activity. On the other hand, the K92-P mutant is inactive as a fungicide, but still retains measurable inhibitory activity for papain and cathepsin B. Against B. cinerea, the antifungal effect of Hv-CPI and of its derived mutants does not always correlate with their activities as proteinase inhibitors, because the Q63-P mutant is inactive as a cystatin, while still inhibiting fungal growth, and the K92-P mutant shows the reciprocal effects. These data indicate that inhibition of plant-pathogenic fungi by barley cystatin is not associated with its cysteine-proteinase inhibitory activity. Moreover, these results are corroborated by the absence of inhibition of intra- and extramycelia-proteinase activities by barley cystatin and by other well-known inhibitors of cysteine-proteinase activity in the fungal zymograms of B. cinerea.

Funding Projects

TypeCodeAcronymLeaderTitle
Madrid Regional Government07M/0015/2001UnspecifiedIsabel DíazEvaluación y especificidad de cistatinas de origen vegetal frente a artrópodos plaga y enemigos naturales
Madrid Regional Government07M/0050/2002UnspecifiedIsabel DíazEvaluación y especifidad de inhibidores de proteasas de origen vegetal frente a hongos fitopatógenos, insectos plaga y enemigos naturales
Government of SpainP98/0734UnspecifiedUnspecifiedUnspecified

More information

Item ID: 54036
DC Identifier: http://oa.upm.es/54036/
OAI Identifier: oai:oa.upm.es:54036
DOI: 10.1094/MPMI.2003.16.10.876
Official URL: https://apsjournals.apsnet.org/doi/10.1094/MPMI.2003.16.10.876
Deposited by: Biblioteca ETSI Agrónomos
Deposited on: 18 Feb 2019 15:44
Last Modified: 18 Feb 2019 15:44
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