Role of inhibitors of proteolytic enzymes in plant defense against phytopathogenic microorganisms

Valueva, T. A.; Mosolov, V. V.

doi:10.1007/s10541-005-0015-5

Cited by 94 publications

(70 citation statements)

References 75 publications

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“…Phytophthora effectors that suppress host defense responses have been described in several pathosystems [10][11][12]. Suppression of host defenses can occur through the production of inhibitor proteins that target host enzymes [13].…”

Section: Introductionmentioning

confidence: 99%

Cloning, characterization and in vitro and in planta expression of a glucanase inhibitor protein (GIP) of Phytophthora cinnamomi

Martins

Belo

et al. 2014

Mol Biol Rep

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Oomycetes from the genus Phytophthora are fungus-like plant pathogens that are devastating for agriculture and natural ecosystems. They are able to secrete a glucanase inhibitor protein (GIP) that inhibits the activity of endoglucanases (EGases) involved in defense responses against infection. One of the most widely distributed and aggressive Phytophthora species, with more than 1,000 host plants is P. cinnamomi. In this work we report the sequencing and characterization of a class of GIPs secreted by Phytophthora cinnamomi. The gip gene from P. cinnamomi has a 937 bp ORF encoding a putative peptide of 312 deduced amino acids. The expression of this gene was studied during growth in different carbon sources (glucose, cellulose and sawdust), by RT-qPCR and its level of expression was evaluated at five time points. The highest expression of gip gene occurred in sawdust at 8 h of induction. In vivo infection of C. sativa revealed an increase in gip expression from 12 to 24 h. At 36 h its expression decreased suggesting that a compensatory mechanism must occur in plant.

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Section: Introductionmentioning

confidence: 99%

Cloning, characterization and in vitro and in planta expression of a glucanase inhibitor protein (GIP) of Phytophthora cinnamomi

Martins

Belo

et al. 2014

Mol Biol Rep

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“…Insect herbivores have developed over time effective strategies to elude the inhibitory effects of plant protease inhibitors (Broadway, 2000), including: (1) the use of complex digestive protease systems with proteases from different mechanistic classes acting in a complementary, coordinated manner (Terra and Ferreira, 1994;Brunelle et al, 1999Brunelle et al, , 2004; (2) the production of alternative, insensitive protease forms following ingestion of protease inhibitors (Jongsma et al, 1995;Bown et al, 1997;Cloutier et al, 1999Cloutier et al, , 2000Broadway, 2001a, 2001b;Zhu-Salzman et al, 2003;Brunelle et al, 2004); and (3) the degradation of defensive protease inhibitors using nontarget, insensitive digestive proteases (Michaud et al, 1995a;Michaud, 1997;Girard et al, 1998a;Giri et al, 1998;Gruden et al, 2003;ZhuSalzman et al, 2003). It is now generally recognized that protease/inhibitor interactions in plant-insect systems are the result of a long, coevolutive process triggering the continuous diversification of proteolytic and protease inhibitory functions in the competing organisms (Lopes et al, 2004;Valueva and Mosolov, 2004;Christeller, 2005;Kiggundu et al, 2006;Girard et al, 2007).…”

mentioning

confidence: 99%

Tailoring the Specificity of a Plant Cystatin toward Herbivorous Insect Digestive Cysteine Proteases by Single Mutations at Positively Selected Amino Acid Sites

et al. 2008

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Plant cystatins, similar to other defense proteins, include hypervariable, positively selected amino acid sites presumably impacting their biological activity. Using 29 single mutants of the eighth domain of tomato (Solanum lycopersicum) multicystatin, SlCYS8, we assessed here the potential of site-directed mutagenesis at positively selected amino acid sites to generate cystatin variants with improved inhibitory potency and specificity toward herbivorous insect digestive cysteine (Cys) proteases. Compared to SlCYS8, several mutants (22 out of 29) exhibited either improved or lowered potency against different model Cys proteases, strongly suggesting the potential of positively selected amino acids as target sites to modulate the inhibitory specificity of the cystatin toward Cys proteases of agronomic significance. Accordingly, mutations at positively selected sites strongly influenced the inhibitory potency of SlCYS8 against digestive Cys proteases of the insect herbivore Colorado potato beetle (Leptinotarsa decemlineata). In particular, several variants exhibited improved potency against both cystatin-sensitive and cystatininsensitive digestive Cys proteases of this insect. Of these, some variants also showed weaker activity against leaf Cys proteases of the host plant (potato [Solanum tuberosum]) and against a major digestive Cys protease of the two-spotted stinkbug Perillus bioculatus, an insect predator of Colorado potato beetle showing potential for biological control. Overall, these observations suggest the usefulness of site-directed mutagenesis at positively selected amino acid sites for the engineering of recombinant cystatins with both improved inhibitory potency toward the digestive proteases of target herbivores and weaker potency against nontarget Cys proteases in the host plant or the environment.

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“…A few PRs families have enzymatic effects such as chitinases (PR-3, PR-8, PR-11) 105,168 , glucanases (PR-2) 136,137 , peroxidases (PR-9) 2,132,331 , ribonucleases (PR-10) 85,190 and (PR-4) 41 , or inhibitory effects such as enzyme inhibitors (PR-6) 326,349 . Inhibitory activity towards proteases or α-amylases is ascribed to the PR-5 298 , PR-12 192 and PR-14 family 160,161 .…”

Section: Biological Function and Mechanism Of Actionmentioning

confidence: 99%

“…PIs comprise a large and diverse group of proteins able to inhibit insects and other invertebrate pests (nematodes and mollusks), as well as animal and bird gut digestive enzymes 224,225,326 and fungal proteases 257,349 . The function of PIs is not limited to their ability to inhibit proteases.…”

Section: Protease Inhibitors (Pis) (Pr-6)mentioning

confidence: 99%

A Review: Biological and Technological Functions of Barley Seed Pathogenesis-Related Proteins (PRs)

Gorjanović

2009

Journal of the Institute of Brewing

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The mature barley seed proteome is dominated by proteins involved in stress responses, including the Pathogenesis-Related proteins (PRs). PRs are currently classified into 17 families. The biochemistry of the PRs families, whose members are constitutively present in barley seed, is surveyed in this paper. These proteins are assumed to protect dormant and germinating seeds against pathogenic microorganisms and pests. The current knowledge on PRs structural and functional properties is summarized in an attempt to illustrate their importance in barley seed innate resistance. At the same time, a platform to understand PRs technological function in cereal foods and in beverage processing and quality is provided.

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Role of inhibitors of proteolytic enzymes in plant defense against phytopathogenic microorganisms

Cited by 94 publications

References 75 publications

Cloning, characterization and in vitro and in planta expression of a glucanase inhibitor protein (GIP) of Phytophthora cinnamomi

Cloning, characterization and in vitro and in planta expression of a glucanase inhibitor protein (GIP) of Phytophthora cinnamomi

Tailoring the Specificity of a Plant Cystatin toward Herbivorous Insect Digestive Cysteine Proteases by Single Mutations at Positively Selected Amino Acid Sites

A Review: Biological and Technological Functions of Barley Seed Pathogenesis-Related Proteins (PRs)

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