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

Martins, Ivone M.; Martins, Fátima; Belo, Hélio; Vaz, Madalena; Carvalho, Marisa; Cravador, A.; Choupina, Altino

doi:10.1007/s11033-014-3101-1

Cited by 15 publications

(24 citation statements)

References 23 publications

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“…The partial gene is truncated at the N-terminus, possibly as a result of sequencing or assembly errors. The expression of one of the full-length genes, PHYCI_217079, increases during the first 24 h after inoculation of roots of chestnut before decreasing over the next 12 h (Martins et al, 2014a).…”

Section: Inhibitors Of Plant Endoglucanases (Gips)mentioning

confidence: 99%

Phytophthora cinnamomi

Hardham

Blackman

2017

Molecular Plant Pathology

163

168

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A root pathogen which causes rotting of fine and fibrous roots, but which can also cause stem cankers. Root damage may inhibit water movement from roots to shoots, leading to dieback of young shoots. USEFUL WEBSITES: http://fungidb.org/fungidb/; http://genome.jgi.doe.gov/Phyci1/Phyci1.home.html; http://www.ncbi.nlm.nih.gov/assembly/GCA_001314365.1; http://www.ncbi.nlm.nih.gov/assembly/GCA_001314505.1.

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Section: Inhibitors Of Plant Endoglucanases (Gips)mentioning

confidence: 99%

Phytophthora cinnamomi

Hardham

Blackman

2017

Molecular Plant Pathology

163

168

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“…TGases structural sequences with elicitin activity, associated to plant defense mechanisms, were isolated and characterized by our group in Phytophthora cinnamomi (partial cds). Thermal asymmetric interlaced-PCR, and hemispecific PCR amplification protocols, that combine nested insert ionspecific primers (designed in highly conserved region of Phytophthora transglutaminases), with degenerate primers, were used to amplify DNA flanking of a known sequence using genomic P. cinnamomi DNA as template Martins et al 2014). In this process, a 2,218-bp DNA fragment was sequenced (GenBank: AM403129.1, unpublished results).…”

Section: Tgase In Phytophthoramentioning

confidence: 99%

Transglutaminases: recent achievements and new sources

Martins

Matos

Costa

et al. 2014

Appl Microbiol Biotechnol

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Transglutaminases are a family of enzymes (EC 2.3.2.13), widely distributed in various organs, tissues, and body fluids, that catalyze the formation of a covalent bond between a free amine group and the γ-carboxamide group of protein or peptide-bound glutamine. Besides forming these bonds, that exhibit high resistance to proteolytic degradation, transglutaminases also form extensively cross-linked, generally insoluble, protein biopolymers that are indispensable for the organism to create barriers and stable structures. The extremely high cost of transglutaminase of animal origin has hampered its wider application and has initiated efforts to find an enzyme of microbial origin. Since the early 1990s, many microbial transglutaminase-producing strains have been found, and production processes have been optimized. This has resulted in a rapidly increasing number of applications of transglutaminase in the food sector. However, applications of microbial transglutaminase in other sectors have also been explored, but in a much lesser extent. Our group has identified a transglutaminase in the oomycete Phytophthora cinnamomi, which is able to induct defense responses and disease-like symptoms. In this mini-review, we report the achievements in this area in order to illustrate the importance and the versatility of transglutaminases.

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“…Our group have identified and characterized some proteins involved in mechanisms of infection by P. cinnamomi: endo-1,3-beta-glucanase GenBank: AM259651.1 (complete cds) (Meirinho et al 2010), endo-glucanase GenBank: AJ964942.1 (partial cds) (unpublished results), glucanase inhibitor protein (GIP) GenBank: AM259384.1 (complete cds) (Martins et al 2014), necrosis-inducing Phytophthora protein 1 (NPP1) GenBank: AM403130.1 (complete cds) (unpublished results) (Gijzen and Nurnberger 2006;Yu et al 2008), and transglutaminase GenBank: AM403129.1 (unpublished results).…”

Section: Pathogenic Processes In Oomycetesmentioning

confidence: 99%

“…In the studies of expression by RT-PCR, the genes isolated by our group in P. cinnamomi, in vivo infection, with cell lines of Castanea sativa, reveal the intimate relationship between plants and phytopathogens that has led to the coevolution of a number of complex strategies for attack and defense (Martins et al 2014).…”

Section: Gene Expression In Phytophthoramentioning

confidence: 99%

Scientifically advanced solutions for chestnut ink disease

Choupina

Estevinho

Martins

2014

Appl Microbiol Biotechnol

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On the north regions of Portugal and Spain, the Castanea sativa Mill. culture is extremely important. The biggest productivity and yield break occurs due to the ink disease, the causal agent being the oomycete Phytophthora cinnamomi. This oomycete is also responsible for the decline of many other plant species in Europe and worldwide. P. cinnamomi and Phytophthora cambivora are considered, by the generality of the authors, as the C. sativa ink disease causal agents. Most Phytophthora species secrete large amounts of elicitins, a group of unique highly conserved proteins that are able to induce hypersensitive response (HR) and enhances plant defense responses in a systemic acquired resistance (SAR) manner against infection by different pathogens. Some other proteins involved in mechanisms of infection by P. cinnamomi were identified by our group: endo-1,3-beta-glucanase (complete cds); exo-glucanase (partial cds) responsible by adhesion, penetration, and colonization of host tissues; glucanase inhibitor protein (GIP) (complete cds) responsible by the suppression of host defense responses; necrosis-inducing Phytophthora protein 1 (NPP1) (partial cds); and transglutaminase (partial cds) which inducts defense responses and disease-like symptoms. In this mini-review, we present some scientifically advanced solutions that can contribute to the resolution of ink disease.

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

Cited by 15 publications

References 23 publications

Phytophthora cinnamomi

Phytophthora cinnamomi

Transglutaminases: recent achievements and new sources

Scientifically advanced solutions for chestnut ink disease

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