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Chitinase

About: Chitinase is a research topic. Over the lifetime, 4690 publications have been published within this topic receiving 161786 citations. The topic is also known as: 1,4-beta-poly-N-acetylglucosaminidase & poly-beta-glucosaminidase.


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Journal ArticleDOI
TL;DR: Serum anti-CHIT30 specifically detected this chitinase amongst five isoenzymes shown in glycol-chitin activity gels, which was produced at tick cuticle during fungal infection.

78 citations

Journal ArticleDOI
TL;DR: The results reported herein demonstrate specific interactions between gene products of the host and pathogen and establish the need to consider fungal proteins that inhibit plant endo-β-1,3-glucanases when attempting to use the genes encoding endosaccharides to engineer resistance to fungi in transgenic plants.
Abstract: Plant endo-β-1,3-glucanases and chitinases inhibit the growth of some fungi and generate elicitor-active oligosaccharides while depolymerizing polysaccharides of mycelial walls. Overexpression of the endo-β-1,3-glucanases and/ or chitinases in transgenic plants provides, in some cases, increased protection against fungal pathogens. However, most of the phytopathogenic fungi that have been tested in vitro are resistant to endo-β-1,3-glucanases and chitinases. Furthermore, some phytopathogenic fungi whose growth is inhibited by these enzymes are able to overcome the effect of these enzymes over a period of hours, indicating an ability of those fungi to adapt to the enzymes. Evidence is presented indicating that fungal pathogens secrete proteins that inhibit selective plant endo-β-1,3-glucanases.A glucanase inhibitor protein (GIP-1) has been purified to homogeneity from the culture fluid of the fungal pathogen of soybeans, Phytophthora sojae f. sp. glycines (Psg), and two basic pathogenesis-related endo-β-1,3-glucanases (EnGLsoy-A and EnGLsoy-B) have been purified from soybean seedlings. GIP-1 inhibits EnGLsoy-A but not EnGLsoy-B. Moreover, GIP-1 does not inhibit endo-β-1,3-glucanases secreted by Psg itself nor does GIP-1 inhibit PR-2c, a pathogenesis-related endo-β-1,3-glucanase of tobacco. Evidence is presented that Psg secretes other GIPs that inhibit other endo-β-1,3-glucanase(s) of soybean. Furthermore, GIP-1 does not exhibit proteolytic activity but does appear to physically bind to EnGLsoy-A. The results reported herein demonstrate specific interactions between gene products of the host and pathogen and establish the need to consider fungal proteins that inhibit plant endo-β-1,3-glucanases when attempting to use the genes encoding endo-β-1,3-glucanases to engineer resistance to fungi in transgenic plants.

78 citations

Journal ArticleDOI
TL;DR: Chitinase A produced by Bacillus thuringiensis subsp.

78 citations

Journal ArticleDOI
TL;DR: This study showed that S. goshikiensis YCXU could be a potential biocontrol agent for controlling watermelon Fusarium wilt disease.

78 citations

Journal ArticleDOI
TL;DR: It is hypothesized that the chitin product of Chs3 forms a scaffold essential for normal externalization of melanosomes, while the Chs8 chit in product, probably produced in cell walls in greater quantity in the absence of CHS2, impedes externalization.
Abstract: The fungal pathogen Candida albicans produces dark-pigmented melanin after 3 to 4 days of incubation in medium containing l-3,4-dihydroxyphenylalanine (l-DOPA) as a substrate. Expression profiling of C. albicans revealed very few genes significantly up- or downregulated by growth in l-DOPA. We were unable to determine a possible role for melanin in the virulence of C. albicans. However, we showed that melanin was externalized from the fungal cells in the form of electron-dense melanosomes that were free or often loosely bound to the cell wall exterior. Melanin production was boosted by the addition of N-acetylglucosamine to the medium, indicating a possible association between melanin production and chitin synthesis. Melanin externalization was blocked in a mutant specifically disrupted in the chitin synthase-encoding gene CHS2. Melanosomes remained within the outermost cell wall layers in chs3Delta and chs2Delta chs3Delta mutants but were fully externalized in chs8Delta and chs2Delta chs8Delta mutants. All the CHS mutants synthesized dark pigment at equivalent rates from mixed membrane fractions in vitro, suggesting it was the form of chitin structure produced by the enzymes, not the enzymes themselves, that was involved in the melanin externalization process. Mutants with single and double disruptions of the chitinase genes CHT2 and CHT3 and the chitin pathway regulator ECM33 also showed impaired melanin externalization. We hypothesize that the chitin product of Chs3 forms a scaffold essential for normal externalization of melanosomes, while the Chs8 chitin product, probably produced in cell walls in greater quantity in the absence of CHS2, impedes externalization.

78 citations


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Performance
Metrics
No. of papers in the topic in previous years
YearPapers
2023186
2022337
2021148
2020172
2019154
2018152