Cell walls of filamentous fungi

Rogers, H. J.; Perkins, H. R.; Ward, J. B.

doi:10.1007/978-94-011-6014-8_13

Cited by 5 publications

(4 citation statements)

References 47 publications

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“…Midguts were then thoroughly washed to remove remaining luminal contents. The presence of chitin in C. maculatus larval midgut and luminal contents was ascertained by the von Wisselingh color test (23). This qualitative test detects chitosan produced after treatment of the chitin-containing materials with saturated KOH for 15 min at 160 o C. After reaction, the presence of chitin was observed with a KI/ iodine solution.…”

Section: Chemical Test For Chitinmentioning

confidence: 99%

Vicilins (7S storage globulins) of cowpea (Vigna unguiculata) seeds bind to chitinous structures of the midgut of Callosobruchus maculatus (Coleoptera: Bruchidae) larvae

Sales

Pimenta²,

Paes

et al. 2001

Braz J Med Biol Res

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The presence of chitin in midgut structures of Callosobruchus maculatus larvae was shown by chemical and immunocytochemical methods. Detection by Western blotting of cowpea (Vigna unguiculata) seed vicilins (7S storage proteins) bound to these structures suggested that C. maculatus-susceptible vicilins presented less staining when compared to C. maculatus-resistant vicilins. Storage proteins present in the microvilli in the larval midgut of the bruchid were recognized by immunolabeling of vicilins in the appropriate sections with immunogold conjugates. These labeling sites coincided with the sites labeled by an anti-chitin antibody. These results, taken together with those previously published showing that the lower rates of hydrolysis of variant vicilins from C. maculatus-resistant seeds by the insects midgut proteinases and those showing that vicilins bind to chitin matrices, may explain the detrimental effects of variant vicilins on the development of C. maculatus larvae.

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Section: Chemical Test For Chitinmentioning

confidence: 99%

Vicilins (7S storage globulins) of cowpea (Vigna unguiculata) seeds bind to chitinous structures of the midgut of Callosobruchus maculatus (Coleoptera: Bruchidae) larvae

Sales

Pimenta²,

Paes

et al. 2001

Braz J Med Biol Res

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“…This result indicated that CgEnd3 plays a role in cell-wall integrity. The cell wall of filamentous fungi is the place of first contact with external stresses and is mainly composed of chitin [63]. S. cerevisiae End3p is required for the correct distribution of chitin at the cell surface [47].…”

Section: Cgend3 Is Required For Cell Wall Integritymentioning

confidence: 99%

CgEnd3 Regulates Endocytosis, Appressorium Formation, and Virulence in the Poplar Anthracnose Fungus Colletotrichum gloeosporioides

Wang

Tian

2021

IJMS

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The hemibiotrophic ascomycete fungus Colletotrichum gloeosporioides is the causal agent of anthracnose on numerous plants, and it causes considerable economic losses worldwide. Endocytosis is an essential cellular process in eukaryotic cells, but its roles in C. gloeosporioides remain unknown. In our study, we identified an endocytosis-related protein, CgEnd3, and knocked it out via polyethylene glycol (PEG)-mediated protoplast transformation. The lack of CgEnd3 resulted in severe defects in endocytosis. C. gloeosporioides infects its host through a specialized structure called appressorium, and ΔCgEnd3 showed deficient appressorium formation, melanization, turgor pressure accumulation, penetration ability of appressorium, cellophane membrane penetration, and pathogenicity. CgEnd3 also affected oxidant adaptation and the expression of core effectors during the early stage of infection. CgEnd3 contains one EF hand domain and four calcium ion-binding sites, and it is involved in calcium signaling. A lack of CgEnd3 changed the responses to cell-wall integrity agents and fungicide fludioxonil. However, CgEnd3 regulated appressorium formation and endocytosis in a calcium signaling-independent manner. Taken together, these results demonstrate that CgEnd3 plays pleiotropic roles in endocytosis, calcium signaling, cell-wall integrity, appressorium formation, penetration, and pathogenicity in C. gloeosporioides, and it suggests that CgEnd3 or endocytosis-related genes function as promising antifungal targets.

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“…The presence of chitin in both larval midguts was ascertained by the von Wisselingh color test [22]. Midguts were then thoroughly washed to remove remaining luminal contents.…”

Section: Detection Of Chitin In the Midgut Of Bruchid Larvaementioning

confidence: 99%

Effects of a Chitin Binding Vicilin from Erythrina velutina Seeds on Bean Bruchid Pests (Callosobruchus maculatus and Zabrotes subfasciatus)

Sales

Teixeira

Oliveira³

et al. 2008

PPL

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Erythrina velutina vicilin, EvV, is a dimeric glycoprotein with Mr of 124.6 kDa. EvV was tested for anti-insect activity against bean bruchid larvae. EvV had LD(50) of 0.10% and ED(50) of 0.14% for Z. subfasciatus and LD(50) of 0.26% and ED(50) of 0.19% for C. maculatus. EvV was not digested by bean larvae enzymes until 12 h of incubation, and at 24 h EvV was more resistant to Z. subfasciatus enzymes.

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Cell walls of filamentous fungi

Cited by 5 publications

References 47 publications

Vicilins (7S storage globulins) of cowpea (Vigna unguiculata) seeds bind to chitinous structures of the midgut of Callosobruchus maculatus (Coleoptera: Bruchidae) larvae

Vicilins (7S storage globulins) of cowpea (Vigna unguiculata) seeds bind to chitinous structures of the midgut of Callosobruchus maculatus (Coleoptera: Bruchidae) larvae

CgEnd3 Regulates Endocytosis, Appressorium Formation, and Virulence in the Poplar Anthracnose Fungus Colletotrichum gloeosporioides

Effects of a Chitin Binding Vicilin from Erythrina velutina Seeds on Bean Bruchid Pests (Callosobruchus maculatus and Zabrotes subfasciatus)

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