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A chitin synthase with a myosin-like motor domain is essential for hyphal growth, appressorium differentiation, and pathogenicity of the maize anthracnose fungus Colletotrichum graminicola.
Mol Plant Microbe Interact 2007; 20(12):1555-67MP

Abstract

Chitin synthesis contributes to cell wall biogenesis and is essential for invasion of solid substrata and pathogenicity of filamentous fungi. In contrast to yeasts, filamentous fungi contain up to 10 chitin synthases (CHS), which might reflect overlapping functions and indicate their complex lifestyle. Previous studies have shown that a class VI CHS of the maize anthracnose fungus Colletotrichum graminicola is essential for cell wall synthesis of conidia and vegetative hyphae. Here, we report on cloning and characterization of three additional CHS genes, CgChsI, CgChsIII, and CgChsV, encoding class I, III, and V CHS, respectively. All CHS genes are expressed during vegetative and pathogenic development. DeltaCgChsI and DeltaCgChsIII mutants did not differ significantly from the wild-type isolate with respect to hyphal growth and pathogenicity. In contrast, null mutants in the CgChsV gene, which encodes a CHS with an N-terminal myosin-like motor domain, are strongly impaired in vegetative growth and pathogenicity. Even in osmotically stabilized media, vegetative hyphae of DeltaCgChsV mutants exhibited large balloon-like swellings, appressorial walls appeared to disintegrate during maturation, and infection cells were nonfunctional. Surprisingly, DeltaCgChsV mutants were able to form dome-shaped hyphopodia that exerted force and showed host cell wall penetration rates comparable with the wild type. However, infection hyphae that formed within the plant cells exhibited severe swellings and were not able to proceed with plant colonization efficiently. Consequently, DeltaCgChsV mutants did not develop macroscopically visible anthracnose disease symptoms and, thus, were nonpathogenic.

Authors+Show Affiliations

Institute of Agricultural and Nutritional Sciences, Martin-Luther-Universität-Halle-Wittenberg, Halle (Saale), Germany.No affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

17990963

Citation

Werner, Stefan, et al. "A Chitin Synthase With a Myosin-like Motor Domain Is Essential for Hyphal Growth, Appressorium Differentiation, and Pathogenicity of the Maize Anthracnose Fungus Colletotrichum Graminicola." Molecular Plant-microbe Interactions : MPMI, vol. 20, no. 12, 2007, pp. 1555-67.
Werner S, Sugui JA, Steinberg G, et al. A chitin synthase with a myosin-like motor domain is essential for hyphal growth, appressorium differentiation, and pathogenicity of the maize anthracnose fungus Colletotrichum graminicola. Mol Plant Microbe Interact. 2007;20(12):1555-67.
Werner, S., Sugui, J. A., Steinberg, G., & Deising, H. B. (2007). A chitin synthase with a myosin-like motor domain is essential for hyphal growth, appressorium differentiation, and pathogenicity of the maize anthracnose fungus Colletotrichum graminicola. Molecular Plant-microbe Interactions : MPMI, 20(12), pp. 1555-67.
Werner S, et al. A Chitin Synthase With a Myosin-like Motor Domain Is Essential for Hyphal Growth, Appressorium Differentiation, and Pathogenicity of the Maize Anthracnose Fungus Colletotrichum Graminicola. Mol Plant Microbe Interact. 2007;20(12):1555-67. PubMed PMID: 17990963.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - A chitin synthase with a myosin-like motor domain is essential for hyphal growth, appressorium differentiation, and pathogenicity of the maize anthracnose fungus Colletotrichum graminicola. AU - Werner,Stefan, AU - Sugui,Janyce A, AU - Steinberg,Gero, AU - Deising,Holger B, PY - 2007/11/10/pubmed PY - 2008/1/9/medline PY - 2007/11/10/entrez SP - 1555 EP - 67 JF - Molecular plant-microbe interactions : MPMI JO - Mol. Plant Microbe Interact. VL - 20 IS - 12 N2 - Chitin synthesis contributes to cell wall biogenesis and is essential for invasion of solid substrata and pathogenicity of filamentous fungi. In contrast to yeasts, filamentous fungi contain up to 10 chitin synthases (CHS), which might reflect overlapping functions and indicate their complex lifestyle. Previous studies have shown that a class VI CHS of the maize anthracnose fungus Colletotrichum graminicola is essential for cell wall synthesis of conidia and vegetative hyphae. Here, we report on cloning and characterization of three additional CHS genes, CgChsI, CgChsIII, and CgChsV, encoding class I, III, and V CHS, respectively. All CHS genes are expressed during vegetative and pathogenic development. DeltaCgChsI and DeltaCgChsIII mutants did not differ significantly from the wild-type isolate with respect to hyphal growth and pathogenicity. In contrast, null mutants in the CgChsV gene, which encodes a CHS with an N-terminal myosin-like motor domain, are strongly impaired in vegetative growth and pathogenicity. Even in osmotically stabilized media, vegetative hyphae of DeltaCgChsV mutants exhibited large balloon-like swellings, appressorial walls appeared to disintegrate during maturation, and infection cells were nonfunctional. Surprisingly, DeltaCgChsV mutants were able to form dome-shaped hyphopodia that exerted force and showed host cell wall penetration rates comparable with the wild type. However, infection hyphae that formed within the plant cells exhibited severe swellings and were not able to proceed with plant colonization efficiently. Consequently, DeltaCgChsV mutants did not develop macroscopically visible anthracnose disease symptoms and, thus, were nonpathogenic. SN - 0894-0282 UR - https://www.unboundmedicine.com/medline/citation/17990963/A_chitin_synthase_with_a_myosin_like_motor_domain_is_essential_for_hyphal_growth_appressorium_differentiation_and_pathogenicity_of_the_maize_anthracnose_fungus_Colletotrichum_graminicola_ L2 - http://apsjournals.apsnet.org/doi/full/10.1094/MPMI-20-12-1555?url_ver=Z39.88-2003&rfr_id=ori:rid:crossref.org&rfr_dat=cr_pub=pubmed DB - PRIME DP - Unbound Medicine ER -