ArticleNature communications2019
Mechanisms of redundancy and specificity of the Aspergillus fumigatus Crh transglycosylases.
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 41 citations in OpenAlex.
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- Comprehensive phenotypic analysis of multiple gene deletions of α-glucan synthase and Crh-transglycosylase gene families inCell surface (Amsterdam, Netherlands) · 2025Article
- Glycoside Hydrolase Family 16 Enzyme RsEG146 From Rhizoctonia solani AG1 IA Induces Cell Death and Triggers Defence Response in Nicotiana tabacum.Molecular plant pathology · 2025Article
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- In silico characterization of molecular factors involved in metabolism and pathogenicity of Phytophthora cinnamomi.Molecular biology reports · 2022Review
- Cryogenian Origin and Subsequent Diversification of the Plant Cell-Wall Enzyme XTH Family.Plant & cell physiology · 2021Article
- Diatomaceous earth/zinc oxide micro-composite assisted antibiotics in fungal therapy.Nano convergence · 2021Article
- Article
- The putative polysaccharide synthase AfCps1 regulates Aspergillus fumigatus morphogenesis and conidia immune response in mouse bone marrow-derived macrophages.Journal of microbiology (Seoul, Korea) · 2021Article
- A seven-membered cell wall related transglycosylase gene family inCell surface (Amsterdam, Netherlands) · 2020Article
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Authors and funding
9 authors at 5 institutions in 4 countries.
Funding
Abstract
Fungal cell wall synthesis is achieved by a balance of glycosyltransferase, hydrolase and transglycosylase activities. Transglycosylases strengthen the cell wall by forming a rigid network of crosslinks through mechanisms that remain to be explored. Here we study the function of the Aspergillus fumigatus family of five Crh transglycosylases. Although crh genes are dispensable for cell viability, simultaneous deletion of all genes renders cells sensitive to cell wall interfering compounds. In vitro biochemical assays and localisation studies demonstrate that this family of enzymes functions redundantly as transglycosylases for both chitin-glucan and chitin-chitin cell wall crosslinks. To understand the molecular basis of this acceptor promiscuity, we solved the crystal structure of A. fumigatus Crh5 (AfCrh5) in complex with a chitooligosaccharide at the resolution of 2.8 Å, revealing an extensive elongated binding cleft for the donor (-4 to -1) substrate and a short acceptor (+1 to +2) binding site. Together with mutagenesis, the structure suggests a "hydrolysis product assisted" molecular mechanism favouring transglycosylation over hydrolysis.
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