Matches in SemOpenAlex for { <https://semopenalex.org/work/W2980900448> ?p ?o ?g. }
- W2980900448 abstract "ABSTRACT The pathogenic fungus Aspergillus fumigatus contains galactomannans localized on the surface layer of its cell walls, which are involved in various biological processes. Galactomannans comprise α-(1→2)-/α-(1→6)-mannan and β-(1→5)-/β-(1→6)-galactofuranosyl chains. We previously revealed that GfsA is a β-galactofuranoside β-(1→5)-galactofuranosyltransferase involved in the biosynthesis of β-(1→5)-galactofuranosyl chains. Here, we clarified the entire biosynthesis of β-(1→5)-galactofuranosyl chains in A. fumigatgus . Two paralogs exist within A. fumigatus : GfsB and GfsC. We show that GfsB and GfsC, in addition to GfsA, are β-galactofuranoside β-(1→5)-galactofuranosyltransferases by biochemical and genetic analyses. GfsA, GfsB, and GfsC can synthesize β-(1→5)-galactofuranosyl oligomers up to lengths of 7, 3, and 5 galactofuranoses within an established in vitro highly efficient assay of galactofuranosyltransferase activity. Structural analyses of galactomannans extracted from the strains Δ gfsB , Δ gfsC , Δ gfsAC , and Δ gfsABC revealed that GfsA and GfsC synthesized all β-(1→5)-galactofuranosyl residues of fungal-type and O-mannose-type galactomannans, and GfsB exhibited limited function in A. fumigatus . The loss of β-(1→5)-galactofuranosyl residues decreased the hyphal growth rate and conidia formation ability as well as increased the abnormal hyphal branching structure and cell surface hydrophobicity, but this loss is dispensable for sensitivity to antifungal agents and virulence toward immune-compromised mice. IMPORTANCE β-(1→5)-galactofuranosyl residues are widely distributed in the subphylum Pezisomycotina of the phylum Ascomycota. Pezizomycotina includes many plant and animal pathogens. Although the structure of β-(1→5)-galactofuranosyl residues of galactomannans in filamentous fungi was discovered long ago, it remains unclear which enzyme is responsible for biosynthesis of this glycan. Fungal cell wall formation processes are complicated, and information concerning glycosyltransferases is essential for their understanding. In this study, we show that GfsA and GfsC are responsible for the biosynthesis of all β-(1→5)-galactofuranosyl residues of fungal-type and O-mannose-type galactomannans. The data presented here indicates that β-(1→5)-galactofuranosyl residues are involved in cell growth, conidiation, polarity, and cell surface hydrophobicity. Our new understanding of β-(1→5)-galactofuranosyl residue biosynthesis provides important novel insights into the formation of the complex cell wall structure and the virulence of the subphylum Pezisomycotina." @default.
- W2980900448 created "2019-10-25" @default.
- W2980900448 creator A5001004472 @default.
- W2980900448 creator A5001574989 @default.
- W2980900448 creator A5004195138 @default.
- W2980900448 creator A5033652060 @default.
- W2980900448 creator A5038736012 @default.
- W2980900448 creator A5054763025 @default.
- W2980900448 creator A5060790153 @default.
- W2980900448 creator A5066762322 @default.
- W2980900448 creator A5068981167 @default.
- W2980900448 creator A5077043379 @default.
- W2980900448 date "2019-10-22" @default.
- W2980900448 modified "2023-09-27" @default.
- W2980900448 title "Biosynthesis of β-(1→5)-Galactofuranosyl Chains of Fungal-Type and O-Mannose-Type Galactomannans within the Invasive PathogenAspergillus fumigatus" @default.
- W2980900448 cites W1824560409 @default.
- W2980900448 cites W1918970836 @default.
- W2980900448 cites W1931368951 @default.
- W2980900448 cites W1957834542 @default.
- W2980900448 cites W1970743288 @default.
- W2980900448 cites W1976467821 @default.
- W2980900448 cites W1977207628 @default.
- W2980900448 cites W1997570099 @default.
- W2980900448 cites W2004015922 @default.
- W2980900448 cites W2011664991 @default.
- W2980900448 cites W2017824703 @default.
- W2980900448 cites W2027532372 @default.
- W2980900448 cites W2036102170 @default.
- W2980900448 cites W2039722369 @default.
- W2980900448 cites W2041978464 @default.
- W2980900448 cites W2042396499 @default.
- W2980900448 cites W2047195096 @default.
- W2980900448 cites W2049894993 @default.
- W2980900448 cites W2078865302 @default.
- W2980900448 cites W2089254735 @default.
- W2980900448 cites W2094626050 @default.
- W2980900448 cites W2096209592 @default.
- W2980900448 cites W2099905667 @default.
- W2980900448 cites W2112293062 @default.
- W2980900448 cites W2124681021 @default.
- W2980900448 cites W2125243075 @default.
- W2980900448 cites W2133858145 @default.
- W2980900448 cites W2137553641 @default.
- W2980900448 cites W2147189708 @default.
- W2980900448 cites W2152386381 @default.
- W2980900448 cites W2329114494 @default.
- W2980900448 cites W2335347037 @default.
- W2980900448 cites W2569875961 @default.
- W2980900448 cites W2598091503 @default.
- W2980900448 cites W2605030089 @default.
- W2980900448 cites W2614664430 @default.
- W2980900448 cites W2783905495 @default.
- W2980900448 cites W2901017189 @default.
- W2980900448 cites W2909746928 @default.
- W2980900448 cites W2966043041 @default.
- W2980900448 cites W2971865815 @default.
- W2980900448 doi "https://doi.org/10.1101/814756" @default.
- W2980900448 hasPublicationYear "2019" @default.
- W2980900448 type Work @default.
- W2980900448 sameAs 2980900448 @default.
- W2980900448 citedByCount "0" @default.
- W2980900448 crossrefType "posted-content" @default.
- W2980900448 hasAuthorship W2980900448A5001004472 @default.
- W2980900448 hasAuthorship W2980900448A5001574989 @default.
- W2980900448 hasAuthorship W2980900448A5004195138 @default.
- W2980900448 hasAuthorship W2980900448A5033652060 @default.
- W2980900448 hasAuthorship W2980900448A5038736012 @default.
- W2980900448 hasAuthorship W2980900448A5054763025 @default.
- W2980900448 hasAuthorship W2980900448A5060790153 @default.
- W2980900448 hasAuthorship W2980900448A5066762322 @default.
- W2980900448 hasAuthorship W2980900448A5068981167 @default.
- W2980900448 hasAuthorship W2980900448A5077043379 @default.
- W2980900448 hasBestOaLocation W29809004481 @default.
- W2980900448 hasConcept C100817775 @default.
- W2980900448 hasConcept C125235067 @default.
- W2980900448 hasConcept C181199279 @default.
- W2980900448 hasConcept C185592680 @default.
- W2980900448 hasConcept C2775887612 @default.
- W2980900448 hasConcept C2779678110 @default.
- W2980900448 hasConcept C2779719659 @default.
- W2980900448 hasConcept C2779787849 @default.
- W2980900448 hasConcept C553450214 @default.
- W2980900448 hasConcept C55493867 @default.
- W2980900448 hasConcept C59822182 @default.
- W2980900448 hasConcept C86803240 @default.
- W2980900448 hasConcept C89423630 @default.
- W2980900448 hasConcept C90080823 @default.
- W2980900448 hasConceptScore W2980900448C100817775 @default.
- W2980900448 hasConceptScore W2980900448C125235067 @default.
- W2980900448 hasConceptScore W2980900448C181199279 @default.
- W2980900448 hasConceptScore W2980900448C185592680 @default.
- W2980900448 hasConceptScore W2980900448C2775887612 @default.
- W2980900448 hasConceptScore W2980900448C2779678110 @default.
- W2980900448 hasConceptScore W2980900448C2779719659 @default.
- W2980900448 hasConceptScore W2980900448C2779787849 @default.
- W2980900448 hasConceptScore W2980900448C553450214 @default.
- W2980900448 hasConceptScore W2980900448C55493867 @default.
- W2980900448 hasConceptScore W2980900448C59822182 @default.
- W2980900448 hasConceptScore W2980900448C86803240 @default.
- W2980900448 hasConceptScore W2980900448C89423630 @default.