title: The GPI-anchored Gas and Crh families are fungal antigens.
abstract: The cell wall is the first interface between a fungus and its extracellular environment. Glycosyltransferases involved in the formation and dynamic remodelling of the polysaccharide network of the cell wall have recently been identified. The best characterized ones belong to the Gas family, which elongates beta(1,3)-glucans, and to the Crh family, which are involved in the cross-linking of chitin to beta(1,6)-glucan. All these proteins carry a glycosylphosphatidylinositol (GPI) anchor. In this work, we show that recombinant soluble forms of Gas1-5 and Crh1p from Saccharomyces cerevisiae and their orthologous proteins Gel1-Gel2 and Crf1 from Aspergillus fumigatus are specifically recognized by antibodies present in the sera of patients with Aspergillus or Candida infections. Quantification of the antibody titres against recombinant Gas/Gel and Crh/Crf proteins separated aspergilloma and candidiasis patients from non-infected individuals. Cross-reactivity was seen between the antibody response of patients with aspergillosis and candidiasis towards the Gas/Gel and Crh/Crf proteins. These results suggest that GPI-anchored cross-linking enzymes are relevant immunologically reactive constituents of the cell wall that may play a role during human fungal infections.
authors.affiliation: Departamento Microbiología II, Facultad de Farmacia, Universidad Complutense, Madrid 28040, Spain.
authors.forename: Javier
authors.initials: J
authors.lastname: Arroyo
authors.forename: Jaqueline
authors.initials: J
authors.lastname: Sarfati
authors.forename: Marie Thérése
authors.initials: MT
authors.lastname: Baixench
authors.forename: Enrico
authors.initials: E
authors.lastname: Ragni
authors.forename: Marivi
authors.initials: M
authors.lastname: Guillén
authors.forename: José Manuel
authors.initials: JM
authors.lastname: Rodriguez-Peña
authors.forename: Laura
authors.initials: L
authors.lastname: Popolo
authors.forename: Jean Paul
authors.initials: JP
authors.lastname: Latgé
mesh_terms: D000908:Antibodies, Fungal / Q000097:blood*; D000946:Antigens, Fungal / Q000276:immunology* / Q000378:metabolism; D001228:Aspergillosis / Q000175:diagnosis*; D001232:Aspergillus fumigatus / Q000737:chemistry / Q000276:immunology / Q000378:metabolism; D002177:Candidiasis / Q000175:diagnosis*; D002473:Cell Wall / Q000378:metabolism; D003429:Cross Reactions; D005656:Fungal Proteins / Q000276:immunology / Q000378:metabolism; D017261:Glycosylphosphatidylinositols / Q000276:immunology / Q000378:metabolism*; D006801:Humans; D008562:Membrane Glycoproteins / Q000276:immunology / Q000378:metabolism; D011994:Recombinant Proteins / Q000276:immunology / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000737:chemistry / Q000276:immunology / Q000378:metabolism
chemical_list: D000908:Antibodies, Fungal; D000946:Antigens, Fungal; D005656:Fungal Proteins; D017261:Glycosylphosphatidylinositols; D008562:Membrane Glycoproteins; D011994:Recombinant Proteins