The GPI‐anchored Gas and Crh families are fungal antigens

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 el...

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Published inYeast (Chichester, England) Vol. 24; no. 4; pp. 289 - 296
Main Authors Arroyo, Javier, Sarfati, Jaqueline, Baixench, Marie Thérése, Ragni, Enrico, Guillén, Marivi, Rodriguez‐Peña, José Manuel, Popolo, Laura, Latgé, Jean Paul
Format Journal Article
LanguageEnglish
Published Chichester, UK John Wiley & Sons, Ltd 01.04.2007
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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 β(1,3)‐glucans, and to the Crh family, which are involved in the cross‐linking of chitin to β(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. Copyright © 2007 John Wiley & Sons, Ltd.
AbstractList 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 β(1,3)‐glucans, and to the Crh family, which are involved in the cross‐linking of chitin to β(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. Copyright © 2007 John Wiley & Sons, Ltd.
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.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.
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 β(1,3)‐glucans, and to the Crh family, which are involved in the cross‐linking of chitin to β(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. Copyright © 2007 John Wiley & Sons, Ltd.
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.
Author Popolo, Laura
Rodriguez‐Peña, José Manuel
Baixench, Marie Thérése
Latgé, Jean Paul
Sarfati, Jaqueline
Ragni, Enrico
Guillén, Marivi
Arroyo, Javier
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Cites_doi 10.1128/IAI.71.6.3010-3019.2003
10.1016/j.femsim.2004.03.012
10.1042/0264-6021:3470741
10.1038/nri1255
10.1016/S0304-4165(98)00138-X
10.1016/S0166-6851(99)00178-4
10.1046/j.1365-2222.2001.01076.x
10.1111/j.1432-1033.2004.04297.x
10.1084/jem.20011433
10.1016/j.diagmicrobio.2006.02.002
10.1074/jbc.M500334200
10.2174/1386207033329751
10.1074/jbc.275.20.14882
10.1111/j.1365-2958.2006.05565.x
10.1128/CMR.12.2.310
10.1242/jcs.115.12.2549
10.1128/MCB.20.9.3245-3255.2000
10.1159/000053664
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References 2001; 124
1993; 24
2004; 41
2005; 280
2002; 195
2000; 105
2006; 55
2003; 6
2000a; 275
1999; 1426
2004; 271
2000; 20
2004; 4
1999; 12
2002; 115
2007; 63
2000b; 347
2003; 71
2001; 31
Latgé JP (e_1_2_5_11_1) 1993; 24
e_1_2_5_15_1
e_1_2_5_14_1
e_1_2_5_9_1
e_1_2_5_16_1
e_1_2_5_8_1
e_1_2_5_7_1
e_1_2_5_10_1
e_1_2_5_6_1
e_1_2_5_13_1
e_1_2_5_5_1
e_1_2_5_12_1
e_1_2_5_4_1
e_1_2_5_3_1
e_1_2_5_2_1
e_1_2_5_19_1
e_1_2_5_18_1
Rodriguez‐Pena JM (e_1_2_5_17_1) 2002; 115
e_1_2_5_20_1
References_xml – volume: 115
  start-page: 2549
  year: 2002
  end-page: 2558
  article-title: Mechanisms for targeting of the GPI‐anchored cell wall protein Crh2p to polarized growth sites
  publication-title: J Cell Sci
– volume: 20
  start-page: 3245
  year: 2000
  end-page: 3255
  article-title: A novel family of cell wall‐related proteins regulated differently during the yeast life cycle
  publication-title: Mol Cell Biol
– volume: 124
  start-page: 43
  year: 2001
  end-page: 47
  article-title: Tapping allergen repertoires by advanced cloning technologies
  publication-title: Int Arch Allergy Immunol
– volume: 71
  start-page: 3010
  year: 2003
  end-page: 3019
  article-title: A recombinant β1,3‐glucanosyltransferase homolog of protects mice against coccidioidomycosis
  publication-title: Infect Immun
– volume: 195
  start-page: 401
  year: 2002
  end-page: 413
  article-title: A small surface molecule provides the first immunological evidence that Chagas' disease is due to a single parasite lineage
  publication-title: J Exp Med
– volume: 1426
  start-page: 385
  year: 1999
  end-page: 400
  article-title: The Gas1 glycoprotein, a putative wall polymer cross‐linker
  publication-title: Biochim Biophys Acta
– volume: 271
  start-page: 3635
  year: 2004
  end-page: 3645
  article-title: Characterization of recombinant forms of the yeast Gas1 protein and identification of residues essential for glucanosyltransferase activity and folding
  publication-title: Eur J Biochem
– volume: 280
  start-page: 20894
  year: 2005
  end-page: 20901
  article-title: Comprehensive proteomic analysis of cell walls: identification of proteins covalently attached via glycosylphosphatidylinositol remnants or mild alkali‐sensitive linkages
  publication-title: J Biol Chem
– volume: 31
  start-page: 761
  year: 2001
  end-page: 770
  article-title: Cloning and expression of allergen Asp f 16 mediating both humoral and cell‐mediated immunity in allergic bronchopulmonary aspergillosis (ABPA)
  publication-title: Clin Exp Allergy
– volume: 4
  start-page: 1
  year: 2004
  end-page: 23
  article-title: Immunity to fungal infections
  publication-title: Nat Rev Immunol
– volume: 63
  start-page: 921
  year: 2007
  end-page: 935
  article-title: Crh1p and Crh2p are required for the cross‐linking of chitin to β(1–6)glucan in the cell wall
  publication-title: Mol. Microbiol
– volume: 105
  start-page: 137
  year: 2000
  end-page: 147
  article-title: Characterization of the merozoite surface protein 4/5 gene of and
  publication-title: Mol Biochem Parasitol
– volume: 6
  start-page: 147
  year: 2003
  end-page: 154
  article-title: Rapid identification of allergen‐encoding cDNA clones by phage display and high‐density arrays
  publication-title: Comb Chem High Throughput Screen
– volume: 55
  start-page: 279
  year: 2006
  end-page: 291
  article-title: Recombinant antigens as diagnostic markers for aspergillosis
  publication-title: Diagn Microbiol Infect Dis
– volume: 12
  start-page: 310
  year: 1999
  end-page: 350
  article-title: and aspergillosis
  publication-title: Clin Microbiol Rev
– volume: 24
  start-page: 269
  year: 1993
  end-page: 274
  article-title: Cell wall antigens in
  publication-title: Arch Med Res
– volume: 275
  start-page: 14882
  year: 2000a
  end-page: 14889
  article-title: GPI‐anchored glucanosyltransferases play an active role in the biosynthesis of the fungal cell wall
  publication-title: J Biol Chem
– volume: 347
  start-page: 741
  year: 2000b
  end-page: 747
  article-title: Identification of the catalytic residues of the first family of β(1–3) glucanosyltransferases identified in fungi
  publication-title: Biochem J
– volume: 41
  start-page: 187
  year: 2004
  end-page: 196
  article-title: Antibody response to cell wall antigens
  publication-title: FEMS Immunol Med Microbiol
– ident: e_1_2_5_6_1
  doi: 10.1128/IAI.71.6.3010-3019.2003
– ident: e_1_2_5_12_1
  doi: 10.1016/j.femsim.2004.03.012
– ident: e_1_2_5_14_1
  doi: 10.1042/0264-6021:3470741
– ident: e_1_2_5_18_1
  doi: 10.1038/nri1255
– volume: 24
  start-page: 269
  year: 1993
  ident: e_1_2_5_11_1
  article-title: Cell wall antigens in Aspergillus fumigatus
  publication-title: Arch Med Res
– ident: e_1_2_5_15_1
  doi: 10.1016/S0304-4165(98)00138-X
– ident: e_1_2_5_8_1
  doi: 10.1016/S0166-6851(99)00178-4
– ident: e_1_2_5_2_1
  doi: 10.1046/j.1365-2222.2001.01076.x
– ident: e_1_2_5_4_1
  doi: 10.1111/j.1432-1033.2004.04297.x
– ident: e_1_2_5_7_1
  doi: 10.1084/jem.20011433
– ident: e_1_2_5_19_1
  doi: 10.1016/j.diagmicrobio.2006.02.002
– ident: e_1_2_5_20_1
  doi: 10.1074/jbc.M500334200
– ident: e_1_2_5_9_1
  doi: 10.2174/1386207033329751
– ident: e_1_2_5_13_1
  doi: 10.1074/jbc.275.20.14882
– ident: e_1_2_5_3_1
  doi: 10.1111/j.1365-2958.2006.05565.x
– ident: e_1_2_5_10_1
  doi: 10.1128/CMR.12.2.310
– volume: 115
  start-page: 2549
  year: 2002
  ident: e_1_2_5_17_1
  article-title: Mechanisms for targeting of the Saccharomyces cerevisiae GPI‐anchored cell wall protein Crh2p to polarized growth sites
  publication-title: J Cell Sci
  doi: 10.1242/jcs.115.12.2549
– ident: e_1_2_5_16_1
  doi: 10.1128/MCB.20.9.3245-3255.2000
– ident: e_1_2_5_5_1
  doi: 10.1159/000053664
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Snippet The cell wall is the first interface between a fungus and its extracellular environment. Glycosyltransferases involved in the formation and dynamic remodelling...
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SubjectTerms Antibodies, Fungal - blood
Antigens, Fungal - immunology
Antigens, Fungal - metabolism
Aspergillosis - diagnosis
aspergillus
Aspergillus fumigatus - chemistry
Aspergillus fumigatus - immunology
Aspergillus fumigatus - metabolism
candida
Candidiasis - diagnosis
Cell Wall - metabolism
Cross Reactions
diagnosis
Fungal Proteins - immunology
Fungal Proteins - metabolism
Glycosylphosphatidylinositols - immunology
Glycosylphosphatidylinositols - metabolism
glycosyltransferase
GPI
Humans
Membrane Glycoproteins - immunology
Membrane Glycoproteins - metabolism
Recombinant Proteins - immunology
Recombinant Proteins - metabolism
Saccharomyces cerevisiae - chemistry
Saccharomyces cerevisiae - immunology
Saccharomyces cerevisiae - metabolism
Title The GPI‐anchored Gas and Crh families are fungal antigens
URI https://onlinelibrary.wiley.com/doi/abs/10.1002%2Fyea.1480
https://www.ncbi.nlm.nih.gov/pubmed/17397107
https://www.proquest.com/docview/70367257
Volume 24
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