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 in | Yeast (Chichester, England) Vol. 24; no. 4; pp. 289 - 296 |
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Main Authors | , , , , , , , |
Format | Journal Article |
Language | English |
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. |
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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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BackLink | https://www.ncbi.nlm.nih.gov/pubmed/17397107$$D View this record in MEDLINE/PubMed |
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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 |
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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 |
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