Assembly and disassembly of Aspergillus fumigatus conidial rodlets
The rodlet structure present on the Aspergillus fumigatus conidial surface hides conidia from immune recognition. In spite of the essential biological role of the rodlets, the molecular basis for their self-assembly and disaggregation is not known. Analysis of the soluble forms of conidia-extracted...
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Format: | Article |
Language: | English |
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Elsevier
2019-12-01
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Series: | The Cell Surface |
Online Access: | http://www.sciencedirect.com/science/article/pii/S2468233018300227 |
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doaj-9aea5c49822e42faa2daaf32f00647a5 |
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record_format |
Article |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Isabel Valsecchi Jennifer I. Lai Emmanuel Stephen-Victor Ariane Pillé Audrey Beaussart Victor Lo Chi L.L. Pham Vishukumar Aimanianda Ann H. Kwan Magalie Duchateau Quentin Giai Gianetto Mariette Matondo Melanie Lehoux Donald C. Sheppard Yves F. Dufrene Jagadeesh Bayry J. Iñaki Guijarro Margaret Sunde Jean-Paul Latgé |
spellingShingle |
Isabel Valsecchi Jennifer I. Lai Emmanuel Stephen-Victor Ariane Pillé Audrey Beaussart Victor Lo Chi L.L. Pham Vishukumar Aimanianda Ann H. Kwan Magalie Duchateau Quentin Giai Gianetto Mariette Matondo Melanie Lehoux Donald C. Sheppard Yves F. Dufrene Jagadeesh Bayry J. Iñaki Guijarro Margaret Sunde Jean-Paul Latgé Assembly and disassembly of Aspergillus fumigatus conidial rodlets The Cell Surface |
author_facet |
Isabel Valsecchi Jennifer I. Lai Emmanuel Stephen-Victor Ariane Pillé Audrey Beaussart Victor Lo Chi L.L. Pham Vishukumar Aimanianda Ann H. Kwan Magalie Duchateau Quentin Giai Gianetto Mariette Matondo Melanie Lehoux Donald C. Sheppard Yves F. Dufrene Jagadeesh Bayry J. Iñaki Guijarro Margaret Sunde Jean-Paul Latgé |
author_sort |
Isabel Valsecchi |
title |
Assembly and disassembly of Aspergillus fumigatus conidial rodlets |
title_short |
Assembly and disassembly of Aspergillus fumigatus conidial rodlets |
title_full |
Assembly and disassembly of Aspergillus fumigatus conidial rodlets |
title_fullStr |
Assembly and disassembly of Aspergillus fumigatus conidial rodlets |
title_full_unstemmed |
Assembly and disassembly of Aspergillus fumigatus conidial rodlets |
title_sort |
assembly and disassembly of aspergillus fumigatus conidial rodlets |
publisher |
Elsevier |
series |
The Cell Surface |
issn |
2468-2330 |
publishDate |
2019-12-01 |
description |
The rodlet structure present on the Aspergillus fumigatus conidial surface hides conidia from immune recognition. In spite of the essential biological role of the rodlets, the molecular basis for their self-assembly and disaggregation is not known. Analysis of the soluble forms of conidia-extracted and recombinant RodA by NMR spectroscopy has indicated the importance of disulfide bonds and identified two dynamic regions as likely candidates for conformational change and intermolecular interactions during conversion of RodA into the amyloid rodlet structure. Point mutations introduced into the RODA sequence confirmed that (1) mutation of a single cysteine was sufficient to block rodlet formation on the conidial surface and (2) both presumed amyloidogenic regions were needed for proper rodlet assembly. Mutations in the two putative amyloidogenic regions retarded and disturbed, but did not completely inhibit, the formation of the rodlets in vitro and on the conidial surface. Even in a disturbed form, the presence of rodlets on the surface of the conidia was sufficient to immunosilence the conidium. However, in contrast to the parental conidia, long exposure of mutant conidia lacking disulfide bridges within RodA or expressing RodA carrying the double (I115S/I146G) mutation activated dendritic cells with the subsequent secretion of proinflammatory cytokines. The immune reactivity of the RodA mutant conidia was not due to a modification in the RodA structure, but to the exposure of different pathogen-associated molecular patterns on the surface as a result of the modification of the rodlet surface layer. The full degradation of the rodlet layer, which occurs during early germination, is due to a complex array of cell wall bound proteases. As reported earlier, this loss of the rodlet layer lead to a strong anti-fumigatus host immune response in mouse lungs. Keywords: Aspergillus fumigatus, Hydrophobins, Rodlets, RodA, Amyloids |
url |
http://www.sciencedirect.com/science/article/pii/S2468233018300227 |
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doaj-9aea5c49822e42faa2daaf32f00647a52020-11-25T03:31:50ZengElsevierThe Cell Surface2468-23302019-12-015Assembly and disassembly of Aspergillus fumigatus conidial rodletsIsabel Valsecchi0Jennifer I. Lai1Emmanuel Stephen-Victor2Ariane Pillé3Audrey Beaussart4Victor Lo5Chi L.L. Pham6Vishukumar Aimanianda7Ann H. Kwan8Magalie Duchateau9Quentin Giai Gianetto10Mariette Matondo11Melanie Lehoux12Donald C. Sheppard13Yves F. Dufrene14Jagadeesh Bayry15J. Iñaki Guijarro16Margaret Sunde17Jean-Paul Latgé18Unité des Aspergillus, Institut Pasteur, Paris, France; Biological NMR Technological Platform, Institut Pasteur, CNRS UMR 3528, Paris, FranceSchool of Medical Sciences and Sydney Nano, The University of Sydney, NSW 2006, AustraliaInstitut National de la Santé et de la Recherche Médicale, Centre de Recherche des Cordeliers, Sorbonne Université, Paris, FranceBiological NMR Technological Platform, Institut Pasteur, CNRS UMR 3528, Paris, FranceInstitute of Life Sciences, Université Catholique de Louvain, Croix du Sud, 4-5, bte L7.07.06, B-1348 Louvain-la-Neuve, Belgium; Walloon Excellence in Life Sciences and Biotechnology, BelgiumSchool of Medical Sciences and Sydney Nano, The University of Sydney, NSW 2006, AustraliaSchool of Medical Sciences and Sydney Nano, The University of Sydney, NSW 2006, AustraliaUnité des Aspergillus, Institut Pasteur, Paris, FranceSchool of Life and Environmental Sciences and Sydney Nano, The University of Sydney, NSW 2006, AustraliaPasteur Proteomics Platform, Mass Spectrometry for Biology Unit, Institut Pasteur, CNRS USR 2000, Paris, FrancePasteur Proteomics Platform, Mass Spectrometry for Biology Unit, Institut Pasteur, CNRS USR 2000, Paris, France; Bioinformatics and Biostatistics Hub, C3BI, CNRS USR 3756, Institut Pasteur, Paris, FrancePasteur Proteomics Platform, Mass Spectrometry for Biology Unit, Institut Pasteur, CNRS USR 2000, Paris, FranceDepartments of Medicine, Microbiology and Immunology, McGill University, Montréal, QC, CanadaDepartments of Medicine, Microbiology and Immunology, McGill University, Montréal, QC, CanadaInstitute of Life Sciences, Université Catholique de Louvain, Croix du Sud, 4-5, bte L7.07.06, B-1348 Louvain-la-Neuve, Belgium; Walloon Excellence in Life Sciences and Biotechnology, BelgiumInstitut National de la Santé et de la Recherche Médicale, Centre de Recherche des Cordeliers, Sorbonne Université, Paris, FranceBiological NMR Technological Platform, Institut Pasteur, CNRS UMR 3528, Paris, FranceSchool of Medical Sciences and Sydney Nano, The University of Sydney, NSW 2006, AustraliaUnité des Aspergillus, Institut Pasteur, Paris, FranceThe rodlet structure present on the Aspergillus fumigatus conidial surface hides conidia from immune recognition. In spite of the essential biological role of the rodlets, the molecular basis for their self-assembly and disaggregation is not known. Analysis of the soluble forms of conidia-extracted and recombinant RodA by NMR spectroscopy has indicated the importance of disulfide bonds and identified two dynamic regions as likely candidates for conformational change and intermolecular interactions during conversion of RodA into the amyloid rodlet structure. Point mutations introduced into the RODA sequence confirmed that (1) mutation of a single cysteine was sufficient to block rodlet formation on the conidial surface and (2) both presumed amyloidogenic regions were needed for proper rodlet assembly. Mutations in the two putative amyloidogenic regions retarded and disturbed, but did not completely inhibit, the formation of the rodlets in vitro and on the conidial surface. Even in a disturbed form, the presence of rodlets on the surface of the conidia was sufficient to immunosilence the conidium. However, in contrast to the parental conidia, long exposure of mutant conidia lacking disulfide bridges within RodA or expressing RodA carrying the double (I115S/I146G) mutation activated dendritic cells with the subsequent secretion of proinflammatory cytokines. The immune reactivity of the RodA mutant conidia was not due to a modification in the RodA structure, but to the exposure of different pathogen-associated molecular patterns on the surface as a result of the modification of the rodlet surface layer. The full degradation of the rodlet layer, which occurs during early germination, is due to a complex array of cell wall bound proteases. As reported earlier, this loss of the rodlet layer lead to a strong anti-fumigatus host immune response in mouse lungs. Keywords: Aspergillus fumigatus, Hydrophobins, Rodlets, RodA, Amyloidshttp://www.sciencedirect.com/science/article/pii/S2468233018300227 |