A novel class of Candida glabrata cell wall proteins with β-helix fold mediates adhesion in clinical isolates
Candida glabrata is an opportunistic pathogenic yeast frequently causing infections in humans. Though it lacks typical virulence factors such as hyphal development, C. glabrata contains a remarkably large and diverse set of putative wall adhesins that is crucial for its success as pathogen. Here, we...
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| Veröffentlicht in: | PLoS pathogens 2021-12, Vol.17 (12), p.e1009980-e1009980 |
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| creator | Reithofer, Viktoria Fernández-Pereira, Jordan Alvarado, María de Groot, Piet Essen, Lars-Oliver |
| description | Candida glabrata is an opportunistic pathogenic yeast frequently causing infections in humans. Though it lacks typical virulence factors such as hyphal development, C. glabrata contains a remarkably large and diverse set of putative wall adhesins that is crucial for its success as pathogen. Here, we present an analysis of putative adhesins from the homology clusters V and VI. First, sequence similarity network analysis revealed relationships between cluster V and VI adhesins and S. cerevisiae haze protective factors (Hpf). Crystal structures of A-regions from cluster VI adhesins Awp1 and Awp3b reveal a parallel right-handed β-helix domain that is linked to a C-terminal β-sandwich. Structure solution of the A-region of Awp3b via single wavelength anomalous diffraction phasing revealed the largest known lanthanide cluster with 21 Gd3+ ions. Awp1-A and Awp3b-A show structural similarity to pectate lyases but binding to neither carbohydrates nor Ca2+ was observed. Phenotypic analysis of awp1Δ, awp3Δ, and awp1,3Δ double mutants did also not confirm their role as adhesins. In contrast, deletion mutants of the cluster V adhesin Awp2 in the hyperadhesive clinical isolate PEU382 demonstrated its importance for adhesion to polystyrene or glass, biofilm formation, cell aggregation and other cell surface-related phenotypes. Together with cluster III and VII adhesins our study shows that C. glabrata CBS138 can rely on a set of 42 Awp1-related adhesins with β-helix/α-crystallin domain architecture for modifying the surface characteristics of its cell wall. |
| doi_str_mv | 10.1371/journal.ppat.1009980 |
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Though it lacks typical virulence factors such as hyphal development, C. glabrata contains a remarkably large and diverse set of putative wall adhesins that is crucial for its success as pathogen. Here, we present an analysis of putative adhesins from the homology clusters V and VI. First, sequence similarity network analysis revealed relationships between cluster V and VI adhesins and S. cerevisiae haze protective factors (Hpf). Crystal structures of A-regions from cluster VI adhesins Awp1 and Awp3b reveal a parallel right-handed β-helix domain that is linked to a C-terminal β-sandwich. Structure solution of the A-region of Awp3b via single wavelength anomalous diffraction phasing revealed the largest known lanthanide cluster with 21 Gd3+ ions. Awp1-A and Awp3b-A show structural similarity to pectate lyases but binding to neither carbohydrates nor Ca2+ was observed. Phenotypic analysis of awp1Δ, awp3Δ, and awp1,3Δ double mutants did also not confirm their role as adhesins. In contrast, deletion mutants of the cluster V adhesin Awp2 in the hyperadhesive clinical isolate PEU382 demonstrated its importance for adhesion to polystyrene or glass, biofilm formation, cell aggregation and other cell surface-related phenotypes. Together with cluster III and VII adhesins our study shows that C. glabrata CBS138 can rely on a set of 42 Awp1-related adhesins with β-helix/α-crystallin domain architecture for modifying the surface characteristics of its cell wall.</description><identifier>ISSN: 1553-7374</identifier><identifier>ISSN: 1553-7366</identifier><identifier>EISSN: 1553-7374</identifier><identifier>DOI: 10.1371/journal.ppat.1009980</identifier><identifier>PMID: 34962966</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Adhesins ; Adhesion ; Biofilms ; Biofilms - growth & development ; Biology and Life Sciences ; Calcium ions ; Candida glabrata ; Candida glabrata - genetics ; Candida glabrata - metabolism ; Candida glabrata - pathogenicity ; Candidiasis - microbiology ; Carbohydrates ; Cell Adhesion ; Cell Adhesion Molecules - chemistry ; Cell Adhesion Molecules - genetics ; Cell Adhesion Molecules - metabolism ; Cell aggregation ; Cell surface ; Cell Wall - metabolism ; Cell walls ; Clinical isolates ; Clusters ; Crystal structure ; Crystallin ; Deletion mutant ; Domains ; Fungal Proteins - chemistry ; Fungal Proteins - genetics ; Fungal Proteins - metabolism ; Gadolinium ; Genomes ; Handedness ; Haze ; Homology ; Humans ; Infections ; Medicine and Health Sciences ; Models, Molecular ; Mutants ; Network analysis ; Phenotypes ; Physical Sciences ; Polystyrene ; Polystyrene resins ; Protective structures ; Proteins ; Research and Analysis Methods ; Similarity ; Surface properties ; Virulence ; Virulence Factors ; Yeasts</subject><ispartof>PLoS pathogens, 2021-12, Vol.17 (12), p.e1009980-e1009980</ispartof><rights>2021 Reithofer et al. This is an open access article distributed under the terms of the Creative Commons Attribution License: http://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. 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Academic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>PLoS pathogens</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Reithofer, Viktoria</au><au>Fernández-Pereira, Jordan</au><au>Alvarado, María</au><au>de Groot, Piet</au><au>Essen, Lars-Oliver</au><au>Deepe, George</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A novel class of Candida glabrata cell wall proteins with β-helix fold mediates adhesion in clinical isolates</atitle><jtitle>PLoS pathogens</jtitle><addtitle>PLoS Pathog</addtitle><date>2021-12-01</date><risdate>2021</risdate><volume>17</volume><issue>12</issue><spage>e1009980</spage><epage>e1009980</epage><pages>e1009980-e1009980</pages><issn>1553-7374</issn><issn>1553-7366</issn><eissn>1553-7374</eissn><abstract>Candida glabrata is an opportunistic pathogenic yeast frequently causing infections in humans. Though it lacks typical virulence factors such as hyphal development, C. glabrata contains a remarkably large and diverse set of putative wall adhesins that is crucial for its success as pathogen. Here, we present an analysis of putative adhesins from the homology clusters V and VI. First, sequence similarity network analysis revealed relationships between cluster V and VI adhesins and S. cerevisiae haze protective factors (Hpf). Crystal structures of A-regions from cluster VI adhesins Awp1 and Awp3b reveal a parallel right-handed β-helix domain that is linked to a C-terminal β-sandwich. Structure solution of the A-region of Awp3b via single wavelength anomalous diffraction phasing revealed the largest known lanthanide cluster with 21 Gd3+ ions. Awp1-A and Awp3b-A show structural similarity to pectate lyases but binding to neither carbohydrates nor Ca2+ was observed. Phenotypic analysis of awp1Δ, awp3Δ, and awp1,3Δ double mutants did also not confirm their role as adhesins. In contrast, deletion mutants of the cluster V adhesin Awp2 in the hyperadhesive clinical isolate PEU382 demonstrated its importance for adhesion to polystyrene or glass, biofilm formation, cell aggregation and other cell surface-related phenotypes. Together with cluster III and VII adhesins our study shows that C. glabrata CBS138 can rely on a set of 42 Awp1-related adhesins with β-helix/α-crystallin domain architecture for modifying the surface characteristics of its cell wall.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>34962966</pmid><doi>10.1371/journal.ppat.1009980</doi><orcidid>https://orcid.org/0000-0002-6879-1609</orcidid><orcidid>https://orcid.org/0000-0002-3980-1695</orcidid><orcidid>https://orcid.org/0000-0003-4272-4026</orcidid><orcidid>https://orcid.org/0000-0003-4405-9453</orcidid><orcidid>https://orcid.org/0000-0002-3112-6947</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | Adhesins Adhesion Biofilms Biofilms - growth & development Biology and Life Sciences Calcium ions Candida glabrata Candida glabrata - genetics Candida glabrata - metabolism Candida glabrata - pathogenicity Candidiasis - microbiology Carbohydrates Cell Adhesion Cell Adhesion Molecules - chemistry Cell Adhesion Molecules - genetics Cell Adhesion Molecules - metabolism Cell aggregation Cell surface Cell Wall - metabolism Cell walls Clinical isolates Clusters Crystal structure Crystallin Deletion mutant Domains Fungal Proteins - chemistry Fungal Proteins - genetics Fungal Proteins - metabolism Gadolinium Genomes Handedness Haze Homology Humans Infections Medicine and Health Sciences Models, Molecular Mutants Network analysis Phenotypes Physical Sciences Polystyrene Polystyrene resins Protective structures Proteins Research and Analysis Methods Similarity Surface properties Virulence Virulence Factors Yeasts |
| title | A novel class of Candida glabrata cell wall proteins with β-helix fold mediates adhesion in clinical isolates |
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