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Integrated post-genomic cell wall analysis reveals floating biofilm formation associated with high expression of flocculins in the pathogen Pichia kudriavzevii.
Alvarado, María; Gómez-Navajas, Jesús Alberto; Blázquez-Muñoz, María Teresa; Gómez-Molero, Emilia; Berbegal, Carmen; Eraso, Elena; Kramer, Gertjan; De Groot, Piet W J.
Afiliación
  • Alvarado M; Regional Center for Biomedical Research, Castilla-La Mancha Science & Technology Park, University of Castilla-La Mancha, Albacete, Spain.
  • Gómez-Navajas JA; Regional Center for Biomedical Research, Castilla-La Mancha Science & Technology Park, University of Castilla-La Mancha, Albacete, Spain.
  • Blázquez-Muñoz MT; Regional Center for Biomedical Research, Castilla-La Mancha Science & Technology Park, University of Castilla-La Mancha, Albacete, Spain.
  • Gómez-Molero E; Regional Center for Biomedical Research, Castilla-La Mancha Science & Technology Park, University of Castilla-La Mancha, Albacete, Spain.
  • Berbegal C; ENOLAB, Estructura de Recerca Interdisciplinar (ERI) BioTecMed and Departament de Microbiologia i Ecología, Universitat de València, Burjassot, Spain.
  • Eraso E; Department of Immunology, Microbiology and Parasitology, Faculty of Medicine and Nursing, University of the Basque Country (UPV/EHU), Bilbao, Spain.
  • Kramer G; Mass Spectrometry of Biomolecules, University of Amsterdam, Swammerdam Institute for Life Sciences Amsterdam, Amsterdam, The Netherlands.
  • De Groot PWJ; Regional Center for Biomedical Research, Castilla-La Mancha Science & Technology Park, University of Castilla-La Mancha, Albacete, Spain.
PLoS Pathog ; 19(5): e1011158, 2023 05.
Article en En | MEDLINE | ID: mdl-37196016
ABSTRACT
The pathogenic yeast Pichia kudriavzevii, previously known as Candida krusei, is more distantly related to Candida albicans than clinically relevant CTG-clade Candida species. Its cell wall, a dynamic organelle that is the first point of interaction between pathogen and host, is relatively understudied, and its wall proteome remains unidentified to date. Here, we present an integrated study of the cell wall in P. kudriavzevii. Our comparative genomic studies and experimental data indicate that the general structure of the cell wall in P. kudriavzevii is similar to Saccharomyces cerevisiae and C. albicans and is comprised of ß-1,3-glucan, ß-1,6-glucan, chitin, and mannoproteins. However, some pronounced differences with C. albicans walls were observed, for instance, higher mannan and protein levels and altered protein mannosylation patterns. Further, despite absence of proteins with high sequence similarity to Candida adhesins, protein structure modeling identified eleven proteins related to flocculins/adhesins in S. cerevisiae or C. albicans. To obtain a proteomic comparison of biofilm and planktonic cells, P. kudriavzevii cells were grown to exponential phase and in static 24-h cultures. Interestingly, the 24-h static cultures of P. kudriavzevii yielded formation of floating biofilm (flor) rather than adherence to polystyrene at the bottom. The proteomic analysis of both conditions identified a total of 33 cell wall proteins. In line with a possible role in flor formation, increased abundance of flocculins, in particular Flo110, was observed in the floating biofilm compared to exponential cells. This study is the first to provide a detailed description of the cell wall in P. kudriavzevii including its cell wall proteome, and paves the way for further investigations on the importance of flor formation and flocculins in the pathogenesis of P. kudriavzevii.
Asunto(s)

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Saccharomyces cerevisiae / Proteoma Tipo de estudio: Risk_factors_studies Idioma: En Revista: PLoS Pathog Año: 2023 Tipo del documento: Article País de afiliación: España

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Saccharomyces cerevisiae / Proteoma Tipo de estudio: Risk_factors_studies Idioma: En Revista: PLoS Pathog Año: 2023 Tipo del documento: Article País de afiliación: España