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This Article Full Text Full Text (PDF) All Versions of this Article: mic.0.028902-0v1 155/6/2004    most recent Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Google Scholar Articles by Moreno-Ruiz, E. Articles by d'Enfert, C. PubMed PubMed Citation Articles by Moreno-Ruiz, E. Articles by d'Enfert, C. Agricola Articles by Moreno-Ruiz, E. Articles by d'Enfert, C.

The GPI-modified proteins Pga59 and Pga62 of Candida albicans are required for cell wall integrity

Giuseppe Ortu^1,2,

Fabien Cottier^1,

Sophie Goyard^1,

¹ Institut Pasteur, Unité Biologie et Pathogénicité Fongiques, INRA USC2019, Paris, France
² Sezione di Microbiologia generale ed Applicat, DISAABA, Sassari, Italy
³ Swammerdam Institute for Life Sciences, University of Amsterdam, Amsterdam, The Netherlands
⁴ Plate-forme de Microscopie Ultrastructurale, Institut Pasteur, Paris, France

The fungal cell wall is essential in maintaining cellular integrity and plays key roles in the interplay between fungal pathogens and their hosts. The PGA59 and PGA62 genes encode two short and related glycosylphosphatidylinositol-anchored cell wall proteins and their expression has been previously shown to be strongly upregulated when the human pathogen Candida albicans grows as biofilms. Using GFP fusion proteins, we have shown that Pga59 and Pga62 are cell-wall-located, N- and O-glycosylated proteins. The characterization of C. albicans pga59/pga59, pga62/pga62 and pga59/pga59 pga62/pga62 mutants suggested a minor role of these two proteins in hyphal morphogenesis and that they are not critical to biofilm formation. Importantly, the sensitivity to different cell-wall-perturbing agents was altered in these mutants. In particular, simultaneous inactivation of PGA59 and PGA62 resulted in high sensitivity to Calcofluor white, Congo red and nikkomicin Z and in resistance to caspofungin. Furthermore, cell wall composition and observation by transmission electron microscopy indicated an altered cell wall structure in the mutant strains. Collectively, these data suggest that the cell wall proteins Pga59 and Pga62 contribute to cell wall stability and structure.

Correspondence
Christophe d'Enfert
denfert{at}pasteur.fr

Present address: Laboratoire de Génétique Moléculaire des Champignons Phytopathogènes, Institut de Génétique Moléculaire, Université Paris-Sud, Orsay, France.

Present address: Department of Biosciences, University of Kent, Canterbury, UK.

Present address: Laboratoire d'Immunologie des Infections á Trypanosoma, Institut Pasteur, Paris, France.

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