Role of Pir1 in the construction of the Candida albicans cell wall

• Published in: Microbiology (Society for General Microbiology) 2004-10, Vol.150 (10), p.3151-3161
• Main Authors: Martinez, Ana I, Castillo, Luis, Garcera, Ana, Elorza, Maria V, Valentin, Eulogio, Sentandreu, Rafael
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; beta-Glucans - metabolism; Candida albicans - genetics; Candida albicans - physiology; Candida albicans - ultrastructure; Cell Wall - genetics; Cell Wall - physiology; Fungal Proteins - physiology; Glycoproteins; Saccharomyces cerevisiae Proteins - physiology; Sequence Homology, Amino Acid
• ISSN: 1350-0872; 1465-2080
• DOI: 10.1099/mic.0.27220-0

Departament de Microbiología i Ecología, Facultat de Farmacia, Universitat de València, Vicent Andrés Estelles s/n, 46100 Burjassot, València, Spain Correspondence Rafael Sentandreu Rafael.sentandreu{at}uv.es Searches in a Candida albicans database ( http://genolist.pasteur.fr/CandidaDB/ ) identified two Individual Protein Files (IPF 15363 and 19968) whose deduced amino acid sequences showed 42 % and 45 % homology with Saccharomyces cerevisiae Pir4. The two DNA sequences are alleles of the same gene ( CaPIR1 ) but IPF 19968 has a deletion of 117 bases. IPF 19968 encodes a putative polypeptide of 364 aa, which is highly O -glycosylated and has an N -mannosylated chain, four cysteine residues and seven repeats. Both alleles are expressed under different growth conditions and during wall construction by regenerating protoplasts. The heterozygous mutant cells are elongated, form clumps of several cells and are hypersensitive to drugs that affect cell wall assembly. CaPir1 was labelled with the V5 epitope and found linked to the 1,3- -glucan of the C. albicans wall and also by disulphide bridges when expressed in S. cerevisiae . Abbreviations: ConA, concanavalin A; Endo-F, endoglycosidase F; IPF, individual protein file