{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Alvarado M"],"funding":["UCLM","Regional Government of Castilla-La Mancha","Spanish Government","European Regional Development Fund"],"pagination":["foaf042"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12359137"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["25"],"pubmed_abstract":["The Pir1 protein in the prevalent pathogenic yeast Candidaalbicans has been hypothesized to be important for cellular integrity by crosslinking cell wall β-1,3-glucans. However, recent studies with deletion mutants have reported contrasting results concerning its actual importance for wall integrity. Here, we present functional characterization of the two members of the Pir family (Pir1 and Pir32) as well as protein structure modeling and mutagenesis studies to elucidate how Pir1, the most important family member, is incorporated into the cell wall. Our data show that Pir1 indeed is involved in β-1,3-glucan binding but its gene deletion did not affect cellular fitness. 3D structure modeling predicts that Pir1 has a core predominantly comprised of antiparallel β-sheets, surrounded by a larg"],"journal":["FEMS yeast research"],"pubmed_title":["Wall incorporation of the β-1,3-glucan cross-linking protein Pir1 in the human pathogen Candida albicans is facilitated by the presence of two or more Pir repeat units."],"pmcid":["PMC12359137"],"funding_grant_id":["CNS2022-135375","SBPLY/19/180501/000114","2023-PRED-21293","PID2020-117983RB-I00","SBPLY/23/180225/000029","2023-GRIN-34150","JDC2023-051226-I"],"pubmed_authors":["Blazquez-Abellan A","Moreno-Martinez AE","Valentin E","De Groot PWJ","Mixao V","Alvarado M","Mateo E","Gabaldon T","Gomez-Navajas JA","Mico M"],"additional_accession":[]},"is_claimable":false,"name":"Wall incorporation of the β-1,3-glucan cross-linking protein Pir1 in the human pathogen Candida albicans is facilitated by the presence of two or more Pir repeat units.","description":"The Pir1 protein in the prevalent pathogenic yeast Candidaalbicans has been hypothesized to be important for cellular integrity by crosslinking cell wall β-1,3-glucans. However, recent studies with deletion mutants have reported contrasting results concerning its actual importance for wall integrity. Here, we present functional characterization of the two members of the Pir family (Pir1 and Pir32) as well as protein structure modeling and mutagenesis studies to elucidate how Pir1, the most important family member, is incorporated into the cell wall. Our data show that Pir1 indeed is involved in β-1,3-glucan binding but its gene deletion did not affect cellular fitness. 3D structure modeling predicts that Pir1 has a core predominantly comprised of antiparallel β-sheets, surrounded by a larg","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Jan","modification":"2026-04-08T15:40:39.241Z","creation":"2026-04-08T05:10:26.243Z"},"accession":"S-EPMC12359137","cross_references":{"pubmed":["40795215"],"doi":["10.1093/femsyr/foaf042"]}}