Taxonomic group: fungi / Ascomycota
(Phylum: Ascomycota)
Organ / tissue: hyphal cell
NCBI PubMed ID: 24779420Publication DOI: 10.1111/mmi.12626Journal NLM ID: 8712028Publisher: Blackwell Publishing
Correspondence: Cramer RA <Robert.A.Cramer.Jr
dartmouth.edu>
Institutions: Department of Microbiology and Immunology, Geisel School of Medicine at Dartmouth, Hanover, USA, Department of Immunology and Infectious Disease, Montana State University, Bozeman, USA
GPI-anchoring is a universal and critical post-translational protein modification in eukaryotes. In fungi, many cell wall proteins are GPI-anchored, and disruption of GPI-anchored proteins impairs cell wall integrity. After being synthesized and attached to target proteins, GPI anchors undergo modification on lipid moieties. In spite of its importance for GPI-anchored protein functions, our current knowledge of GPI lipid remodelling in pathogenic fungi is limited. In this study, we characterized the role of a putative GPI lipid remodelling protein, designated PerA, in the human pathogenic fungus Aspergillus fumigatus. PerA localizes to the endoplasmic reticulum and loss of PerA leads to striking defects in cell wall integrity. A perA null mutant has decreased conidia production, increased susceptibility to triazole antifungal drugs, and is avirulent in a murine model of invasive pulmonary aspergillosis. Interestingly, loss of PerA increases exposure of β-glucan and chitin content on the hyphal cell surface, but diminished TNF production by bone marrow-derived macrophages relative to wild type. Given the structural specificity of fungal GPI-anchors, which is different from humans, understanding GPI lipid remodelling and PerA function in A. fumigatus is a promising research direction to uncover a new fungal specific antifungal drug target.
Aspergillus fumigatus, GPI
Structure type: homopolymer
Location inside paper: pg. 1291, column 2, line 16
Trivial name: chitin
Compound class: O-polysaccharide, cell wall polysaccharide, glucan, polysaccharide, chitin
Contained glycoepitopes: IEDB_135813,IEDB_137340,IEDB_141807,IEDB_151531,IEDB_153212,IEDB_241099,IEDB_423114,IEDB_423150,SB_74,SB_85
Methods: ELISA, DNA extraction, RNA extraction, qRT-PCR, light microscopy, germination assay, XTT assay
Comments, role: The article does not possess any information on chitin structure.
Related record ID(s): 40517, 43385, 101632, 118702, 139869, 143703, 145244, 147175, 149428, 149871, 149874
NCBI Taxonomy refs (TaxIDs): 746128,
5476Reference(s) to other database(s): GTC:G97099AY, CCSD:
46067, CBank-STR:5851, GenDB:KF905651
Show glycosyltransferases
There is only one chemically distinct structure:
Found 
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