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Stabilization of the Human Pathogen Candida. albicans' Cyr1p receptor via Bacterial Peptidoglycan Fragments
Author(s) -
Crump Geneva,
Mashayekh Siavash,
LeimkuhlerGrimes Catherine
Publication year - 2021
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.2021.35.s1.04549
Subject(s) - candida albicans , microbiology and biotechnology , biology , peptidoglycan , pathogen , corpus albicans , immune system , human pathogen , bacteria , yeast , genetics
The structurally complex bacterial peptidoglycan (PG) is a polymer of carbohydrates and crosslinked peptides that are present in both Gram Negative and Positive bacteria. PG can elicit immune responses in hosts across various kingdoms. One way such responses are generated is through signaling of the evolutionary conserved Leucine Rich Repeat (LRR) protein domain. Fungi reside in the human microbiota among many microorganisms such as Bacteria and Archea. The polymorphic fungus Candida. albicans ( C. albicans ) is perhaps the most common fungi of the human microbiota. In healthy individuals this commensal pathogen provides a symbiotic relationship, whereas in immune compromised individuals infections ranging from superficial skin infections to high mortality systemic infections ensue. The pathogenic potential of this fungus is preceded by a morphological switch from that of a commensal budding state to an extended hyphal state. The signal integrator responsible for this morphological change is the adenyl cyclase Cyr1p binding to its ligand(s); bacterial peptidoglycan fragment(s). Cyr1p contains a conserved LRR domain that behaves as the sensor for PG. In this way, Cyr1p behaves as a Pathogen Recognition Receptor via its LRR domain. To determine the promiscuity of the Cyr1p‐LRR domain, we have conducted Cellular Thermal Shift Assays on recombinant Cyr1p‐LRR domain and hyphal growth phenotypical assays in WT C. albicans cells using a variety of bacterial PG fragments. These studies help to characterize and define yeast‐bacterial interactions within the human host.