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Title: Chemoenzymatic probes reveal peptidoglycan recognition and uptake mechanisms in Candida albicans
Authors: Li, Lanxin
Ng, Allan Wee Ren
Adamson, Christopher
Hayashi, Hirohito
Li, Chenyu
Lim, Huiyi
Qiao, Yuan
Keywords: Science::Chemistry::Biochemistry
Issue Date: 2022
Source: Li, L., Ng, A. W. R., Adamson, C., Hayashi, H., Li, C., Lim, H. & Qiao, Y. (2022). Chemoenzymatic probes reveal peptidoglycan recognition and uptake mechanisms in Candida albicans. ACS Chemical Biology.
Project: NRF-NRFF12-2020-0006
NTU-SUG grant
Journal: ACS Chemical Biology 
Abstract: Candida albicans, the major fungal pathogen in humans, is under the strong influence of bacterial peptidoglycan fragments to undergo the yeast-to-hyphae transition, a key virulent step in C. albicans pathogenesis and infections. However, due to the synthetic difficulties of obtaining peptidoglycan fragments for biological studies, mechanistic details of how C. albicans recognizes and uptakes these peptidoglycan fragments have not been well elucidated. Notably, previous works have solely focused on the synthetic peptidoglycan ligand, muramyl dipeptide (MDP), despite its poor hyphal-inducing activity in C. albicans. In this work, we isolated and purified natural peptidoglycan fragments via enzymatic degradation of bacteria cell wall sacculi and chemoenzymatically installed a series of functional d-amino acids into the natural muropeptide, creating peptidoglycan probes that bear photoaffinity, bio-orthogonal, or fluorescent functionality. Using these chemoenzymatic peptidoglycan probes, we established that natural peptidoglycan fragments, which are potent hyphal-inducers, interact with the C. albicans Cyr1 sensor protein in the in-gel fluorescence assay as well as in in vitro pulldown studies. Moreover, we established that bacterial peptidoglycan probes enter C. albicans cells via an energy-dependent endocytic process.
ISSN: 1554-8929
DOI: 10.1021/acschembio.2c00468
Schools: School of Physical and Mathematical Sciences 
Rights: This document is the Accepted Manuscript version of a Published Work that appeared in final form in ACS Chemical Biology, copyright © American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:SPMS Journal Articles

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