A protein O-GlcNAc glycosyltransferase regulates the antioxidative response in Yersinia pestis

Shiyang Cao, Tong Wang, Yifan Ren, Gengshan Wu, Yuan Zhang, Yafang Tan, Yazhou Zhou, Hongyan Chen, Yu Zhang, Yajun Song, Ruifu Yang () and Zongmin Du ()
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Shiyang Cao: Academy of Military Medical Sciences
Tong Wang: Academy of Military Medical Sciences
Yifan Ren: Academy of Military Medical Sciences
Gengshan Wu: Academy of Military Medical Sciences
Yuan Zhang: Academy of Military Medical Sciences
Yafang Tan: Academy of Military Medical Sciences
Yazhou Zhou: Academy of Military Medical Sciences
Hongyan Chen: Academy of Military Medical Sciences
Yu Zhang: Academy of Military Medical Sciences
Yajun Song: Academy of Military Medical Sciences
Ruifu Yang: Academy of Military Medical Sciences
Zongmin Du: Academy of Military Medical Sciences

Nature Communications, 2024, vol. 15, issue 1, 1-16

Abstract: Abstract Post-translational addition of O-linked N-acetylglucosamine (O-GlcNAc) to proteins is commonly associated with a variety of stress responses and cellular processes in eukaryotes, but its potential roles in bacteria are unclear. Here, we show that protein HmwC acts as an O-GlcNAc transferase (OGT) responsible for O-GlcNAcylation of multiple proteins in Yersinia pestis, a flea-borne pathogen responsible for plague. We identify 64 O-GlcNAcylated proteins (comprising 65 sites) with differential abundance under conditions mimicking the mammalian host (Mh) and flea vector (Fv) environments. Deletion of hmwC, encoding a putative OGT, structurally distinct from any existing member of the GT41 family, results in reduced O-GlcNAcylation, reduced growth, and alterations in virulence properties and survival under stress. Purified HmwC can modify target proteins in vitro using UDP-GlcNAc as sugar donor. One of the target proteins, OsdY, promotes Y. pestis survival under oxidative stress conditions. Thus, our results support that regulation of antioxidative responses through O-GlcNAcylation may be a conserved process shared by prokaryotes and eukaryotes.

Date: 2024
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DOI: 10.1038/s41467-024-50959-w

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