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Glycoproteomic and Proteomic Analysis of Reveals Glycosylation Events Within FliF and MotB Are Dispensable for Motility

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Specialty Microbiology
Date 2024 May 6
PMID 38709084
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Abstract

Importance: is an opportunistic pathogen of concern within the Cystic Fibrosis community. Despite a greater appreciation of the unique physiology of gained over the last 20 years a complete understanding of the proteome and especially the O-glycoproteome, is lacking. In this study, we utilize systems biology approaches to expand the known glycoproteome as well as track the dynamics of glycoproteins across growth phases, culturing media and in response to the loss of glycosylation. We show that the glycoproteome of is largely stable across conditions and that the loss of glycosylation only impacts five glycoproteins including the motility associated proteins FliF and MotB. Examination of MotB and FliF shows, while these proteins are essential for motility, glycosylation is dispensable. Combined this work supports that glycosylation can be dispensable for protein function and may influence protein properties beyond stability.

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