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Updated: May 26, 2026

A Tandem Liquid Chromatography–Mass Spectrometry-based Approach for Metabolite Analysis of Staphylococcus aureus
08:03

A Tandem Liquid Chromatography–Mass Spectrometry-based Approach for Metabolite Analysis of Staphylococcus aureus

Published on: March 28, 2017

Evidence for a new post-translational modification in Staphylococcus aureus: hydroxymethylation of asparagine and

Patrice Waridel1, Mathilde Ythier, Aurélie Gfeller

  • 1Protein Analysis Facility, University of Lausanne, 1015 Lausanne, Switzerland. Patrice.Waridel@unil.ch

Journal of Proteomics
|December 31, 2011
PubMed

Insights

We discovered a rare post-translational modification, hydroxymethylation, in Staphylococcus aureus surface proteins. This modification, found under specific conditions, may influence bacterial virulence factors.

Area of Science:

  • Microbiology
  • Proteomics
  • Biochemistry

Background:

  • Staphylococcus aureus relies on surface proteins for colonization and invasion.
  • Understanding protein modifications is crucial for deciphering bacterial pathogenesis.

Purpose of the Study:

  • To investigate post-translational modifications in Staphylococcus aureus surface proteins.
  • To identify and characterize novel or under-documented modifications.

Main Methods:

  • Analysis of "trypsin-shaved" surface proteins using high-resolution LC-MS/MS.
  • Examination of bacterial cultures at various growth stages and conditions.

Main Results:

  • Identified peptides with a mass shift indicative of hydroxymethylation on asparagine and glutamine residues.
  • Observed this modification in 15 proteins (41 sites), primarily on surface proteins, under specific growth conditions.
  • Results suggest the modification is not an artifact of sample preparation.

Conclusions:

  • Hydroxymethylation is a post-translational modification present in Staphylococcus aureus.
  • The specific occurrence suggests a regulated biological role.
  • Hypothesized role in modulating virulence factors due to its prevalence on surface proteins.

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