Evidence for a new post-translational modification in Staphylococcus aureus: hydroxymethylation of asparagine and glutamine.
Staphylococcus aureus is an opportunistic pathogen whose infectious capacity depends on surface proteins, which enable bacteria to colonize and invade host tissues and cells. We analyzed "trypsin-shaved" surface proteins of S. aureus cultures by high resolution LC-MS/MS at different growth stages and culture conditions. Some modified peptides were identified, with a mass shift corresponding to the addition of a CH₂O group (+30.0106 u). We present evidence that this shift corresponds to a hyxdroxymethylation of asparagine and glutamine residues. This known but poorly documented post-translational modification was only found in a few proteins of S. aureus grown under specific conditions. This specificity seemed to exclude the hypothesis of an artifact due to sample preparation. Altogether hydroxymethylation was observed in 35 peptides from 15 proteins in our dataset, which corresponded to 41 modified sites, 35 of them being univocally localized. While no function can currently be assigned to this post-translational modification, we hypothesize that it could be linked to modulation of virulence factors, since it was mostly found on some surface proteins of S. aureus.
Protein Analysis Facility, University of Lausanne, 1015 Lausanne, Switzerland. Patrice.Waridel@unil.ch
Patrice
P
Waridel
Mathilde
M
Ythier
Aurélie
A
Gfeller
Philippe
P
Moreillon
Manfredo
M
Quadroni
D001216:Asparagine / Q000378:metabolism*; D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism*; D002853:Chromatography, Liquid; D005973:Glutamine / Q000378:metabolism*; D008565:Membrane Proteins / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D013211:Staphylococcus aureus / Q000378:metabolism*; D053719:Tandem Mass Spectrometry
D001426:Bacterial Proteins; D008565:Membrane Proteins; D005973:Glutamine; D001216:Asparagine