Collection of annotated MALDI-TOF mass peaks of Helicobacter pylori collated from the literature

Mass spectrometry has evolved to be the dominant technique in proteomics, especially with the advent of soft ionization techniques such as matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS). This work presents a dataset comprising MALDI-TOF MS mass peaks of Helicobacter pylori collated from different sources in the scientific literature. The mass peaks were first annotated by aligning their mass-to-charge ratio to the molecular weight of proteins in the proteome of H. pylori. This alignment gives the amino acid sequence of the mass peaks, which was used in a BLASTp search to provide confirmation of the identity of the mass peaks. In general, there is good agreement on the mass peaks’ identity from the UniProt proteome and the BLASTp search. Finally, the different proteins identified were assessed on their ability to uniquely identify H. pylori based on their nucleotide sequence. Overall, almost all proteins annotated could be used to uniquely identify H. pylori.