New mass spectrometry tool accurately identifies bacteria
Scientists identify bacterial species by analyzing their proteins using mass spectrometry, or MS. This technique first fragments proteins into smaller peptides using an enzyme called trypsin. These sequences can then be compared to references in databases. The largest MS-based studies on bacteria have focused on just a handful of species, so a team of researchers recently created a resource for mapping data onto a more diverse population of bacteria.

Miriam Abele, Armin Soleymaniniya and colleagues at the Technical University of Munich developed MS2Bac, a software system that enables bacterial identification from protein data. They published their in Molecular & Cellular Proteomics. MS2Bac maps tryptic peptides onto reference bacterial species or strains, achieving almost perfect accuracy for species identification. To develop this tool, the team first performed MS on the proteins from over 300 bacterial species to create a reference database. They also compared their identification method with other approaches, such as Fourier transform infrared spectroscopy, and found that MS2Bac was the most accurate.
MS2Bac can also identify specific proteins, antibiotic resistance markers. It covers many hypothetical proteins, which are not well understood, providing a basis for further functional studies. This is the first study to incorporate single-cell organisms into the database, a proteomics resource for multiomics analyses. This tool will greatly help researchers and clinicians determine bacterial species from clinically and environmentally relevant samples.
Enjoy reading ASBMB Today?
Become a member to receive the print edition four times a year and the digital edition monthly.
Learn moreGet the latest from ASBMB Today
Enter your email address, and we’ll send you a weekly email with recent articles, interviews and more.
Latest in Science
Science highlights or most popular articles

How sugars shape Marfan syndrome
Research from the University of Georgia shows that Marfan syndrome–associated fibrillin-1 mutations disrupt O glycosylation, revealing unexpected changes that may alter the protein's function in the extracellular matrix.

What’s in a diagnosis?
When Jessica Foglio’s son Ben was first diagnosed with cerebral palsy, the label didn’t feel right. Whole exome sequencing revealed a rare disorder called Salla disease. Now Jessica is building community and driving research for answers.

Peer through a window to the future of science
Aaron Hoskins of the University of Wisconsin–Madison and Sandra Gabelli of Merck, co-chairs of the 2026 ASBMB annual meeting, to be held March 7–10, explain how this gathering will inspire new ideas and drive progress in molecular life sciences.

Glow-based assay sheds light on disease-causing mutations
University of Michigan researchers create a way to screen protein structure changes caused by mutations that may lead to new rare disease therapeutics.

How signals shape DNA via gene regulation
A new chromatin isolation technique reveals how signaling pathways reshape DNA-bound proteins, offering insight into potential targets for precision therapies. Read more about this recent ¾ÅÓÎÌåÓý paper.

A game changer in cancer kinase target profiling
A new phosphonate-tagging method improves kinase inhibitor profiling, revealing off-target effects and paving the way for safer, more precise cancer therapies tailored to individual patients. Read more about this recent ¾ÅÓÎÌåÓý paper.