Widespread protein lysine acetylation in gut microbiome and its alterations in patients with Crohn's diseaseOriginal paper
Karen Pendergrass is a microbiome researcher specializing in microbiome-targeted interventions (MBTIs). She systematically analyzes scientific literature to identify microbial patterns, develop hypotheses, and validate interventions. As the founder of the Microbiome Signatures Database, she bridges microbiome research with clinical practice. In 2012, based on her own investigative research, she became the first documented case of FMT for Celiac Disease, four years before the first published case study.
Read MoreWhat was studied?
Researchers examined protein lysine acetylation (Kac), a post-translational modification, across the gut microbiome as a whole, rather than in single organisms. They then compared Kac patterns between Crohn's disease patients and controls.
How was it studied?
The team used a peptide immuno-affinity enrichment strategy coupled with Orbitrap mass spectrometry to capture Kac peptides from gut microbiome samples. An integrated metaproteomics and lysine acetylomics bioinformatic workflow, developed for this study, identified and quantified both microbial and human protein Kac sites.
What did they find?
The approach identified 35,200 Kac peptides from microbial and human proteins in gut microbiome samples. Kac was widespread across microbial metabolic pathways, including anaerobic fermentation that generates short-chain fatty acids. In Crohn's disease patients versus controls, 52 host and 136 microbial protein Kac sites were differentially abundant.
Why it matters
This is the first characterization of protein Kac at the whole-microbiome level, establishing that acetylation is altered in disease. The microbiome-wide acetylomic approach opens a new layer for studying functional dysregulation in Crohn's disease and other conditions.