Proteomics

Dataset Information

0

Peptidomic analysis of bacterial protease activity in acute wound fluids


ABSTRACT: The clinical assessment of wound infection and related complications is challenging and the development of objective methods to measure wound status and predict healing outcomes is therefore essential. As bacterial protease activities play important roles in infection, analysis of changes in the wound peptidome by individual bacterial enzymes could provide insight into proteolytic events occurring in infected wounds, and may aid in the discovery of biomarkers. Wound infection was mimicked by incubating sterile acute wound fluids ex vivo with the bacterial proteases Pseudomonas aeruginosa LasB and Staphyloccocus aureus V8. Using a peptidomics approach, we characterized the low-molecular-weight peptidome of the digested samples and identified over 100 protein targets for each enzyme. Additionally, we found enzyme-specific peptides and digestion patterns.

INSTRUMENT(S): Orbitrap Eclipse

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Wound Fluid

DISEASE(S): Wounds And Injuries

SUBMITTER: Mariena van der Plas  

LAB HEAD: Mariena J.A.

PROVIDER: PXD037047 | Pride | 2024-03-07

REPOSITORIES: Pride

altmetric image

Publications

Peptidomic analysis of endogenous and bacterial protease activity in human plasma and wound fluids.

Cai Jun J   Nielsen Maike W MW   Kalogeropoulos Konstantinos K   Auf dem Keller Ulrich U   van der Plas Mariena J A MJA  

iScience 20240126 2


Endogenous and bacterial proteases play important roles in wound healing and infection. Analysis of alterations in the low-molecular-weight peptidome by individual enzymes could therefore provide insight into proteolytic events occurring in wounds and may aid in the discovery of biomarkers. Using liquid chromatography with tandem mass spectrometry, we characterized the peptidome of plasma and acute wound fluids digested <i>ex vivo</i> with human (neutrophil elastase and cathepsin G) and bacteria  ...[more]

Similar Datasets

2024-03-07 | PXD037245 | Pride
2021-09-10 | PXD023884 | Pride
2014-08-19 | E-GEOD-60492 | biostudies-arrayexpress
2012-11-14 | E-GEOD-25945 | biostudies-arrayexpress
2021-01-18 | PXD023244 | Pride
2014-01-01 | E-GEOD-51167 | biostudies-arrayexpress
2011-09-19 | E-GEOD-23007 | biostudies-arrayexpress
2015-11-24 | E-GEOD-75359 | biostudies-arrayexpress
2017-09-14 | PXD006674 | Pride
2021-03-29 | PXD014797 | Pride