Imaging mass spectrometry for assessing temporal proteomics: Analysis of calprotectin in Acinetobacter baumannii pulmonary infection. Issue 7 (24th July 2013)

• Record Type: Journal Article
• Authors: Moore, Jessica L.; Becker, Kyle W.; Nicklay, Joshua J.; Boyd, Kelli L.; Skaar, Eric P.; Caprioli, Richard M.; Lodeiro, Carlos; Martínez, José Luis Capelo; Santos, Hugo M.
• Is Part Of: Proteomics. Volume 14:Issue 7/8(2014:Apr.)
• Page Start: 820
• Page End: 828
• Publication Date: 2013-07-24
• Subjects: Proteins -- Separation -- Periodicals; Bioinformatics -- Periodicals; Proteomics -- Periodicals; Genomes -- Periodicals; Molecular genetics -- Periodicals; 572.605
• DOI: 10.1002/pmic.201300046
• Languages: English
• ISSNs: 1615-9853

Abstract

<abstract abstract-type="main"> <title> <x xml:space="preserve">Abstract</x> </title> <p>Imaging MS is routinely used to show spatial localization of proteins within a tissue sample and can also be employed to study temporal protein dynamics. The antimicrobial S100 protein calprotectin, a heterodimer of subunits S100A8 and S100A9, is an abundant cytosolic component of neutrophils. Using imaging MS, calprotectin can be detected as a marker of the inflammatory response to bacterial challenge. In a murine model of <italic>Acinetobacter baumannii</italic> pneumonia, protein images of S100A8 and S100A9 collected at different time points throughout infection aid in visualization of the innate immune response to this pathogen. Calprotectin is detectable within 6 h of infection as immune cells respond to the invading pathogen. As the bacterial burden decreases, signals from the inflammatory proteins decrease. Calprotectin is no longer detectable 96–144 h post infection, correlating to a lack of detectable bacterial burden in lungs. These experiments provide a label‐free, multiplexed approach to study host response to a bacterial threat and eventual clearance of the pathogen over time.</p> </abstract>