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ARS Home » Southeast Area » Fayetteville, Arkansas » Poultry Production and Product Safety Research » Research » Publications at this Location » Publication #320594

Title: Proteomic changes in chicken plasma induced by Salmonella typhimurium lipopolysaccharides

item BALAMURUGAN, PACKIALAKSHMI - University Of Arkansas
item LIYANAGE, ROHANA - University Of Arkansas
item LAY, JACKSON - University Of Arkansas
item MAKKAR, SARBJEET - University Of Arkansas
item Rath, Narayan

Submitted to: Proteomics Insights
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 2/12/2016
Publication Date: 3/31/2016
Citation: Balamurugan, P., Liyanage, R., Lay, J., Makkar, S., Rath, N.C. 2016. Proteomic changes in chicken plasma induced by Salmonella typhimurium lipopolysaccharides. Proteomics Insights. 7:1-9.

Interpretive Summary: Certain bacteria produce toxins called lipopolysaccharides (LPS) that cause sickenss. We used it as a model to determine the changes in blood proteins profiles of chickens to identify biomarkers than can be useful as diagnostic. Our results showed that LPS injection caused sickness and weightloss and produced both qualitative and quantitative changes changes in several blood proteins some of which can potentially be markers to diagnose health problems in poultry.

Technical Abstract: Lipopolysaccharides (LPS) are cell wall components of gram-negative bacteria that cause inflammation and sickness through genetic and proteomic activation. The objective of our study was to identify the proteomic changes in plasma associated with inflammation induced by LPS treatment. Five-week-old chickens were injected with saline or LPS and the blood samples were collected after 24 h. The plasma samples were depleted of high abundant proteins (HAPD) with acetonitrile, desalted using C18 tips, and analyzed by Matrix assisted laser desorption ionization-time-of-flight mass spectrometry (MALDI-TOF-MS). The mass spectra were compared by ClinProTools and 2 candidate peptides were isolated by reverse phase liquid chromatography (RP-HPLC) for characterization by peptide mass fingerprinting (PMF) which showed an increase in a fibrinogen precursor derived peptide and reduction in an apolipoprotein AII- isoform X1 derived peptide in LPS samples. HAPD plasma proteome were subjected to reduction, alkylation, trypsin digestion and liquid chromatography–tandem mass spectrometry (LC-MS/MS). Label free quantitation using Skyline/Mstats software showed increases in alpha-1 acid glycoprotein, chemokine-CCLI10, and cathelicidin-2 while interferon stimulated gene-12-2 protein was decreased in LPS group. These differentially expressed proteins are potentially useful as candidate biomarkers of infection and inflammation in poultry.