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Discovery of Infectious Disease Biomarkers in Murine Anthrax Model Using Mass Spectrometry of the Low-Molecular-Mass Serum Proteome

Aarthi Narayanan1, Weidong Zhou2, Mark Ross2, Jane Tang3, Lance Liotta2, Emanuel Petricoin2, Fatah Kashanchi4, Charles Bailey1, Serguei Popov1
1National Center for Biodefense and Infectious Diseases
2Center for Proteomics and Molecular Medicine, George Mason University, 10900 University Blvd,Manassas, Virginia – 20110-2201
3Noblis, 3150 Fairview Park Drive, Falls Church, Virginia – 22042
4The George Washington University, 2121 Street, NW, Washington, DC 20052
*Corresponding author: Dr. Serguei Popov,
George Mason University,
10900 University Blvd, Manassas,
Virginia – 20110-2201,
Phone: 703 993 4713,
E-mail: spopov@gmu.edu
September 23, 2009; Accepted September 29, 2009; Published September 30, 20
Citation: Narayanan A, Zhou W, Ross M, Tang J, Liotta L, et al. (2009) Discovery of Infectious Disease Biomarkers in Murine Anthrax Model Using Mass Spectrometry of the Low-Molecular-Mass Serum Proteome. J Proteomics Bioinform 2: 408-415. doi:10.4172/jpb.1000101
Copyright: ©2009 Narayanan A, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Abstract

A novel mass spectrometry (MS)-based approach to the identification of host-derived biomarkers (BMs) in the circulating low-molecular-mass (LMM) fraction (<25 kDa) of blood proteome was tested in a murine model. DBA2/J mice were challenged intraperitonially with spores of either the toxigenic B. anthracis Sterne strain (pXO1+, pXO2-) that is virulent in DBA/2 mice or the nontoxigenic, non-virulent delta Sterne strain (pXO1-, pXO2-). Serum samples were obtained at multiple time points and seperated by continuous flow denaturing gel electrophoresis followed by Coomassie staining to isolate the LMM archive for subsequent MS identification. Peptide fragments derived from more than 200 proteins displayed low-variance differential abundances between lethal and non-lethal challenges. Several proteins from the MS analysis were subjected to secondary verification by western blots. Serum abundances of 6 proteins (carbonic anhydrase 2, adenylate kinase 1, peroxyredoxin 2, UMP-CMP kinase, Ras-related C3 botulinum substrate 1, and destrin) from a total of 10 tested proteins were strongly coincident with established anthrax disease and mortality thus making them potential candidates for hostderived anthrax disease associated BMs. These BMs were demonstrated to be “elastic” in that their abundance levels in sera of doxycycline-treated mice responded to the therapeutic intervention thus making them useful tools for monitoring efficacies of existing and novel treatment regimens.

 
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