| Literature DB >> 22522804 |
Yun Sang Cho1, Karen M Dobos, Jessica Prenni, Hongliang Yang, Ann Hess, Ida Rosenkrands, Peter Andersen, Sung Weon Ryoo, Gill-Han Bai, Michael J Brennan, Angelo Izzo, Helle Bielefeldt-Ohmann, John T Belisle.
Abstract
Purified protein derivative (PPD) has served as a safe and effective diagnostic reagent for 60 years and is the only broadly available material to diagnose latent tuberculosis infections. This reagent is also used as a standard control for a number of in vitro immunological assays. Nevertheless, the molecular composition and specific products that contribute to the extraordinary immunological reactivity of PPD are poorly defined. Here, a proteomic approach was applied to elucidate the gene products in the U.S. Food and Drug Administration (FDA) standard PPD-S2. Many known Mycobacterium tuberculosis T-cell antigens were detected. Of significance, four heat shock proteins (HSPs) (GroES, GroEL2, HspX, and DnaK) dominated the composition of PPD. The chaperone activities and capacity of these proteins to influence immunological responses may explain the exquisite solubility and immunological potency of PPD. Spectral counting analysis of three separate PPD reagents revealed significant quantitative variances. Gross delayed-type hypersensitivity (DTH) responses in M. tuberculosis infected guinea pigs were comparable among these PPD preparations; however, detailed histopathology of the DTH lesions exposed unique differences, which may be explained by the variability observed in the presence and abundance of early secretory system (Esx) proteins. Variability in PPD reagents may explain differences in DTH responses reported among populations.Entities:
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Year: 2012 PMID: 22522804 PMCID: PMC3756804 DOI: 10.1002/pmic.201100544
Source DB: PubMed Journal: Proteomics ISSN: 1615-9853 Impact factor: 3.984