Deciphering the proteome of the in vivo diagnostic reagent "purified protein derivative" from Mycobacterium tuberculosis

Cho, Yun Sang, Dobos, Karen M., Prenni, Jessica, Yang, Hongliang, Hess, Ann, Rosenkrands, Ida, Andersen, Peter, Ryoo, Sung Weon, Bai, Gill-Han, Brennan, Michael J., Izzo, Angelo, Bielefeldt-Ohmann, Helle and Belisle, John T. (2012) Deciphering the proteome of the in vivo diagnostic reagent "purified protein derivative" from Mycobacterium tuberculosis. Proteomics, 12 7: 979-991. doi:10.1002/pmic.201100544

Author Cho, Yun Sang
Dobos, Karen M.
Prenni, Jessica
Yang, Hongliang
Hess, Ann
Rosenkrands, Ida
Andersen, Peter
Ryoo, Sung Weon
Bai, Gill-Han
Brennan, Michael J.
Izzo, Angelo
Bielefeldt-Ohmann, Helle
Belisle, John T.
Title Deciphering the proteome of the in vivo diagnostic reagent "purified protein derivative" from Mycobacterium tuberculosis
Journal name Proteomics   Check publisher's open access policy
ISSN 1615-9853
Publication date 2012
Year available 2012
Sub-type Article (original research)
DOI 10.1002/pmic.201100544
Volume 12
Issue 7
Start page 979
End page 991
Total pages 13
Place of publication Weinheim, Germany
Publisher Wiley - V C H Verlag GmbH and Co. KGaA
Collection year 2013
Language eng
Subject 1312 Molecular Biology
1303 Specialist Studies in Education
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.
Keyword Microbiology
Mycobacterium tuberculosis
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Non-UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Non HERDC
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