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Deciphering the proteome of the in vivo diagnostic reagent “purified protein derivative” from M ycobacterium tuberculosis
Author(s) -
Cho Yun Sang,
Dobos Karen M.,
Prenni Jessica,
Yang Hongliang,
Hess Ann,
Rosenkrands Ida,
Andersen Peter,
Ryoo Sung Weon,
Bai GillHan,
Brennan Michael J.,
Izzo Angelo,
BielefeldtOhmann Helle,
Belisle John T.
Publication year - 2012
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.201100544
Subject(s) - proteome , mycobacterium tuberculosis , purified protein derivative , heat shock protein , tuberculosis , antigen , biology , in vivo , latent tuberculosis , immunogenicity , tuberculosis vaccines , immunology , microbiology and biotechnology , biochemistry , medicine , gene , pathology
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 . F ood and D rug A dministration ( FDA ) standard PPD ‐ S 2. Many known M ycobacterium tuberculosis T ‐cell antigens were detected. Of significance, four heat shock proteins ( HSP s) (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 ( E sx) proteins. Variability in PPD reagents may explain differences in DTH responses reported among populations.