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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; Belisle, John T.
Affiliation
  • Cho YS; Mycobacteria Research Laboratories, Department of Microbiology, Immunology, and Pathology, Colorado State University, Fort Collins, CO, USA.
Proteomics ; 12(7): 979-91, 2012 Apr.
Article in En | MEDLINE | ID: mdl-22522804
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.
Subject(s)

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Bacterial Proteins / Tuberculin / Proteome / Mycobacterium tuberculosis / Antigens, Bacterial Type of study: Diagnostic_studies Limits: Animals Language: En Journal: Proteomics Journal subject: BIOQUIMICA Year: 2012 Type: Article Affiliation country: United States

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Bacterial Proteins / Tuberculin / Proteome / Mycobacterium tuberculosis / Antigens, Bacterial Type of study: Diagnostic_studies Limits: Animals Language: En Journal: Proteomics Journal subject: BIOQUIMICA Year: 2012 Type: Article Affiliation country: United States