ProGP57 (38 kDa antigen)

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ProGP ID ProGP57 (38 kDa antigen)
Validation Status Uncharacterized
Organism Information
Organism NameMycobacterium tuberculosis H37Rv
Domain Bacteria
Classification Phylum : Actinobacteria
Class : Actinomycetia
Orders : Corynebacteriales
Family : Mycobacteriaceae
Genus : Mycobacterium
Species : tuberculosis
Strain : H37Rv
Taxonomic ID (NCBI) 1773
Genome Information
GenBank AL123456.3
EMBL BX842578
Organism Additional Information It is the causative agent of human tuberculosis. The pathogenesis is influenced by its lipoglycans and glycolipids (having a wide range of immunomodulatory activities), and a variety of its virulence factors and antigens.
Protein Information
Protein Name38 kDa antigen
Function It is a disease associated species-specific antigen that displays high immunogenicity at B- and T-cell levels. Two epitopes namely a carbohydrate-dependent and a carbohydrate-independent, have been identified on this antigen using TB71 and TB72 monoclonal antibodies. Owing to its highly specific recognition of patients with lung tuberculosis and its non-reactivity with normal sera. It has a great potential for the serological diagnosis of tuberculosis.
Glycosylation Status
Technique(s) used for Glycosylation DetectionSchiff's reagent staining, peroxidase-conjugated concanavalin A (ConA)-binding
Glycan Information
Glycan Annotation 25.7% carbohydrate estimated by phenol-sulfuric acid assay.
Literature
Year of Identification1989
Year of Identification Month Wise1989.12
ReferenceRosales‐Borjas, D.M., Zambrano‐Villa, S., Elinos, M., Kasem, H., Osuna, A., Mancilla, R. and Ortiz‐Ortiz, L., 1998. Rapid screening test for tuberculosis using a 38‐kDa antigen from Mycobacterium tuberculosis. Journal of clinical laboratory analysis, 12(2), pp.126-129.
Corresponding Author L Ortiz-Ortiz
ContactMiguel Oraá University Hospital, Guanare, Edo. Portuguesa, Venezuela.
ReferenceMehaffy, C., Belisle, J.T. and Dobos, K.M., 2019. Mycobacteria and their sweet proteins: An overview of protein glycosylation and lipoglycosylation in M. tuberculosis. Tuberculosis, 115, pp.1-13.
Corresponding Author Carolina Mehaffy
ContactDepartment of Microbiology, Immunology and Pathology, Colorado State University, 1682 Campus delivery, Fort Collins, CO, USA
Reference Espitia, C. and Mancilla, R. (1989) Identification, isolation and partial characterization of Mycobacterium tuberculosis glycoprotein antigens. Clin Exp Immunol, 77, 378-383. [PubMed: 2478323]
ContactDepartment of Immunology, National Autonomous University of Mexico, D.F