Analysis of Antibody Responses to Mycobacterium leprae Phenolic Glycolipid I, Lipoarabinomannan, and Recombinant Proteins To Define Disease Subtype-Specific Antigenic Profiles in Leprosy

Author:

Spencer John S.12345,Kim Hee Jin12345,Wheat William H.12345,Chatterjee Delphi12345,Balagon Marivic V.12345,Cellona Roland V.12345,Tan Esterlina V.12345,Gelber Robert12345,Saunderson Paul12345,Duthie Malcolm S.12345,Reece Stephen T.12345,Burman William12345,Belknap Robert12345,Mac Kenzie William R.12345,Geluk Annemieke12345,Oskam Linda12345,Dockrell Hazel M.12345,Brennan Patrick J.12345

Affiliation:

1. Department of Microbiology, Immunology and Pathology, Colorado State University, Fort Collins, Colorado

2. Leonard Wood Memorial Leprosy Research Center, Cebu, Philippines

3. Infectious Disease Research Institute, Seattle, Washington

4. Denver Health, Denver, Colorado

5. Centers for Disease Control, Atlanta, Georgia

Abstract

ABSTRACT A simple serodiagnostic test based on the Mycobacterium leprae -specific phenolic glycolipid I(PGL-I), for individuals with leprosy is nearly universally positive in leprosy patients with high bacillary loads but cannot be used as a stand-alone diagnostic test for the entire spectrum of the disease process. For patients with early infection with no detectable acid-fast bacilli in lesions or with low or no antibody titer to PGL-I, as in those at the tuberculoid end of the disease spectrum, this diagnostic approach has limited usefulness. To identify additional M. leprae antigens that might enhance the serological detection of these individuals, we have examined the reactivity patterns of patient sera to PGL-I, lipoarabinomannan (LAM), and six recombinant M. leprae proteins (ML1877, ML0841, ML2028, ML2038, ML0380, and ML0050) by Western blot analysis and enzyme-linked immunosorbent assay (ELISA). Overall, the responses to ML2028 (Ag85B) and ML2038 (bacterioferritin) were consistently high in both multibacillary and paucibacillary groups and weak or absent in endemic controls, while responses to other antigens showed considerable variability, from strongly positive to completely negative. This analysis has given a clearer understanding of some of the differences in the antibody responses between individuals at opposite ends of the disease spectrum, as well as illustrating the heterogeneity of antibody responses toward protein, carbohydrate, and glycolipid antigens within a clinical group. Correlating these response patterns with a particular disease state could allow for a more critical assessment of the form of disease within the leprosy spectrum and could lead to better patient management.

Publisher

American Society for Microbiology

Subject

Microbiology (medical),Clinical Biochemistry,Immunology,Immunology and Allergy

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