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Clinical and Diagnostic Laboratory Immunology, January 2003, p. 88-94, Vol. 10, No. 1
1071-412X/03/$08.00+0     DOI: 10.1128/CDLI.10.1.88-94.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Specificity and Diversity of Antibodies to Mycobacterium tuberculosis Arabinomannan

Josephine Anne D. Navoa,¹ Suman Laal,² Liise-Anne Pirofski,^3,4 Gary R. McLean,^4, Zhongdong Dai,⁵ John B. Robbins,⁵ Rachel Schneerson,⁵ Arturo Casadevall,^3,4 and Aharona Glatman-Freedman^1*

Departments of Pediatrics,¹ Medicine,³ Microbiology and Immunology,⁴ Albert Einstein College of Medicine, Bronx, and Department of Pathology, New York University School of Medicine, New York, New York,² National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland⁵

Received 27 June 2002/ Returned for modification 6 September 2002/ Accepted 14 October 2002

Arabinomannan (AM) is a polysaccharide antigen of the mycobacterial capsule. However, it is uncertain whether AM constitutes an immunologically distinct fraction of Mycobacterium tuberculosis. In this study, we analyzed the repertoire and specificity of antibodies to AM by using AM-binding murine monoclonal antibodies (MAbs) and human serum samples. Murine MAbs were found to be diverse in their specificity to AM and cross-reactivity with other arabinose-containing mycobacterial polysaccharides, with MAb 9d8 binding exclusively to AM. Human antibodies to AM were detected in serum samples from patients with pulmonary tuberculosis (TB), as well as in those from healthy, purified protein derivative-negative controls, with significantly higher titers among patients. The binding of human antibodies to AM was inhibited by MAb 9d8 in three patients with TB but not in controls. MAb 5c11, which recognizes other mycobacterial arabinose-containing carbohydrates in addition to AM, inhibited the binding of serum samples from 75% of patients and 76% of controls. Analysis of human antibodies with murine MAbs to human V_H determinants demonstrated diversity among antibodies to AM with qualitative and quantitative differences compared with antibodies to lipoarabinomannan. In summary, our study suggests that antibodies to AM are diverse and heterogeneous with respect to antigen recognition and V_H determinant expression, with human serum samples containing different subsets of antibodies to AM with the specificities of AM-binding murine MAbs. One MAb and a subset of human antibodies bind AM specifically, suggesting that this polysaccharide is antigenically distinct and is expressed in human infection.

Present address: The Biomedical Research Center, Vancouver, British Columbia, Canada V6T 1Z3.

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