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Clinical and Vaccine Immunology, May 2009, p. 653-659, Vol. 16, No. 5
1071-412X/09/$08.00+0     doi:10.1128/CVI.00460-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Identification of Domains of the Hag/MID Surface Protein Recognized by Systemic and Mucosal Antibodies in Adults with Chronic Obstructive Pulmonary Disease following Clearance of Moraxella catarrhalis{triangledown}

Eric R. LaFontaine,1 Lauren E. Snipes,1 Brian Bullard,1,{dagger} Aimee L. Brauer,2 Sanjay Sethi,3,5 and Timothy F. Murphy2,4,5*

Department of Infectious Diseases, College of Veterinary Medicine, University of Georgia, Athens, Georgia 30602,1 Divisions of Infectious Diseases,2 Pulmonary and Critical Care Medicine of the Department of Medicine,3 Department of Microbiology, University at Buffalo, State University of New York,4 Veterans Affairs Western New York Healthcare System, Buffalo, New York 142155

Received 3 December 2008/ Returned for modification 2 January 2009/ Accepted 15 March 2009

Moraxella catarrhalis is a common cause of respiratory tract infection in the setting of chronic obstructive pulmonary disease (COPD). Adults with COPD acquire and clear strains of M. catarrhalis from the respiratory tract continuously and develop strain-specific protection following clearance of a strain. In previous work, we identified Hag/MID (Moraxella immunoglobulin D-binding protein), a large multifunctional surface protein that acts as an adhesin and hemagglutinin, as a target of antibody responses in adults with COPD after clearance of M. catarrhalis. The goal of the present study was to characterize the domains of Hag/MID to which humans make antibodies, including both systemic and mucosal antibody responses. Analysis of recombinant peptide constructs, which spanned the M. catarrhalis strain O35E Hag/MID protein, with well-characterized serum and sputum samples revealed that most adults with COPD made antibodies directed toward a region of the molecule bounded by amino acids 706 to 863. Serum immunoglobulin G (IgG) and IgA purified from sputum both recognized the same domain. Some flanking sequence of this fragment was necessary for the epitope(s) in this region to maintain its conformation to bind human antibodies. These results reveal that humans consistently generate both systemic and mucosal antibody responses to an immunodominant region of the Hag/MID molecule, which was previously shown to overlap with several biologically relevant domains, including epithelial cell adherence, IgD binding, collagen binding, and hemagglutination.

* Corresponding author. Mailing address: VA Western New York Healthcare System, Medical Research 151, 3495 Bailey Avenue, Buffalo, NY 14215. Phone: (716) 862-7874. Fax: (716) 862-6526. E-mail: murphyt{at}buffalo.edu

{triangledown} Published ahead of print on 25 March 2009.

{dagger} Present address: Department of Molecular Virology, Immunology and Medical Genetics, Ohio State University, Columbus, OH 43210.

Clinical and Vaccine Immunology, May 2009, p. 653-659, Vol. 16, No. 5
1071-412X/09/$08.00+0     doi:10.1128/CVI.00460-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • de Vries, S. P. W., Bootsma, H. J., Hays, J. P., Hermans, P. W. M. (2009). Molecular Aspects of Moraxella catarrhalis Pathogenesis. Microbiol. Mol. Biol. Rev. 73: 389-406 [Abstract] [Full Text]  


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