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Infection and Immunity, September 1999, p. 4578-4585, Vol. 67, No. 9
0019-9567/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Analysis of Antigenic Structure and Human Immune Response to Outer Membrane Protein CD of Moraxella catarrhalis

Timothy F. Murphy,1,2,3,* Charmaine Kirkham,1 Ernesto DeNardin,4 and Sanjay Sethi3,5

Divisions of Infectious Diseases1 and Pulmonary and Critical Care Medicine,5 Department of Medicine, and Department of Microbiology,2 School of Medicine and Biomedical Sciences, and Department of Oral Biology, School of Dental Medicine,4 State University of New York at Buffalo, and the Veterans Affairs Western New York Healthcare System,3 Buffalo, New York 14215

Received 16 April 1999/Returned for modification 21 May 1999/Accepted 21 June 1999

Moraxella catarrhalis is an important cause of otitis media in children and lower respiratory tract infections in adults with chronic obstructive pulmonary disease (COPD). Outer membrane protein CD (OMP CD) is a 45-kDa protein which is a potential vaccine antigen to prevent infections caused by M. catarrhalis. Eight monoclonal antibodies were used to study the antigenic structure of the OMP CD molecule by assaying recombinant peptides corresponding to the sequence of the protein. This approach identified two surface-exposed epitopes, including one near the amino terminus (amino acids 25 to 44) and one in the central region of the molecule (amino acids 261 to 331). Assays with serum and sputum supernatants of adults with COPD revealed variable levels of antibodies to OMP CD among individuals. To determine which portions of the OMP CD molecule were recognized by human antibodies, three human serum samples were studied with six recombinant peptides which span the sequence of OMP CD. All three sera contained immunoglobulin G antibodies which recognized exclusively the peptide corresponding to amino acids 203 to 260 by immunoblot assay. Adsorption experiments with whole bacteria established that some of the human antibodies are directed at surface-exposed epitopes on OMP CD. We conclude that OMP CD is a highly conserved molecule which contains at least two separate epitopes which are exposed on the bacterial surface. While individual adults with COPD show variability in the immune response to OMP CD, a specific region of the OMP CD molecule (amino acids 203 to 260) is important as a target of the human immune response.


* Corresponding author. Mailing address: Veterans Affairs Western New York Healthcare System, Medical Research 151, 3495 Bailey Ave., Buffalo, NY 14215. Phone: (716) 829-2173. Fax: (716) 862-6526. E-mail: murphyt{at}acsu.buffalo.edu.


Infection and Immunity, September 1999, p. 4578-4585, Vol. 67, No. 9
0019-9567/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.



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