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Infection and Immunity, August 1999, p. 3793-3799, Vol. 67, No. 8
0019-9567/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Analysis of the Immunological Responses to Transferrin and Lactoferrin Receptor Proteins from Moraxella catarrhalis

Rong-hua Yu,1 Robert A. Bonnah,1 Samuel Ainsworth,2 and Anthony B. Schryvers1,*

Department of Microbiology and Infectious Diseases, University of Calgary, Calgary, Alberta, Canada,1 and Veterans Administration Hospital, Alexandria, Louisiana2

Received 15 October 1998/Returned for modification 10 February 1999/Accepted 5 May 1999

Moraxella catarrhalis expresses surface receptor proteins that specifically bind host transferrin (Tf) and lactoferrin (Lf) in the first step of the iron acquisition pathway. Acute- and convalescent-phase antisera from a series of patients with M. catarrhalis pulmonary infections were tested against Tf and Lf receptor proteins purified from the corresponding isolates. After the purified proteins had been separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and Western blotting, we observed strong reactivity against Tf-binding protein B (TbpB; also called OMP1) and Lf-binding protein B (LbpB) but little or no reactivity against Tf-binding protein A (TbpA) or Lf-binding protein A (LbpA), using the convalescent-phase antisera. Considerable antigenic heterogeneity was observed when TbpBs and LbpBs isolated from different strains were tested with the convalescent-phase antisera. Comparison to the reactivity against electroblotted total cellular proteins revealed that the immune response against LbpB and TbpB constitutes a significant portion of the total detectable immune response to M. catarrhalis proteins. Preparations of affinity-isolated TbpA and LbpA reacted with convalescent-phase antisera in a solid-phase binding assay, but blocking with soluble TbpB, soluble LbpB, or extracts from an LbpA- mutant demonstrated that this reactivity was attributed to contaminants in the TbpA and LbpA preparations. These studies demonstrate the immunogenicity of M. catarrhalis TbpB and LbpB in humans and support their potential as vaccine candidates.

* Corresponding author. Mailing address: Department of Microbiology and Infectious Diseases, University of Calgary, 3330 Hospital Dr., N.W., Calgary, Alberta, T2N 4N1, Canada. Phone: 403-220-3703. Fax: 403-270-2772. E-mail: schryver{at}acs.ucalgary.ca.

Infection and Immunity, August 1999, p. 3793-3799, Vol. 67, No. 8
0019-9567/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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