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Infection and Immunity, May 1999, p. 2138-2144, Vol. 67, No. 5
0019-9567/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Immunization with Recombinant Transferrin Binding Protein B Enhances Clearance of Nontypeable Haemophilus influenzae from the Rat Lung

Dianne C. Webb,1,2,* and Allan W. Cripps1

Gadi Research Centre, Faculty of Applied Science, University of Canberra,1 and Membrane Biochemistry Group, Division of Biochemistry and Molecular Biology, John Curtin School of Medical Research, Australian National University,2 Canberra City, ACT 2601, Australia

Received 28 December 1998/Accepted 26 January 1999

Nontypeable Haemophilus influenzae (NTHI) is an opportunistic pathogen, and heterogeneity in the surface-exposed immunodominant domains of NTHI proteins is thought to be associated with the failure of an infection to stimulate an immune response that is cross-protective against heterologous NTHI strains. The aim of this study was to assess the vaccine potential of a surface-exposed component of the NTHI human transferrin receptor, TbpB, and to determine if the antibody response elicited was cross-reactive with heterologous strains of NTHI. The efficacy of immunization with a recombinant form of TbpB (rTbpB) was determined by assessing the pulmonary clearance of viable bacteria 4 h after a live challenge with NTHI. There was a significant reduction in the number of viable bacteria in both the bronchoalveolar lavage fluid (34% for the 20-µg dose and 58% for the 40-µg dose) and lung homogenates (26% for the 20-µg dose and 60% for the 40-µg dose) of rats immunized with rTbpB compared to the control animals. While rTbpB-specific antibodies from immunized rats were nonspecific in the recognition of TbpB from six heterologous NTHI strains on Western blots, these antibodies differed in their ability to block transferrin binding to heterologous strains and to cross-react in bactericidal assays. If bactericidal antibodies are key indicators of the efficacy of the immune response in eliminating NTHI, this data suggests that while immunization with rTbpB stimulates protective responses against the homologous isolate, variability in the recognition of TbpB from heterologous isolates may limit the potential of rTbpB as an NTHI vaccine component.

* Corresponding author. Present address: Leukocyte Signalling and Regulation Laboratory, John Curtin School of Medical Research, Australian National University, P.O. Box 334, Canberra City, ACT 2601, Australia. Phone: (61) 6 2492267. Fax: (61) 6 2490415. E-mail: Dianne.Webb{at}anu.edu.au.

Infection and Immunity, May 1999, p. 2138-2144, Vol. 67, No. 5
0019-9567/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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