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Infection and Immunity, April 1999, p. 1935-1942, Vol. 67, No. 4
Gadi Research Centre, Faculty of Applied
Science, University of Canberra, Canberra, Australian Capital
Territory 2601, Australia
Received 22 September 1998/Returned for modification 12 November
1998/Accepted 3 December 1998
A 26-kDa protein (OMP26) isolated and purified from nontypeable
Haemophilus influenzae (NTHI) strain 289 has been shown to enhance clearance of infection following pulmonary challenge with NTHI
in rats. DNA sequence analysis revealed that it was 99% identical to a
gene encoding a cell envelope protein of the H. influenzae Rd strain (TIGR accession no. HI0916). The deduced amino acid sequence
revealed a hydrophilic polypeptide rich in basic amino acids.
Restriction fragment length polymorphism analysis suggested that the
OMP26 gene was relatively conserved among isolates of NTHI. Analysis of
the deduced amino acid sequence of the OMP26 gene from 20 different
isolates showed that similarity with NTHI-289 ranged from 96.5% (1 isolate) to 99.5% (14 isolates). Two recombinant forms of OMP26, a
full length 28-kDa protein (equivalent to preprotein) and a 26-kDa
protein lacking a 23-amino-acid leader peptide (equivalent to processed
protein), were assessed in immunization studies for the ability to
induce an immune response that would be as effective as the native
protein in enhancing the clearance of NTHI following pulmonary
challenge in rats. Immunization with the recombinant protein that
included the leader peptide was more effective in enhancing pulmonary
clearance, and it induced a better cell-mediated response and higher
titers of systemic and mucosal antibody. This study has characterized a
26-kDa protein from NTHI that shows significant potential as a vaccine candidate.
0019-9567/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
Characterization of the Gene Encoding a
26-Kilodalton Protein (OMP26) from Nontypeable Haemophilus
influenzae and Immune Responses to the Recombinant
Protein
*
Corresponding author. Mailing address: Faculty of
Applied Science, University of Canberra, ACT 2601, Australia. Phone:
61-2-6201 2160. Fax: 61-2-6201 2461. E-mail:
kyd{at}science.canberra.edu.au.
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