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Characterization of the gene encoding a 26-kilodalton protein (OMP26) from nontypeable Haemophilus influenzae and immune responses to the recombinant protein

journal contribution
posted on 06.12.2017, 00:00 by W El-Adhami, Jennelle Kyd, D Bastin, A Cripps
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% (1isolate) 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 effectiveas 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.

Funding

Category 1 - Australian Competitive Grants (this includes ARC, NHMRC)

History

Volume

67

Issue

4

Start Page

1935

End Page

1942

Number of Pages

8

eISSN

1070-6313

ISSN

0019-9567

Location

United States

Publisher

American Society for Microbiology

Language

en-aus

Peer Reviewed

Yes

Open Access

No

External Author Affiliations

University of Canberra;

Era Eligible

No

Journal

Infection and immunity.

Exports

CQUniversity

Exports