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Infection and Immunity, February 2001, p. 773-778, Vol. 69, No. 2
Department of
Microbiology1 and Division of Infectious
Diseases, Department of Medicine,2 State
University of New York at Buffalo, and Veterans Affairs Western
New York Healthcare System,3 Buffalo, New York
14215
Received 22 May 2000/Returned for modification 5 July 2000/Accepted 11 November 2000
The P2 porin protein is the most abundant protein in the outer
membrane of nontypeable Haemophilus influenzae (NTHI).
Analysis of sequences of P2 from different strains reveals the presence of both heterogeneous and conserved surface-exposed loops of the P2
molecule among strains. The present study was undertaken to test the
hypothesis that antibodies to a conserved surface-exposed loop are
bactericidal for multiple strains of NTHI and could thus form the basis
of vaccines to prevent infection due to NTHI. Polyclonal antiserum to a
peptide corresponding to loop 6 was raised and was immunopurified over
a loop 6 peptide column. Analysis of the antibodies to whole organisms
and peptides corresponding to each of the eight loops of P2 by
immunoassays revealed that the antibodies were highly specific for loop
6 of P2. The immunopurified antibodies bound to P2 of 14 of 15 strains
in immunoblot assays. These antibodies to loop 6 demonstrated
complement-mediated bactericidal killing of 8 of 15 strains. These
results support the concept of using conserved regions of the P2
protein as a vaccine antigen.
0019-9567/01/$04.00+0 DOI: 10.1128/IAI.69.2.773-778.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
Antibodies to Loop 6 of the P2 Porin Protein of
Nontypeable Haemophilus influenzae Are Bactericidal against
Multiple Strains
*
Corresponding author. Mailing address: VA Western New
York Healthcare System, Medical Research 151, 3495 Bailey Ave.,
Buffalo, NY 14215. Phone: (716) 862-7874. Fax: (716) 862-6526. E-mail: murphyt{at}acsu.buffalo.edu.
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