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Infection and Immunity, April 2000, p. 2119-2128, Vol. 68, No. 4
Department of Pediatrics, Division of
Molecular Medicine, The Ohio State University College of Medicine and
Public Health, Columbus, Ohio,1 and
Department of Microbiology and Immunology, University of
Rochester Medical Center, Rochester, New York2
Received 28 October 1999/Returned for modification 6 December
1999/Accepted 6 January 2000
To identify potential immunodominant and/or adhesin binding domains
of the outer membrane protein P5-homologous fimbrin adhesin of
nontypeable Haemophilus influenzae (NTHI), three sets of
synthetic peptides were synthesized and assayed in an adherence
inhibition assay, by Western blotting, and in a biomolecular
interaction analysis (BIA) system. The first series of 34 8- to 10-mer
peptides represented the entire mature protein sequentially. The second set of four peptides (each 19 to 28 residues) represented the four
predicted major surface-exposed regions (or loops) of this adhesin. The
third series of seven peptides (each 27 to 34 residues) were
specifically designed to map the third surface-exposed region. Data
obtained by BIA indicated limited reactivity of a panel of high-titered
immune chinchilla sera to the 8- to 10-mer peptides representing the
mature protein, likely because these linear peptides did not represent
continuous epitopes. However, several of these short peptides did
inhibit adherence of multiple NTHI strains to a human respiratory
epithelial cell. Overall, greatest relative reactivity in both BIA and
adherence inhibition assays was demonstrated against, or shown by,
peptides mapping to the third and fourth predicted surface-exposed
regions of this adhesin, thereby indicating the presence of
immunodominant and adhesin binding domains at these sites. Middle ear
fluids sequentially recovered from a chinchilla with an ongoing
NTHI-induced otitis media (OM) as well as sera from children with OM
due to NTHI also reacted exclusively with peptides representing the
third and fourth surface-exposed regions of the P5-fimbrin adhesin,
indicating a similarity in immune recognition of this bacterial protein
by these two hosts. Collectively, these data together with the
previously demonstrated protective efficacy of immunogens derived from
this adhesin in chinchilla models support the continued development of
P5-fimbrin based vaccine components.
0019-9567/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
Epitope Mapping of the Outer Membrane Protein P5-Homologous
Fimbrin Adhesin of Nontypeable Haemophilus
influenzae
*
Corresponding author. Mailing address: Department of
Pediatrics, Division of Molecular Medicine, The Ohio State University College of Medicine and Public Health, Children's Research Institute, Rm. W302, 700 Children's Dr., Columbus, OH 43205-2696. Phone: (614)
722-2915. Fax: (614) 722-2716. E-mail:
BakaletL{at}pediatrics.ohio-state.edu.
Infection and Immunity, April 2000, p. 2119-2128, Vol. 68, No. 4
0019-9567/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
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