This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Proulx, C Articles by Brodeur, B R Search for Related Content PubMed PubMed Citation Articles by Proulx, C Articles by Brodeur, B R

 Previous Article  |  Next Article 

Infect Immun. 1991 March; 59(3): 963-970

Identification of a surface-exposed immunodominant epitope on outer membrane protein P1 of Haemophilus influenzae type b.

National Laboratory for Immunology, Laboratory Centre for Disease Control, Ottawa, Ontario, Canada.

ABSTRACT

Eight murine monoclonal antibodies (MAbs) directed against outer membrane protein P1 of Haemophilus influenzae type b were generated and characterized. Seven of the eight MAbs reacted with recombinant P1 and purified P1 protein from H. influenzae type b strains MinnA and 1613; MAb P1.8 was specific for the latter strain. A panel of 32 nontypeable and 140 encapsulated Haemophilus strains recovered worldwide representing the major clonal families of serotypes a, b, and d was used to evaluate the distribution among Haemophilus strains of the epitopes identified by the P1-specific MAbs. The epitope reactive with the seven MAbs which recognized P1 from strains MinnA and 1613 was shared by 92% of the encapsulated Haemophilus isolates tested. The epitope is present in the H. influenzae type b strains from clonal families commonly recovered from cases of invasive disease in North America and Europe. A series of nested 5' and 3' deletions of the P1 gene were constructed and analyzed to localize the determinants on P1 recognized by the MAbs. MAbs P1.2, P1.4, P1.5, P1.6, and P1.7 recognized an epitope localized to the carboxy-terminal portion of P1. Murine MAbs P1.1 and P1.3 and two human MAbs, HiH-7 and HiH-10, recognized a complex epitope which was partially localized to the carboxy-terminal portion of the P1 protein. These data indicate that an immunodominant surface-exposed epitope is present on the carboxy-terminal portion of the P1 protein of type b Haemophilus isolates responsible for the majority of invasive disease in North America.

This article has been cited by other articles:

• Hedegaard, J., Okkels, H., Bruun, B., Kilian, M., Mortensen, K. K., Norskov-Lauritsen, N. (2001). Phylogeny of the genus Haemophilus as determined by comparison of partial infB sequences. Microbiology 147: 2599-2609 [Abstract] [Full Text]  
• Bolduc, G. R., Bouchet, V., Jiang, R.-Z., Geisselsoder, J., Truong-Bolduc, Q. C., Rice, P. A., Pelton, S. I., Goldstein, R. (2000). Variability of Outer Membrane Protein P1 and Its Evaluation as a Vaccine Candidate against Experimental Otitis Media due to Nontypeable Haemophilus influenzae: an Unambiguous, Multifaceted Approach. Infect. Immun. 68: 4505-4517 [Abstract] [Full Text]