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Infection and Immunity, October 2000, p. 5778-5784, Vol. 68, No. 10
0019-9567/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Peptide Mimic of Phosphorylcholine, a Dominant Epitope Found on Streptococcus pneumoniae

Shannon L. Harris,1 Moon K. Park,2 Moon H. Nahm,2 and Betty Diamond1,*

Department of Microbiology and Immunology, Albert Einstein College of Medicine, Bronx, New York 10461,1 and Departments of Pediatrics and Pathology, University of Rochester Medical Center, Rochester, New York 146422

Received 23 May 2000/Returned for modification 3 July 2000/Accepted 20 July 2000

Even in the age of antibiotics, Streptococcus pneumoniae causes significant morbidity, especially in the young, the elderly, and the immunocompromised. While a carbohydrate-based vaccine exists, it is poorly immunogenic in the at-risk populations. In mice, antibodies directed against phosphorylcholine (PC), an epitope present on the cell wall C polysaccharide of all pneumococcal serotypes, protect against infection. However, PC itself is a poor vaccine candidate. We report here peptide mimics of PC based on the anti-idiotypic interaction of T15 anti-PC antibodies. T15 antibodies, the dominant and protective idiotype induced in mice by PC immunization, self-associate via a 24-amino-acid region in the PC binding site (ASRNKANDYTTEYSASVKGRFIVS; peptide 1). Peptide 1 has been shown to bind in the PC binding site. We demonstrated that amino acid sequences derived from peptide 1 starting at amino acid 9, 11, or 13 inhibit PC binding. Therefore, we immunized mice with bovine serum albumin (BSA) conjugates of peptide 1 or either of two selected 12-mers. The 12-mer peptides were not immunogenic. Mice immunized with peptide 1-BSA developed an anti-PC response consisting mainly immunoglobulin G1 and expressed the T15 heavy chain. Nonetheless, neither BALB/c nor CBA/N mice were protected from lethal pneumococcal infections by immunization with peptide 1-BSA. Preliminary data suggest that peptide 1-BSA is not able to elicit the canonical T15 light chain, explaining the absence of protection. This idiotype-derived mimotope of PC is a useful tool for understanding immunologic cross-reactivity and learning to design T-cell-dependent vaccines for S. pneumoniae.

* Corresponding author. Mailing address: Department of Microbiology and Immunology, Albert Einstein College of Medicine, 1300 Morris Park Ave., Bronx, NY 10461. Phone: (718) 430-4081. Fax: (718) 430-8711. E-mail: diamond{at}aecom.yu.edu.

Infection and Immunity, October 2000, p. 5778-5784, Vol. 68, No. 10
0019-9567/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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