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Infection and Immunity, October 2003, p. 5724-5732, Vol. 71, No. 10
0019-9567/03/$08.00+0     DOI: 10.1128/IAI.71.10.5724-5732.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Serum Immunoglobulin G Response to Candidate Vaccine Antigens during Experimental Human Pneumococcal Colonization

Tera L. McCool,1 Thomas R. Cate,2 Elaine I. Tuomanen,3 Peter Adrian,4 Tim J. Mitchell,5 and Jeffrey N. Weiser1*

Departments of Microbiology and Pediatrics, University of Pennsylvania School of Medicine, Philadelphia, Pennsylvania 19104,1 Respiratory Pathogens Research Unit, Baylor College of Medicine, Houston, Texas 77030-3498,2 Department of Infectious Diseases, St. Jude Children's Research Hospital, Memphis, Tennessee 38105,3 Laboratory of Pediatrics, Erasmus University Rotterdam, 3000 DR Rotterdam, The Netherlands,4 Division of Infection and Immunity, Institute of Biomedical and Life Sciences, University of Glasgow, Glasgow G12-8QQ, Scotland5

Received 14 March 2003/ Returned for modification 14 May 2003/ Accepted 21 July 2003

The immune response to pneumococcal surface structures during colonization was examined in a model of experimental human pneumococcal carriage. Healthy uncolonized adults were given a type 23F or 6B pneumococcus, and a portion of these subjects became colonized (6 of 14 with type 23F and 6 of 8 with type 6B). Sera from colonized and uncolonized subjects were used to determine the titer of antibody specific to pneumococcal surface components under consideration in development of noncapsular polysaccharide-based vaccines. These vaccine candidates included pneumococcal surface protein A (PspA), choline binding protein A (CbpA), lipoteichoic acid, immunoglobulin A1 (IgA1) protease, pneumolysin, proteinase maturation protein A, and pneumococcal surface adhesin A. Only the two related choline binding proteins, PspA and CbpA, were immunogenic in colonized subjects as determined by a statistically significant rise in the serum IgG titer. The serum IgG response to PspA was shown previously to correlate inversely with susceptibility to carriage and was localized to a region within the N-terminal portion of PspA. This region is highly variable in amino acid sequence between pneumococcal strains. Despite the sequence diversity in the immunodominant regions of both PspA and CbpA, a significant strain-to-strain cross-reactivity in the serum IgG response following experimental human carriage was observed. These findings support the need for further investigation of the human antibody response to PspA and CbpA and the potential use of one or both of these proteins as novel vaccine antigens for the prevention of pneumococcal colonization.

* Corresponding author. Mailing address: 402A Johnson Pavilion, Department of Microbiology, University of Pennsylvania, Philadelphia, PA 19104-6076. Phone: (215) 573-3511. Fax: (215) 898-9557. E-mail: weiser{at}mail.med.upenn.edu.

Editor: V. J. DiRita

Infection and Immunity, October 2003, p. 5724-5732, Vol. 71, No. 10
0019-9567/03/$08.00+0     DOI: 10.1128/IAI.71.10.5724-5732.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



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