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Infection and Immunity, March 2003, p. 1033-1041, Vol. 71, No. 3
0019-9567/03/$08.00+0     DOI: 10.1128/IAI.71.3.1033-1041.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Regions of PspA/EF3296 Best Able To Elicit Protection against Streptococcus pneumoniae in a Murine Infection Model

Hazeline Roche, Anders Håkansson, Susan K. Hollingshead, and David E. Briles*

Department of Microbiology, University of Alabama at Birmingham, Birmingham, Alabama

Received 2 July 2002/ Returned for modification 1 August 2002/ Accepted 20 November 2002

Pneumococcal surface protein A (PspA) can elicit protection against Streptococcus pneumoniae in mouse infection models. PspA is classified by serology and amino acid sequence into two major families that are divided by sequence into five clades. The most variable portion of the molecule is the {alpha}-helical domain, which comprises the N-terminal half of PspA. Prior studies of a family 1 PspA protein observed that protective antibodies are reactive with epitopes in the {alpha}-helical domain and that most cross-protective epitopes mapped to the 108 most C-terminal amino acids of the {alpha}-helical region. In these studies, we have used six overlapping recombinant fragments of family 2, clade 3 PspA/EF3296 to map the protection-eliciting regions of its {alpha}-helical domain. The three fragments, which included the 104 most C-terminal amino acids of the {alpha}-helical domain (314 to 418), could each elicit protection against EF3296. A fragment comprising amino acids 75 to 305 failed to elicit significant protection. A fragment containing amino acids 1 to 115 elicited protection against EF3296 in BALB/c mice but not in CBA/N mice. All three fragments containing amino acids 314 to 418 were able to elicit cross-protection against pneumococci expressing PspA proteins of clades 2, 3, 4, and 5. Cross-protection elicited by these three fragments was easier to demonstrate in CBA/N mice than in BALB/c mice. The 1-to-115 fragment, however, elicited some cross-protection against clades 2 and 4 in BALB/c mice but not in CBA/N mice. These studies provide support for the importance of the C-terminal 104 and N-terminal 115 amino acids of the {alpha}-helical region of PspA in the elicitation of cross-protection.

* Corresponding author. Mailing address: Department of Microbiology, University of Alabama at Birmingham, BBRB-662 Box 10, 845 19th St. South, Birmingham, AL 35294. Phone: (205) 934-6595. Fax: (205) 934-0605. E-mail: dbriles{at}uab.edu.

Editor: D. L. Burns

Infection and Immunity, March 2003, p. 1033-1041, Vol. 71, No. 3
0019-9567/03/$08.00+0     DOI: 10.1128/IAI.71.3.1033-1041.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



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