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Infection and Immunity, October 2006, p. 5888-5892, Vol. 74, No. 10
0019-9567/06/$08.00+0 doi:10.1128/IAI.00553-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.
Department of Microbiology, University of Mississippi Medical Center, 2500 N. State Street, Jackson, Mississippi 39216,1 Research Service, Veterans Affairs Medical Center, 1500 Woodrow Wilson Drive, Jackson, Mississippi 392162
Received 4 April 2006/ Returned for modification 24 May 2006/ Accepted 7 July 2006
The human pathogen Streptococcus pneumoniae contains genes for a putative polyamine ABC transporter which are organized in an operon and designated potABCD. Polyamine transport protein D (PotD) is an extracellular protein which binds polyamines and possibly other structurally related molecules. PotD has been shown to contribute to virulence in both a murine sepsis model and a pneumonia model with capsular type 3 pneumococci. The protective efficacy of recombinant PotD was evaluated by active immunization and intravenous challenge with capsular type 3 pneumococci in CBA/N mice. Immunized mice had 91.7% survival following lethal pneumococcal challenge, compared with 100% mortality in the control group. Immunized animals had high-titer anti-PotD antibodies following three immunizations with alum. Protection in a sepsis model was also seen after passive administration of rabbit antiserum raised against PotD (P < 0.004). These results suggest that antibodies to PotD confer protection against invasive pneumococcal disease and that this protein should be studied further as a potential vaccine candidate for protection against invasive pneumococcal infections.
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