The Purification and Immunogenicity of Pneumococcal Surface Protein (PspA) from Invasive Streptococcus pneumoniae KNIH1156 Isolated in Korea

국내 임상 분리주 Streptococcus pneumoniae KNIH1156으로부터 PspA 단백 항원의 정제 및 면역원성 확인

  • 정경석 (안산 1 대학 임상병리과) ;
  • 배송미 (국립보건원 세균부 호흡기 세균과)
  • Published : 2002.03.01


Pneumococcal surfacce protein A (PspA) is an important virulence factor and an antigenically variable surface protein of the pneumococci. To purify the PspA from S. pneumoniae KNIH1156 , a clinical isolate (type 19F), we have taken advantage of the fact that PspA is released from the surface of pneumococci into the medium by growing in a CDM-ET medium and PspA is capable of binding human lactoferrin, the iron carrier protein. PspA of S. pneumoniae KNIH1156 was purified from culture supernatant by human lactoferrin (hLf) affinity chromatography. The purified PspA was confirmed with anti-PspA antiserum and also had the binding capacity to hLf specifically. To determine whether the purified PspA could elicit protection in mice against pneumococcal inflection, we immunized the mice with purified PspA and subsequently challenged with S. pneumoniae KNIH1156. Immunization with purified PspA protected mice from 500 times the $LD^{50}$ of S. pneumoniae KNIH1156. Therefore, it has been shown that purified PspA fromS. pneumoniae KNIH1156 (type 19F) is a protective immunogen.


antigen;PspA;purification;Streptococcus pneumoniae;virulence


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