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Characterization of the Streptococcus pneumoniae BgaC protein as a novel surface β -galactosidase with specific hydrolysis activity for the Galβ1-3GlcNAc moiety of oligosaccharide

첫 페이지 보기
  • 발행기관
    한국당과학회 바로가기
  • 간행물
    한국당과학회 학술대회 바로가기
  • 통권
    2008 Eastern Asian Glycoscience Symposium (2008.11)바로가기
  • 페이지
    pp.47-48
  • 저자
    Yun Mi Lee, Jae Kap Jeong, Ohsuk Kwon, Doo-Byoung Oh, Jung Mi Lee, Seonghun Kim, Eun-Hye Kim, Tu Nhat Le, Dong-Kwon Rhee, Hyun-Ah Kang
  • 언어
    영어(ENG)
  • URL
    https://www.earticle.net/Article/A192320

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원문정보

초록

영어
Streptococcus pneumoniae is a causative agent for high morbidity and mortality. Although sugar moieties have been recognized as a ligand for initial contact with the host, only a few exoglycosidaseshave been reported in S. pneumoniae. In this study, a putative -galactosidase, encoded by the bgaC gene of S. pneumoniae, was characterized for its enzymatic activity and virulence. The recombinant BgaC protein, expressed and purified from Escherichia coli, was found to have a highly regiospecific and sugar specific hydrolysis activity for the Gal1-3-GlcNAc moiety of oligosaccharide. Interestingly, the BgaC hydrolysis activity was localized at the cell surface of S. pneumoniae, indicating that BgaC is expressed as a surface protein although it does not have a typical signal sequenceor membrane anchorage motif. The surface localization of BgaC was further supported by immunofluorescence microscopy analysis using an antibody raised against BgaC. Although the bgaC deletion mutation did not significantly attenuate the virulence of S. pneumoniae in vivo, the bgaC mutant strain showed relatively lower viable cell numbers compared to the wild type after 24 h infection in vivo, whereas it showed higher adherence and invasion at 6 and 12 h post- infection in vivo. Our data strongly indicate for the first time that S. pneumoniae bgaC encodes a surface β-galactosidase with high substrate specificity that is significantly associated with the infection activity of pneumococci.

저자

  • Yun Mi Lee [ Omics and Integration Research Center, KRIBB, Daejeon 305-333, Korea ]
  • Jae Kap Jeong [ Omics and Integration Research Center, KRIBB, Daejeon 305-333, Korea ]
  • Ohsuk Kwon [ Omics and Integration Research Center, KRIBB, Daejeon 305-333, Korea ]
  • Doo-Byoung Oh [ Omics and Integration Research Center, KRIBB, Daejeon 305-333, Korea ]
  • Jung Mi Lee [ Omics and Integration Research Center, KRIBB, Daejeon 305-333, Korea ]
  • Seonghun Kim [ Omics and Integration Research Center, KRIBB, Daejeon 305-333, Korea ]
  • Eun-Hye Kim [ College of Pharmacy, Sungkyunkwan University, Suwon 440-746, Korea ]
  • Tu Nhat Le [ College of Pharmacy, Sungkyunkwan University, Suwon 440-746, Korea ]
  • Dong-Kwon Rhee [ College of Pharmacy, Sungkyunkwan University, Suwon 440-746, Korea ]
  • Hyun-Ah Kang [ Department of Life Science, Chung-Ang University ]

참고문헌

자료제공 : 네이버학술정보

간행물 정보

발행기관

  • 발행기관명
    한국당과학회 [Korean Society for Glycoscience]
  • 설립연도
    2006
  • 분야
    의약학>약학
  • 소개
    본 학회는 화학, 생화학, 분자생물학, 미생물학, 식품공학, 의학, 약학, 유전공학 및 생물공학, 환경 및 기타 공업 등 전 분야의 탄수화물관련 이론과 기술을 연구 발전시키고 산학협동을 통해 이를 보급하여 국내 관련 산업의 발전 및 국민생활의 과학화에 기여하고자 하며, 이러한 목표와 비젼의 실현을 위해 회원들이 적극적인 참여와 활동을 전개하고자 한다.

간행물

  • 간행물명
    한국당과학회 학술대회
  • 간기
    연간
  • 수록기간
    2006~2022
  • 십진분류
    KDC 517 DDC 614

이 권호 내 다른 논문 / 한국당과학회 학술대회 2008 Eastern Asian Glycoscience Symposium

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