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Secretory expression of a cell surface protein phospholipase B1 with altered N-glycan structure in the Human Pathogen Cryptococcus neoformans

첫 페이지 보기
  • 발행기관
    한국당과학회 바로가기
  • 간행물
    한국당과학회 학술대회 바로가기
  • 통권
    2013 한국당과학회 동계학술대회 (2013.02)바로가기
  • 페이지
    pp.46-46
  • 저자
    Dong-Jik Lee, Jun Sun Choi, Hyun Ah Kang
  • 언어
    영어(ENG)
  • URL
    https://www.earticle.net/Article/A212708

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원문정보

초록

영어
Cryptococcus neoformans is an encapsulated basidiomycete causing severe diseases, mostly meningoencephalitis, in immunocompromised individuals such as AIDS patients. Secreted phospholipase B1 (PLB1) is important for infection of C. neoformans to the host lung. PLB1 are conserved in all serotypes of C. neoformans, with an overall sequence homology of more than 90%. Previous studies have shown that PLB1 is highly modified by N-linked glycosylation which is essential for the three PLB1 enzymatic activities and secretion. Noticeably, the PLB1 proteins for all cryptococcal serotypes are reported to have different molecular mass, reflecting serotype-specific N-glycans assembled on the secreted PLB1 proteins. As an effort to obtain the purified PLB1 proteins with altered N-glycan structure, which would be used to analyze the effect of N-linked glycans on its role as a virulence determinant we constructed His-tagged and glycosylphosphatidylinositol (GPI) anchorless PLB1 that can be secreted due to lack of membrane association. The GPI anchorless PLB1 protein was expressed in C. neoformans H99 wild type (serotypes A), and glycosylation mutant strains such as Cnoch1Δ, and Cnmnn2Δ, which have defects in the outer chine biosynthesis of N-linked glycans. Compared to the size of the wild type PLB1, those of secreted PLB1 in the mutant strains appeared to be reduced but converged to the same molecular mass after N-glycosidase treatment, indicating the size difference is attributed to the altered structure of N- glycan outer chines. Moreover, the results indicate that the outer chain structures of N-glycans do not crucially affect the secretion efficiency of PLB1.

저자

  • Dong-Jik Lee [ Department of Life Science, Center for Fungal Pathogenesis, Chung-Ang University, Seoul, 156-756, South Korea ]
  • Jun Sun Choi [ Department of Life Science, Center for Fungal Pathogenesis, Chung-Ang University, Seoul, 156-756, South Korea ]
  • Hyun Ah Kang [ Department of Life Science, Center for Fungal Pathogenesis, Chung-Ang University, Seoul, 156-756, South Korea ]

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 2013 한국당과학회 동계학술대회

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