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Novel Features of Protein Glycosylation in the Human Pathogenic Yeast Cryptococcus neoformans

첫 페이지 보기
  • 발행기관
    한국당과학회 바로가기
  • 간행물
    한국당과학회 학술대회 바로가기
  • 통권
    2016 한국당과학회 동계학술대회 (2016.01)바로가기
  • 페이지
    pp.30-31
  • 저자
    Dong Jik Lee, Eun jung Tak, Seung Yeon Chung, Hyun Ah Kang
  • 언어
    영어(ENG)
  • URL
    https://www.earticle.net/Article/A294684

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원문정보

초록

영어
The encapsulated basidiomycetous Cryptococcus neoformans species complex is an opportunistic fungal pathogen causing fatal cryptococcal meningoencephalitis in immunocompromised populations, such as AIDS patients. In this presentation, we report the unique structure and biosynthesis pathway of N-/O-glycans and their physiological roles in C. neoformans. By analyzing oligosaccharide profiles combined with exoglycosidase treatment, C. neoformans was shown to have serotype-specific high-mannose type N-glycans with or without xylose residue. Moreover, comparative analysis of acidic N-glycan profiles from wild-type and och1Δ, mnn2Δ, and uxs1Δ mutant strains strongly indicated the presence of xylose-phosphates attached to mannose residues in the core form and outer chain of N-glycans (1). We further showed that the major C. neoformans O-glycans were short manno-oligosaccharides that were connected mostly by α1,2-linkages but connected by an α 1,6-linkage at the third mannose residue. C. neoformans KTR3 was shown to be responsible for the addition of the second α1,2 mannose residue to the major O-glycans lacking xylose. The ktr3Δ mutant strain displayed attenuated virulence in a mouse model of cryptococcosis, suggesting that the extended structure of O-glycans is required for full pathogenicity of C. neoformans. Intriguingly, C. neoformans HOC1 and HOC3, homologs of the Saccharomyces cerevisiae OCH1 family genes, were shown to transfer the third mannose residue, via an α1,6 linkage, to minor O-glycans containing xylose and to major O-glycans without xylose, respectively, indicating two independent O-glycan biosynthesis pathways involving different sets of processing enzymes in C. neoformans (2). The glycosylation-defective mutant strains developed in our study are currently used for systematic investigation on how structural alterations of N-/O-glycans affect the intensity of virulence and the extent of host immunological interactions in C. neoformans.

저자

  • Dong Jik Lee [ Department of Life Science, Chung-Ang University ]
  • Eun jung Tak [ Department of Life Science, Chung-Ang University ]
  • Seung Yeon Chung [ Department of Life Science, Chung-Ang University ]
  • Hyun Ah Kang [ 강현아 | 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 2016 한국당과학회 동계학술대회

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