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학술연구/단체지원/교육 등 연구자 활동을 지속하도록 DBpia가 지원하고 있어요.
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연구자들이 자신의 연구와 전문성을 널리 알리고, 새로운 협력의 기회를 만들 수 있는 네트워킹 공간이에요.
논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 발행연도
- 2002.1
- 수록면
- 332 - 339 (8page)
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CD9 plays an critical role in the diapedesis of port of MHC molecules. Engagement of CD9 by agonistic monoclonal antibodies has been re-ported to triger multifactorial events including T cell activation as well as cell-cell adhesion during hematopoietic cell diferentiation. In this study, to identify the functional domains partici-pating in the celular events, we mapped the epitopes of CD99, which are recognized by two agonistic CD99 monoclonal antibodies, DN16 and YG32. Using recombinant fusion proteins of GST with whole or parts of CD9, we found that both antibodies interact with CD9 molecules independently of sugar moieties. DN16 mAb de-tected a linear epitope located in the amino terminal region of CD99 while YG32 mAb bound another linear epitope in the center of the extra-celular domain. To confirm that the identified epitopes of CD99 are actualy recognized by the two mAbs, we showed the presence of physical interaction betwen the mAbs and the fusion proteins or synthetic peptides containing the corresponding epitopes using surface plasmon resonance analyses. The dissociation constants of DN16 and YG32 mAbs for the antigen were calculated as 1.2710-7 and 7.0810-9 M, re-spectively. These studies will help understand the functional domains and the subsequent signaling mechanism of CD99.
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