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  • 02월 26일 17시 이후 : 초록수정 불가능, 일정확인 및 검색만 가능

제115회 대한화학회 학술발표회, 총회 및 기기전시회 안내 Structural bases for the inhibition of endosomal trafficking by Legionella pneumophila protein VipD

등록일
2015년 2월 12일 10시 18분 39초
접수번호
0759
발표코드
BIO.O-5 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
발표시간
금 12시 : 00분
발표형식
구두발표
발표분야
생명화학 - Oral Presentation of Young Biochemists
저자 및
공동저자
이광훈
오송첨단의료산업진흥재단 신약개발지원센터, Korea
Legionella pneumophila is a pathogen bacterium that causes Legionnaires' disease accompanied by severe pneumonia. Surprisingly, this pathogen invades and replicates inside macrophages, whose major function is to detect and destroy invading microorganisms. How L. pneumophila can be "immune" to this primary immune cell has been a focus of intensive research. Upon being engulfed by a macrophage cell, L. pneumophila translocates hundreds of bacterial proteins into this host cell. These proteins, called bacterial effectors, are thought to manipulate normal host cellular processes. However, which host molecules and how they are targeted by the bacterial effectors are largely unknown. In this study, we determined the three-dimensional structure of L. pneumophila effector protein VipD, whose function in macrophage was unknown. Ensuing analyses revealed that VipD selectively and tightly binds two host signaling proteins Rab5 and Rab22, which are key regulators of early endosomal vesicle trafficking. These interactions prevent the activated form of Rab5 and Rab22 from binding their downstream signaling proteins, resulting in the blockade of endosomal trafficking in macrophages. This work shows that L. pneumophila targets endosomal Rab proteins and delineates the underlying molecular mechanism, providing a new insight into the pathogen's strategies to dysregulate normal intracellular processes.

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