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論文
- タイトル
- タイトル（英）
- Interaction of poliovirus with its purified receptor and conformational alteration in the virion
- 参照URL
- https://researchmap.jp/koike-st/published_papers/37432899
- 著者
- 著者（英）
- M Arita,S Koike,J Aoki,H Horie,A Nomoto
- 担当区分
- 概要
- 概要（英）
- Polypeptides of amino acids 1 to 241 (PVR241) and 1 to 330 (PVR330) of the human poliovirus receptor (hPVR) were produced in a baculovirus expression system. PVR241 contained extracellular domains 1 and 2 of hPVR, and PVR330 contained extracellular domains 1, 2, and 3. These peptides were purified by immunoaffinity column chromatography with an anti-hPVR monoclonal antibody (MAb). After the purification, PVR241 and PVR330 appeared to retain their native conformation as judged by reactivity with an anti-PVR MAb that recognized domain 1 of hPVR in a conformation-dependent manner. The virulent Mahoney strain of poliovirus type 1 was mixed with the purified PVRs in various concentrations. An average of at least 43 PVR330 molecules were able to bind to one virion particle under the conditions used, The equilibrium dissociation constant between the PVR330 molecule and the PVR binding site (canyon) on the virion was determined to be 4.50 +/- (0.86) x 10(-8) M at 4 degrees C. Higher rates of conformational change of the virus (160S) to 135S and 80S particles were observed as the concentration of PVR330 was increased. In this in vitro system, the ratio of the amount of the 135S particle to that of the 80S particle seemed to be always constant. After the disappearance of the 160S particle, the amount of the 80S particle was not increased by further incubation at 37 degrees C. These results suggested that the 80S particle was not derived from the 135S particle under the conditions used in this study.
- 出版者・発行元
- 出版者・発行元（英）
- AMER SOC MICROBIOLOGY
- 誌名
- 誌名（英）
- JOURNAL OF VIROLOGY
- 巻
- 72
- 号
- 5
- 開始ページ
- 3578
- 終了ページ
- 3586
- 出版年月
- 1998年5月
- 査読の有無
- 査読有り
- 招待の有無
- 掲載種別
- 研究論文（学術雑誌）
- ISSN
- 0022-538X
- DOI URL
- 共同研究・競争的資金等の研究課題
研究者
小池 智
(コイケ サトシ)