Demonstration of a Ferric Vibrioferrin-Binding Protein in the Outer Membrane of <i>Vibrio parahaemolyticus</i>
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- Yamamoto Shigeo
- Faculty of Pharmaceutical Sciences, Okayama University
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- Akiyama Toshihito
- Faculty of Pharmaceutical Sciences, Okayama University
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- Okujo Noriyuki
- Faculty of Pharmaceutical Sciences, Okayama University
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- Matsu-ura Shiro
- Division of Biochemistry, Iatron Laboratories, Inc.
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- Shinoda Sumio
- Faculty of Pharmaceutical Sciences, Okayama University
抄録
Under iron-restricted conditions, Vibrio parahaemolyticus produces a siderophore, vibrioferrin, accompanying expression of two major outer membrane proteins of 78 and 83kDa. Autoradiographic analysis of nondenaturing polyacrylamide gel electrophoregrams of outer membrane preparations previously incubated with [55Fe]ferric vibrioferrin revealed a single radiolabeled band, in which the 78-kDa protein was detected predominantly by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The antiserum against the purified 78-kDa protein partially inhibited Fe-VF binding to isolated OMPs. The 78-kDa protein was cleaved by the treatment of whole cells with proteinase K, indicating that a portion of this protein is exposed on the surface of the outer membrane. The treated cells lost most of their iron uptake activity mediated by vibrioferrin. These results suggest that the ferric vibrioferrin-binding protein of 78kDa may function as the receptor for ferric vibrioferrin involved in the initial step of vibrioferrin-mediated iron uptake. Immunoblot analysis using the antiserum against the 78-kDa protein demonstrated that the molecular mass and antigenic properties of the protein were highly conserved among V. parahaemolyticus strains examined. The antiserum also recognized an iron-repressible outer membrane protein of 78kDa from iron-restricted V. alginolyticus strains, some of which appeared to produce vibrioferrin.
収録刊行物
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- MICROBIOLOGY and IMMUNOLOGY
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MICROBIOLOGY and IMMUNOLOGY 39 (10), 759-766, 1995
Center For Academic Publications Japan
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詳細情報 詳細情報について
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- CRID
- 1571980078012202240
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- NII論文ID
- 130003484174
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- ISSN
- 03855600
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- 本文言語コード
- en
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- データソース種別
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- CiNii Articles