Electron Microscopy of the Major Outer Membrane Protein of Campylobacter jejuni
The surfaces of the disrupted-cell surfaces of the Campylobacter jejuni strains FUM158432 and M1 were examined using the negative-staining technique and electron microscopy. The surfaces of the whole cells and the outer membranes were covered with small dark dots which, in some areas, were arranged...
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| Veröffentlicht in: | MICROBIOLOGY and IMMUNOLOGY 1996, Vol.40(10), pp.749-754 |
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| container_title | MICROBIOLOGY and IMMUNOLOGY |
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| creator | Amako, Kazunobu Wai, Sun Nyunt Umeda, Akiko Shigematsu, Mika Takade, Akemi |
| description | The surfaces of the disrupted-cell surfaces of the Campylobacter jejuni strains FUM158432 and M1 were examined using the negative-staining technique and electron microscopy. The surfaces of the whole cells and the outer membranes were covered with small dark dots which, in some areas, were arranged in hexagonal patterns. The hexagonal arrangement was more clearly seen in extracted outer membrane. The size of each structure was measured based on a center-to-center distance with the adjacent structure, and was determined to be 9.9±0.9nm. A profile of the proteins in the outer membrane by SDS-PAGE, performed in 0.1% SDS and at 100C, showed 42kDa proteins to comprise the major outer membrane protein of this bacterium. Digestion of the outer membrane materials with proteinase reduced this protein band in the SDS-PAGE, and the amount of dark dots on the electron micrograph indicated the structure to be the major outer membrane protein (porin) of this bacterium. The power spectrogram of a computer-assisted Fourier transformation of the hexagonally arranged porin proteins suggests that the porin has a trimeric structure rather than a monomeric one. |
| doi_str_mv | 10.1111/j.1348-0421.1996.tb01136.x |
| format | Article |
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The surfaces of the whole cells and the outer membranes were covered with small dark dots which, in some areas, were arranged in hexagonal patterns. The hexagonal arrangement was more clearly seen in extracted outer membrane. The size of each structure was measured based on a center-to-center distance with the adjacent structure, and was determined to be 9.9±0.9nm. A profile of the proteins in the outer membrane by SDS-PAGE, performed in 0.1% SDS and at 100C, showed 42kDa proteins to comprise the major outer membrane protein of this bacterium. Digestion of the outer membrane materials with proteinase reduced this protein band in the SDS-PAGE, and the amount of dark dots on the electron micrograph indicated the structure to be the major outer membrane protein (porin) of this bacterium. The power spectrogram of a computer-assisted Fourier transformation of the hexagonally arranged porin proteins suggests that the porin has a trimeric structure rather than a monomeric one.</description><identifier>ISSN: 0385-5600</identifier><identifier>EISSN: 1348-0421</identifier><identifier>DOI: 10.1111/j.1348-0421.1996.tb01136.x</identifier><identifier>PMID: 8981348</identifier><identifier>CODEN: MIIMDV</identifier><language>eng</language><publisher>Tokyo: Blackwell Publishing Ltd</publisher><subject>Bacterial Proteins ; Bacteriology ; Biological and medical sciences ; Campylobacter jejuni ; Campylobacter jejuni - chemistry ; Campylobacter jejuni - ultrastructure ; Cell Membrane - chemistry ; Cell Membrane - ultrastructure ; Electron microscopy ; Electrophoresis, Polyacrylamide Gel ; Fourier Analysis ; Fundamental and applied biological sciences. 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The surfaces of the whole cells and the outer membranes were covered with small dark dots which, in some areas, were arranged in hexagonal patterns. The hexagonal arrangement was more clearly seen in extracted outer membrane. The size of each structure was measured based on a center-to-center distance with the adjacent structure, and was determined to be 9.9±0.9nm. A profile of the proteins in the outer membrane by SDS-PAGE, performed in 0.1% SDS and at 100C, showed 42kDa proteins to comprise the major outer membrane protein of this bacterium. Digestion of the outer membrane materials with proteinase reduced this protein band in the SDS-PAGE, and the amount of dark dots on the electron micrograph indicated the structure to be the major outer membrane protein (porin) of this bacterium. The power spectrogram of a computer-assisted Fourier transformation of the hexagonally arranged porin proteins suggests that the porin has a trimeric structure rather than a monomeric one.</description><subject>Bacterial Proteins</subject><subject>Bacteriology</subject><subject>Biological and medical sciences</subject><subject>Campylobacter jejuni</subject><subject>Campylobacter jejuni - chemistry</subject><subject>Campylobacter jejuni - ultrastructure</subject><subject>Cell Membrane - chemistry</subject><subject>Cell Membrane - ultrastructure</subject><subject>Electron microscopy</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Fourier Analysis</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Image processing</subject><subject>Image Processing, Computer-Assisted</subject><subject>Microbiology</subject><subject>Microscopy, Electron</subject><subject>MOMP</subject><subject>Morphology, structure, chemical composition</subject><subject>Outer membrane</subject><subject>Porin</subject><subject>Porins - chemistry</subject><subject>Porins - ultrastructure</subject><issn>0385-5600</issn><issn>1348-0421</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1996</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqVkV2L1DAUhoso67j6E4QiIt50zPeHV-uWdVzYmRFUvAxpeuq29mNMOjjz703tMHilmIskcJ48OZw3SV5gtMRxvWmWmDKVIUbwEmstlmOBMKZieXiQLM6lh8kCUcUzLhB6nDwJoUGISKLYRXKhtJq4RbK9acGNfujTde38ENywO6ZDlY73kK5tM_h0ux_Bp2voCm97SD_6YYS6n5jcdrtjOxTWTUQDzb6vnyaPKtsGeHY6L5Mv728-5x-yu-3qNn93lznJtchYAUAUEooJzQlVBHFSckeJIKXlhRKScaFpqVzFnEUUx4uqmGQYuCoB08vk1ezd-eHHHsJoujo4aNvY47APRirBONPinyDmUiKNJ-Prv4NME4FjgzKib2d0mljwUJmdrzvrjwYjMyVkGjON10wxmCkhc0rIHOLj56d_9kUH5fnpKZJYf3mq2-BsW8WpuzqcMcIJUpRG7GrGftYtHP-jAbO-Xf--RsVqVjRhtN_g7LB-rF0LprN9WWMtpWFoEs-7ZPpMuHvrDfTRlM2mOoxw-EP03QhJJTdfNyuz2mzy_Pr6k8npL8Ig0-k</recordid><startdate>19960101</startdate><enddate>19960101</enddate><creator>Amako, Kazunobu</creator><creator>Wai, Sun Nyunt</creator><creator>Umeda, Akiko</creator><creator>Shigematsu, Mika</creator><creator>Takade, Akemi</creator><general>Blackwell Publishing Ltd</general><general>Center For Academic Publications Japan</general><general>Center for Academic Publications Japan</general><scope>BSCLL</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>C1K</scope><scope>7X8</scope></search><sort><creationdate>19960101</creationdate><title>Electron Microscopy of the Major Outer Membrane Protein of Campylobacter jejuni</title><author>Amako, Kazunobu ; Wai, Sun Nyunt ; Umeda, Akiko ; Shigematsu, Mika ; Takade, Akemi</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c7596-4bee2806846952382052d5c3262da5b86745693d8cf4ca0318cf8f4741e58de13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1996</creationdate><topic>Bacterial Proteins</topic><topic>Bacteriology</topic><topic>Biological and medical sciences</topic><topic>Campylobacter jejuni</topic><topic>Campylobacter jejuni - chemistry</topic><topic>Campylobacter jejuni - ultrastructure</topic><topic>Cell Membrane - chemistry</topic><topic>Cell Membrane - ultrastructure</topic><topic>Electron microscopy</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Fourier Analysis</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Image processing</topic><topic>Image Processing, Computer-Assisted</topic><topic>Microbiology</topic><topic>Microscopy, Electron</topic><topic>MOMP</topic><topic>Morphology, structure, chemical composition</topic><topic>Outer membrane</topic><topic>Porin</topic><topic>Porins - chemistry</topic><topic>Porins - ultrastructure</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Amako, Kazunobu</creatorcontrib><creatorcontrib>Wai, Sun Nyunt</creatorcontrib><creatorcontrib>Umeda, Akiko</creatorcontrib><creatorcontrib>Shigematsu, Mika</creatorcontrib><creatorcontrib>Takade, Akemi</creatorcontrib><collection>Istex</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><jtitle>MICROBIOLOGY and IMMUNOLOGY</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Amako, Kazunobu</au><au>Wai, Sun Nyunt</au><au>Umeda, Akiko</au><au>Shigematsu, Mika</au><au>Takade, Akemi</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Electron Microscopy of the Major Outer Membrane Protein of Campylobacter jejuni</atitle><jtitle>MICROBIOLOGY and IMMUNOLOGY</jtitle><addtitle>Microbiology and Immunology</addtitle><date>1996-01-01</date><risdate>1996</risdate><volume>40</volume><issue>10</issue><spage>749</spage><epage>754</epage><pages>749-754</pages><issn>0385-5600</issn><eissn>1348-0421</eissn><coden>MIIMDV</coden><abstract>The surfaces of the disrupted-cell surfaces of the Campylobacter jejuni strains FUM158432 and M1 were examined using the negative-staining technique and electron microscopy. The surfaces of the whole cells and the outer membranes were covered with small dark dots which, in some areas, were arranged in hexagonal patterns. The hexagonal arrangement was more clearly seen in extracted outer membrane. The size of each structure was measured based on a center-to-center distance with the adjacent structure, and was determined to be 9.9±0.9nm. A profile of the proteins in the outer membrane by SDS-PAGE, performed in 0.1% SDS and at 100C, showed 42kDa proteins to comprise the major outer membrane protein of this bacterium. Digestion of the outer membrane materials with proteinase reduced this protein band in the SDS-PAGE, and the amount of dark dots on the electron micrograph indicated the structure to be the major outer membrane protein (porin) of this bacterium. The power spectrogram of a computer-assisted Fourier transformation of the hexagonally arranged porin proteins suggests that the porin has a trimeric structure rather than a monomeric one.</abstract><cop>Tokyo</cop><pub>Blackwell Publishing Ltd</pub><pmid>8981348</pmid><doi>10.1111/j.1348-0421.1996.tb01136.x</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0385-5600 |
| ispartof | MICROBIOLOGY and IMMUNOLOGY, 1996, Vol.40(10), pp.749-754 |
| issn | 0385-5600 1348-0421 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_78645496 |
| source | J-STAGE Free; MEDLINE; Freely Accessible Japanese Titles; Alma/SFX Local Collection |
| subjects | Bacterial Proteins Bacteriology Biological and medical sciences Campylobacter jejuni Campylobacter jejuni - chemistry Campylobacter jejuni - ultrastructure Cell Membrane - chemistry Cell Membrane - ultrastructure Electron microscopy Electrophoresis, Polyacrylamide Gel Fourier Analysis Fundamental and applied biological sciences. Psychology Image processing Image Processing, Computer-Assisted Microbiology Microscopy, Electron MOMP Morphology, structure, chemical composition Outer membrane Porin Porins - chemistry Porins - ultrastructure |
| title | Electron Microscopy of the Major Outer Membrane Protein of Campylobacter jejuni |
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