Comparative imaging of a bacterial surface‐located GFP fusion protein by epifluorescence and scanning near‐field optical microscopy
Summary IcsA is an autotransporter protein that plays a role in the virulence of Shigella bacteria. We have examined the cellular localization of a fusion of an IcsA fragment to the green fluorescent protein (GFP) expressed in Escherichia coli using a dual epifluorescence and scanning near‐field opt...
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| Veröffentlicht in: | Journal of microscopy (Oxford) 2005-04, Vol.218 (1), p.46-51 |
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| container_title | Journal of microscopy (Oxford) |
| container_volume | 218 |
| creator | GUNNING, A. P. BONGAERTS, R. J. M. KIRBY, A. R. HINTON, J. C. D. MORRIS, V. J. |
| description | Summary
IcsA is an autotransporter protein that plays a role in the virulence of Shigella bacteria. We have examined the cellular localization of a fusion of an IcsA fragment to the green fluorescent protein (GFP) expressed in Escherichia coli using a dual epifluorescence and scanning near‐field optical microscope. By combining the data obtained from far‐field with near‐field microscopy of the same sample, discrimination between surface‐bound fusion proteins and fusion proteins located in the cellular cytoplasm becomes possible. Furthermore, and for the first time, the inherent advantages in resolution of the near‐field images provides highly specific details of the location of a GFP fusion protein on a bacterial cell surface. |
| doi_str_mv | 10.1111/j.1365-2818.2005.01464.x |
| format | Article |
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IcsA is an autotransporter protein that plays a role in the virulence of Shigella bacteria. We have examined the cellular localization of a fusion of an IcsA fragment to the green fluorescent protein (GFP) expressed in Escherichia coli using a dual epifluorescence and scanning near‐field optical microscope. By combining the data obtained from far‐field with near‐field microscopy of the same sample, discrimination between surface‐bound fusion proteins and fusion proteins located in the cellular cytoplasm becomes possible. Furthermore, and for the first time, the inherent advantages in resolution of the near‐field images provides highly specific details of the location of a GFP fusion protein on a bacterial cell surface.</description><identifier>ISSN: 0022-2720</identifier><identifier>EISSN: 1365-2818</identifier><identifier>DOI: 10.1111/j.1365-2818.2005.01464.x</identifier><identifier>PMID: 15817062</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Science Ltd</publisher><subject>AFM ; Bacterial Proteins - genetics ; Bacterial Proteins - metabolism ; DNA-Binding Proteins - genetics ; DNA-Binding Proteins - metabolism ; Escherichia coli ; Escherichia coli - genetics ; Escherichia coli - metabolism ; fluorescence ; Green Fluorescent Proteins - genetics ; Green Fluorescent Proteins - metabolism ; IcsA ; Microscopy, Atomic Force ; Microscopy, Fluorescence - methods ; Microscopy, Scanning Probe - methods ; Recombinant Fusion Proteins - genetics ; Recombinant Fusion Proteins - metabolism ; Shigella ; Shigella - genetics ; Transcription Factors - genetics ; Transcription Factors - metabolism</subject><ispartof>Journal of microscopy (Oxford), 2005-04, Vol.218 (1), p.46-51</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c3434-bc5dfa921c39e64a7ede9fc6f9636ba30b564a94af47c18310d8e01283d0481e3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1111%2Fj.1365-2818.2005.01464.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fj.1365-2818.2005.01464.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1417,1433,27924,27925,45574,45575,46409,46833</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15817062$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>GUNNING, A. P.</creatorcontrib><creatorcontrib>BONGAERTS, R. J. M.</creatorcontrib><creatorcontrib>KIRBY, A. R.</creatorcontrib><creatorcontrib>HINTON, J. C. D.</creatorcontrib><creatorcontrib>MORRIS, V. J.</creatorcontrib><title>Comparative imaging of a bacterial surface‐located GFP fusion protein by epifluorescence and scanning near‐field optical microscopy</title><title>Journal of microscopy (Oxford)</title><addtitle>J Microsc</addtitle><description>Summary
IcsA is an autotransporter protein that plays a role in the virulence of Shigella bacteria. We have examined the cellular localization of a fusion of an IcsA fragment to the green fluorescent protein (GFP) expressed in Escherichia coli using a dual epifluorescence and scanning near‐field optical microscope. By combining the data obtained from far‐field with near‐field microscopy of the same sample, discrimination between surface‐bound fusion proteins and fusion proteins located in the cellular cytoplasm becomes possible. Furthermore, and for the first time, the inherent advantages in resolution of the near‐field images provides highly specific details of the location of a GFP fusion protein on a bacterial cell surface.</description><subject>AFM</subject><subject>Bacterial Proteins - genetics</subject><subject>Bacterial Proteins - metabolism</subject><subject>DNA-Binding Proteins - genetics</subject><subject>DNA-Binding Proteins - metabolism</subject><subject>Escherichia coli</subject><subject>Escherichia coli - genetics</subject><subject>Escherichia coli - metabolism</subject><subject>fluorescence</subject><subject>Green Fluorescent Proteins - genetics</subject><subject>Green Fluorescent Proteins - metabolism</subject><subject>IcsA</subject><subject>Microscopy, Atomic Force</subject><subject>Microscopy, Fluorescence - methods</subject><subject>Microscopy, Scanning Probe - methods</subject><subject>Recombinant Fusion Proteins - genetics</subject><subject>Recombinant Fusion Proteins - metabolism</subject><subject>Shigella</subject><subject>Shigella - genetics</subject><subject>Transcription Factors - genetics</subject><subject>Transcription Factors - metabolism</subject><issn>0022-2720</issn><issn>1365-2818</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkb9u1TAUhy0EoreFV0Ce2BKO7fxxBgZ0RUurojLAbDnOceWrJA52Qns3tq48I0-C03sFY_Fiy_6dz8f-CKEMcpbGu13ORFVmXDKZc4AyB1ZURX7_jGz-HjwnGwDOM15zOCGnMe4AQJYSXpITVkpWQ8U35GHrh0kHPbsfSN2gb914S72lmrbazBic7mlcgtUGf__81XujZ-zoxfkXapfo_Ein4Gd0I233FCdn-8UHjAZHg1SPHY1Gj-PKHFGHRLAO-476aXYmkQdngo_GT_tX5IXVfcTXx_mMfDv_-HX7Kbu-ubjcfrjOjChEkbWm7KxuODOiwarQNXbYWFPZphJVqwW0ZdptCm2L2jApGHQSgXEpOigkQ3FG3h64qe_vC8ZZDS612_d6RL9EVdU159CwJ4McmKxlUaegPATXp8SAVk0hfWTYKwZqtaV2apWiVilqtaUeban7VPrmeMfSDtj9KzzqSYH3h8Cd63H_32B19flyXYk_oJunig</recordid><startdate>200504</startdate><enddate>200504</enddate><creator>GUNNING, A. P.</creator><creator>BONGAERTS, R. J. M.</creator><creator>KIRBY, A. R.</creator><creator>HINTON, J. C. D.</creator><creator>MORRIS, V. J.</creator><general>Blackwell Science Ltd</general><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>7T7</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>200504</creationdate><title>Comparative imaging of a bacterial surface‐located GFP fusion protein by epifluorescence and scanning near‐field optical microscopy</title><author>GUNNING, A. P. ; BONGAERTS, R. J. M. ; KIRBY, A. R. ; HINTON, J. C. D. ; MORRIS, V. J.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3434-bc5dfa921c39e64a7ede9fc6f9636ba30b564a94af47c18310d8e01283d0481e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>AFM</topic><topic>Bacterial Proteins - genetics</topic><topic>Bacterial Proteins - metabolism</topic><topic>DNA-Binding Proteins - genetics</topic><topic>DNA-Binding Proteins - metabolism</topic><topic>Escherichia coli</topic><topic>Escherichia coli - genetics</topic><topic>Escherichia coli - metabolism</topic><topic>fluorescence</topic><topic>Green Fluorescent Proteins - genetics</topic><topic>Green Fluorescent Proteins - metabolism</topic><topic>IcsA</topic><topic>Microscopy, Atomic Force</topic><topic>Microscopy, Fluorescence - methods</topic><topic>Microscopy, Scanning Probe - methods</topic><topic>Recombinant Fusion Proteins - genetics</topic><topic>Recombinant Fusion Proteins - metabolism</topic><topic>Shigella</topic><topic>Shigella - genetics</topic><topic>Transcription Factors - genetics</topic><topic>Transcription Factors - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>GUNNING, A. P.</creatorcontrib><creatorcontrib>BONGAERTS, R. J. M.</creatorcontrib><creatorcontrib>KIRBY, A. R.</creatorcontrib><creatorcontrib>HINTON, J. C. D.</creatorcontrib><creatorcontrib>MORRIS, V. 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J.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Comparative imaging of a bacterial surface‐located GFP fusion protein by epifluorescence and scanning near‐field optical microscopy</atitle><jtitle>Journal of microscopy (Oxford)</jtitle><addtitle>J Microsc</addtitle><date>2005-04</date><risdate>2005</risdate><volume>218</volume><issue>1</issue><spage>46</spage><epage>51</epage><pages>46-51</pages><issn>0022-2720</issn><eissn>1365-2818</eissn><abstract>Summary
IcsA is an autotransporter protein that plays a role in the virulence of Shigella bacteria. We have examined the cellular localization of a fusion of an IcsA fragment to the green fluorescent protein (GFP) expressed in Escherichia coli using a dual epifluorescence and scanning near‐field optical microscope. By combining the data obtained from far‐field with near‐field microscopy of the same sample, discrimination between surface‐bound fusion proteins and fusion proteins located in the cellular cytoplasm becomes possible. Furthermore, and for the first time, the inherent advantages in resolution of the near‐field images provides highly specific details of the location of a GFP fusion protein on a bacterial cell surface.</abstract><cop>Oxford, UK</cop><pub>Blackwell Science Ltd</pub><pmid>15817062</pmid><doi>10.1111/j.1365-2818.2005.01464.x</doi><tpages>6</tpages></addata></record> |
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| subjects | AFM Bacterial Proteins - genetics Bacterial Proteins - metabolism DNA-Binding Proteins - genetics DNA-Binding Proteins - metabolism Escherichia coli Escherichia coli - genetics Escherichia coli - metabolism fluorescence Green Fluorescent Proteins - genetics Green Fluorescent Proteins - metabolism IcsA Microscopy, Atomic Force Microscopy, Fluorescence - methods Microscopy, Scanning Probe - methods Recombinant Fusion Proteins - genetics Recombinant Fusion Proteins - metabolism Shigella Shigella - genetics Transcription Factors - genetics Transcription Factors - metabolism |
| title | Comparative imaging of a bacterial surface‐located GFP fusion protein by epifluorescence and scanning near‐field optical microscopy |
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