Escherichia coli hemolysin permeabilizes small unilamellar vesicles loaded with calcein by a single-hit mechanism
Escherichia coli hemolysin produces small unilamellar lipid vesicles permeable to the fluorescent dye calcein by forming pores through their membrane. The process of permeabilization proceeds as a pseudo first-order reaction, indicating that the toxin is active as a monomer; consistently no evidence...
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| Veröffentlicht in: | FEBS letters 1988-05, Vol.232 (1), p.217-220 |
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| creator | Menestrina, Gianfranco |
| description | Escherichia coli hemolysin produces small unilamellar lipid vesicles permeable to the fluorescent dye calcein by forming pores through their membrane. The process of permeabilization proceeds as a pseudo first-order reaction, indicating that the toxin is active as a monomer; consistently no evidence for cooperativity has been found in a dose-response titration. The rate of interaction increases on lowering the pH of the solution and by introducing negatively charged lipids into the vesicles. The overall pore formation mechanism resembles that of other toxins of bacterial origin such as colicins, diphtheria, tetanus and botulinum toxin. |
| doi_str_mv | 10.1016/0014-5793(88)80420-4 |
| format | Article |
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The overall pore formation mechanism resembles that of other toxins of bacterial origin such as colicins, diphtheria, tetanus and botulinum toxin.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/0014-5793(88)80420-4</identifier><identifier>PMID: 3284764</identifier><identifier>CODEN: FEBLAL</identifier><language>eng</language><publisher>Amsterdam: Elsevier B.V</publisher><subject>Artificial membranes and reconstituted systems ; Biological and medical sciences ; Electrochemistry ; Escherichia coli ; Escherichia coli - analysis ; Fluoresceins ; Fluorescent Dyes ; Fundamental and applied biological sciences. Psychology ; Hemolysin ; Hemolysin Proteins - pharmacology ; Hydrogen-Ion Concentration ; Kinetics ; Lipid vesicle ; Liposomes - metabolism ; Membrane physicochemistry ; Molecular biophysics ; Permeability ; pH dependence ; Phosphatidylinositols ; Phosphatidylserines ; Pore formation ; Single-hit mechanism ; Surface potential ; Surface Properties</subject><ispartof>FEBS letters, 1988-05, Vol.232 (1), p.217-220</ispartof><rights>1988</rights><rights>FEBS Letters 232 (1988) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><rights>1989 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5264-fe4b11ba755b6adf503cfbb82f29f675927dc644902b44f04850db18695bf0253</citedby><cites>FETCH-LOGICAL-c5264-fe4b11ba755b6adf503cfbb82f29f675927dc644902b44f04850db18695bf0253</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/0014579388804204$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65534</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=7101279$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/3284764$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Menestrina, Gianfranco</creatorcontrib><title>Escherichia coli hemolysin permeabilizes small unilamellar vesicles loaded with calcein by a single-hit mechanism</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>Escherichia coli hemolysin produces small unilamellar lipid vesicles permeable to the fluorescent dye calcein by forming pores through their membrane. The process of permeabilization proceeds as a pseudo first-order reaction, indicating that the toxin is active as a monomer; consistently no evidence for cooperativity has been found in a dose-response titration. The rate of interaction increases on lowering the pH of the solution and by introducing negatively charged lipids into the vesicles. The overall pore formation mechanism resembles that of other toxins of bacterial origin such as colicins, diphtheria, tetanus and botulinum toxin.</description><subject>Artificial membranes and reconstituted systems</subject><subject>Biological and medical sciences</subject><subject>Electrochemistry</subject><subject>Escherichia coli</subject><subject>Escherichia coli - analysis</subject><subject>Fluoresceins</subject><subject>Fluorescent Dyes</subject><subject>Fundamental and applied biological sciences. 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Psychology</topic><topic>Hemolysin</topic><topic>Hemolysin Proteins - pharmacology</topic><topic>Hydrogen-Ion Concentration</topic><topic>Kinetics</topic><topic>Lipid vesicle</topic><topic>Liposomes - metabolism</topic><topic>Membrane physicochemistry</topic><topic>Molecular biophysics</topic><topic>Permeability</topic><topic>pH dependence</topic><topic>Phosphatidylinositols</topic><topic>Phosphatidylserines</topic><topic>Pore formation</topic><topic>Single-hit mechanism</topic><topic>Surface potential</topic><topic>Surface Properties</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Menestrina, Gianfranco</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</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>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Menestrina, Gianfranco</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Escherichia coli hemolysin permeabilizes small unilamellar vesicles loaded with calcein by a single-hit mechanism</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>1988-05-09</date><risdate>1988</risdate><volume>232</volume><issue>1</issue><spage>217</spage><epage>220</epage><pages>217-220</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><coden>FEBLAL</coden><abstract>Escherichia coli hemolysin produces small unilamellar lipid vesicles permeable to the fluorescent dye calcein by forming pores through their membrane. 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| ispartof | FEBS letters, 1988-05, Vol.232 (1), p.217-220 |
| issn | 0014-5793 1873-3468 |
| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Artificial membranes and reconstituted systems Biological and medical sciences Electrochemistry Escherichia coli Escherichia coli - analysis Fluoresceins Fluorescent Dyes Fundamental and applied biological sciences. Psychology Hemolysin Hemolysin Proteins - pharmacology Hydrogen-Ion Concentration Kinetics Lipid vesicle Liposomes - metabolism Membrane physicochemistry Molecular biophysics Permeability pH dependence Phosphatidylinositols Phosphatidylserines Pore formation Single-hit mechanism Surface potential Surface Properties |
| title | Escherichia coli hemolysin permeabilizes small unilamellar vesicles loaded with calcein by a single-hit mechanism |
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