Killing of Candida albicans by lactoferricin B, a potent antimicrobial peptide derived from the N-terminal region of bovine lactoferrin
Candida albicans was found to be highly susceptible to inhibition and inactivation by lactoferricin B, a peptide produced by enzymatic cleavage of bovine lactoferrin. Effective concentrations of the peptide varied within the range of 18 to 150 micrograms/ml depending on the strain and the culture me...
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| Veröffentlicht in: | Medical microbiology and immunology 1993-05, Vol.182 (2), p.97-105 |
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| container_title | Medical microbiology and immunology |
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| creator | BELLAMY, W WAKABAYASHI, H TAKASE, M KAWASE, K SHIMAMURA, S TOMITA, M |
| description | Candida albicans was found to be highly susceptible to inhibition and inactivation by lactoferricin B, a peptide produced by enzymatic cleavage of bovine lactoferrin. Effective concentrations of the peptide varied within the range of 18 to 150 micrograms/ml depending on the strain and the culture medium used. Its effect was lethal, causing a rapid loss of colony-forming capability. 14C-labeled lactoferricin B bound to C. albicans and the rate of binding appeared to be consistent with the rate of killing induced by the peptide. The extent of binding was diminished in the presence of Mg2+ or Ca2+ ions which acted to reduce its anticandidal effectiveness. Binding occurred optimally at pH 6.0 and killing was maximal near the same pH. Such evidence suggests the lethal effect of lactoferricin B results from its direct interaction with the cell surface. Cells exposed to lactoferricin B exhibited profound ultrastructural damage which appeared to reflect its induction of an autolytic response. These findings suggest that active peptides of lactoferrin could potentially contribute to the host defense against C. albicans. |
| doi_str_mv | 10.1007/bf00189377 |
| format | Article |
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Effective concentrations of the peptide varied within the range of 18 to 150 micrograms/ml depending on the strain and the culture medium used. Its effect was lethal, causing a rapid loss of colony-forming capability. 14C-labeled lactoferricin B bound to C. albicans and the rate of binding appeared to be consistent with the rate of killing induced by the peptide. The extent of binding was diminished in the presence of Mg2+ or Ca2+ ions which acted to reduce its anticandidal effectiveness. Binding occurred optimally at pH 6.0 and killing was maximal near the same pH. Such evidence suggests the lethal effect of lactoferricin B results from its direct interaction with the cell surface. Cells exposed to lactoferricin B exhibited profound ultrastructural damage which appeared to reflect its induction of an autolytic response. These findings suggest that active peptides of lactoferrin could potentially contribute to the host defense against C. albicans.</description><identifier>ISSN: 0300-8584</identifier><identifier>EISSN: 1432-1831</identifier><identifier>DOI: 10.1007/bf00189377</identifier><identifier>PMID: 8332105</identifier><identifier>CODEN: MMIYAO</identifier><language>eng</language><publisher>Berlin: Springer</publisher><subject>Action of physical and chemical agents ; Amino Acid Sequence ; Antifungal Agents - metabolism ; Antifungal Agents - pharmacology ; Biological and medical sciences ; Calcium Chloride - pharmacology ; Candida albicans - drug effects ; Candida albicans - metabolism ; Candida albicans - ultrastructure ; Fundamental and applied biological sciences. Psychology ; Fungal Proteins - metabolism ; Fungal Proteins - pharmacology ; Hydrogen-Ion Concentration ; Lactoferrin - chemistry ; Lactoferrin - pharmacology ; Magnesium Chloride - pharmacology ; Microbial Sensitivity Tests ; Microbiological Techniques ; Microbiology ; Molecular Sequence Data ; Mycology ; Peptides - chemistry ; Peptides - pharmacology</subject><ispartof>Medical microbiology and immunology, 1993-05, Vol.182 (2), p.97-105</ispartof><rights>1993 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c377t-3ffd0ad365603d2510400a5a703d7b4165d3ce2ea9a989660f0c4196c38356eb3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4823041$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8332105$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>BELLAMY, W</creatorcontrib><creatorcontrib>WAKABAYASHI, H</creatorcontrib><creatorcontrib>TAKASE, M</creatorcontrib><creatorcontrib>KAWASE, K</creatorcontrib><creatorcontrib>SHIMAMURA, S</creatorcontrib><creatorcontrib>TOMITA, M</creatorcontrib><title>Killing of Candida albicans by lactoferricin B, a potent antimicrobial peptide derived from the N-terminal region of bovine lactoferrin</title><title>Medical microbiology and immunology</title><addtitle>Med Microbiol Immunol</addtitle><description>Candida albicans was found to be highly susceptible to inhibition and inactivation by lactoferricin B, a peptide produced by enzymatic cleavage of bovine lactoferrin. Effective concentrations of the peptide varied within the range of 18 to 150 micrograms/ml depending on the strain and the culture medium used. Its effect was lethal, causing a rapid loss of colony-forming capability. 14C-labeled lactoferricin B bound to C. albicans and the rate of binding appeared to be consistent with the rate of killing induced by the peptide. The extent of binding was diminished in the presence of Mg2+ or Ca2+ ions which acted to reduce its anticandidal effectiveness. Binding occurred optimally at pH 6.0 and killing was maximal near the same pH. Such evidence suggests the lethal effect of lactoferricin B results from its direct interaction with the cell surface. Cells exposed to lactoferricin B exhibited profound ultrastructural damage which appeared to reflect its induction of an autolytic response. These findings suggest that active peptides of lactoferrin could potentially contribute to the host defense against C. albicans.</description><subject>Action of physical and chemical agents</subject><subject>Amino Acid Sequence</subject><subject>Antifungal Agents - metabolism</subject><subject>Antifungal Agents - pharmacology</subject><subject>Biological and medical sciences</subject><subject>Calcium Chloride - pharmacology</subject><subject>Candida albicans - drug effects</subject><subject>Candida albicans - metabolism</subject><subject>Candida albicans - ultrastructure</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Fungal Proteins - metabolism</subject><subject>Fungal Proteins - pharmacology</subject><subject>Hydrogen-Ion Concentration</subject><subject>Lactoferrin - chemistry</subject><subject>Lactoferrin - pharmacology</subject><subject>Magnesium Chloride - pharmacology</subject><subject>Microbial Sensitivity Tests</subject><subject>Microbiological Techniques</subject><subject>Microbiology</subject><subject>Molecular Sequence Data</subject><subject>Mycology</subject><subject>Peptides - chemistry</subject><subject>Peptides - pharmacology</subject><issn>0300-8584</issn><issn>1432-1831</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1993</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpNkEFv1TAQhC0EKq-FC3ckHxCHisA6jhPnSJ8oICq4wDna2Oti5NjB9qvUX8DfJlUfFafVaD7NaoaxFwLeCoDh3ewAhB7lMDxiO9HJthFaisdsBxKg0Up3T9lpKb82auhbOGEnWspWgNqxP198CD5e8-T4HqP1FjmG2RuMhc-3PKCpyVHO3vjIL95w5GuqFCvHWP3iTU6zx8BXWqu3xC1lf0OWu5wWXn8S_9pUyouPG5Pp2qd492lONz7Sf-HxGXviMBR6frxn7Mflh-_7T83Vt4-f9--vGrO1q410zgJa2asepG2VgA4AFQ6bGuZO9MpKQy3hiKMe-x4cmE6MvZFaqp5mecZe3-euOf0-UKnT4ouhEDBSOpRpUFr1oxAbeH4Pbg1LyeSmNfsF8-0kYLpbfbq4_Lf6Br88ph7mhewDepx5818dfSwGg8sYjS8PWKdbCZ2QfwEJ-Yn_</recordid><startdate>19930501</startdate><enddate>19930501</enddate><creator>BELLAMY, W</creator><creator>WAKABAYASHI, H</creator><creator>TAKASE, M</creator><creator>KAWASE, K</creator><creator>SHIMAMURA, S</creator><creator>TOMITA, M</creator><general>Springer</general><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>7X8</scope></search><sort><creationdate>19930501</creationdate><title>Killing of Candida albicans by lactoferricin B, a potent antimicrobial peptide derived from the N-terminal region of bovine lactoferrin</title><author>BELLAMY, W ; WAKABAYASHI, H ; TAKASE, M ; KAWASE, K ; SHIMAMURA, S ; TOMITA, M</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c377t-3ffd0ad365603d2510400a5a703d7b4165d3ce2ea9a989660f0c4196c38356eb3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1993</creationdate><topic>Action of physical and chemical agents</topic><topic>Amino Acid Sequence</topic><topic>Antifungal Agents - metabolism</topic><topic>Antifungal Agents - pharmacology</topic><topic>Biological and medical sciences</topic><topic>Calcium Chloride - pharmacology</topic><topic>Candida albicans - drug effects</topic><topic>Candida albicans - metabolism</topic><topic>Candida albicans - ultrastructure</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Fungal Proteins - metabolism</topic><topic>Fungal Proteins - pharmacology</topic><topic>Hydrogen-Ion Concentration</topic><topic>Lactoferrin - chemistry</topic><topic>Lactoferrin - pharmacology</topic><topic>Magnesium Chloride - pharmacology</topic><topic>Microbial Sensitivity Tests</topic><topic>Microbiological Techniques</topic><topic>Microbiology</topic><topic>Molecular Sequence Data</topic><topic>Mycology</topic><topic>Peptides - chemistry</topic><topic>Peptides - pharmacology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>BELLAMY, W</creatorcontrib><creatorcontrib>WAKABAYASHI, H</creatorcontrib><creatorcontrib>TAKASE, M</creatorcontrib><creatorcontrib>KAWASE, K</creatorcontrib><creatorcontrib>SHIMAMURA, S</creatorcontrib><creatorcontrib>TOMITA, M</creatorcontrib><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>MEDLINE - Academic</collection><jtitle>Medical microbiology and immunology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>BELLAMY, W</au><au>WAKABAYASHI, H</au><au>TAKASE, M</au><au>KAWASE, K</au><au>SHIMAMURA, S</au><au>TOMITA, M</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Killing of Candida albicans by lactoferricin B, a potent antimicrobial peptide derived from the N-terminal region of bovine lactoferrin</atitle><jtitle>Medical microbiology and immunology</jtitle><addtitle>Med Microbiol Immunol</addtitle><date>1993-05-01</date><risdate>1993</risdate><volume>182</volume><issue>2</issue><spage>97</spage><epage>105</epage><pages>97-105</pages><issn>0300-8584</issn><eissn>1432-1831</eissn><coden>MMIYAO</coden><abstract>Candida albicans was found to be highly susceptible to inhibition and inactivation by lactoferricin B, a peptide produced by enzymatic cleavage of bovine lactoferrin. Effective concentrations of the peptide varied within the range of 18 to 150 micrograms/ml depending on the strain and the culture medium used. Its effect was lethal, causing a rapid loss of colony-forming capability. 14C-labeled lactoferricin B bound to C. albicans and the rate of binding appeared to be consistent with the rate of killing induced by the peptide. The extent of binding was diminished in the presence of Mg2+ or Ca2+ ions which acted to reduce its anticandidal effectiveness. Binding occurred optimally at pH 6.0 and killing was maximal near the same pH. Such evidence suggests the lethal effect of lactoferricin B results from its direct interaction with the cell surface. Cells exposed to lactoferricin B exhibited profound ultrastructural damage which appeared to reflect its induction of an autolytic response. These findings suggest that active peptides of lactoferrin could potentially contribute to the host defense against C. albicans.</abstract><cop>Berlin</cop><pub>Springer</pub><pmid>8332105</pmid><doi>10.1007/bf00189377</doi><tpages>9</tpages></addata></record> |
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| subjects | Action of physical and chemical agents Amino Acid Sequence Antifungal Agents - metabolism Antifungal Agents - pharmacology Biological and medical sciences Calcium Chloride - pharmacology Candida albicans - drug effects Candida albicans - metabolism Candida albicans - ultrastructure Fundamental and applied biological sciences. Psychology Fungal Proteins - metabolism Fungal Proteins - pharmacology Hydrogen-Ion Concentration Lactoferrin - chemistry Lactoferrin - pharmacology Magnesium Chloride - pharmacology Microbial Sensitivity Tests Microbiological Techniques Microbiology Molecular Sequence Data Mycology Peptides - chemistry Peptides - pharmacology |
| title | Killing of Candida albicans by lactoferricin B, a potent antimicrobial peptide derived from the N-terminal region of bovine lactoferrin |
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