File Download
  Links for fulltext
     (May Require Subscription)
Supplementary

Article: Inhibition of growth and secreted aspartyl proteinase production in Candida albicans by lysozyme

TitleInhibition of growth and secreted aspartyl proteinase production in Candida albicans by lysozyme
Authors
Issue Date1999
PublisherSociety for General Microbiology. The Journal's web site is located at http://jmm.sgmjournals.org
Citation
Journal Of Medical Microbiology, 1999, v. 48 n. 8, p. 721-730 How to Cite?
AbstractLysozyme (muramidase) is a non-specific, antimicrobial protein ubiquitous in human mucosal secretions such as saliva. Although its antibacterial and antifungal activities are well recognised, there are no data on the specific concentrations necessary to affect the growth of Candida albicans or about the effect of lysozyme on the production of secreted aspartyl proteinase (Sap), a putative virulence factor of C. albicans. Five Sap-producing isolates of C. albicans were cultured in YCB-BSA medium with various concentrations of lysozyme to examine its effect on yeast cell growth, ultrastructural cellular topography and extracellular and intracellular Sap concentration and activity. Lysozyme was candidacidal at high concentrations and decreased significantly the extracellular Sap concentration at sublethal doses, accompanied by intracellular accumulation of the enzyme. At low concentrations of lysozyme (c. 10 μg/ml). Sap activity decreased more than two-fold and Sap concentration decreased five-fold without any appreciable effect on cell growth or viability. Ultrastructural investigations showed ballooned cells and cells with invaginations (expecially present near bud scars), indicating that cell-wall components may be possible targets for this enzyme. All concentrations of lysozyme tested were well within physiologically attainable levels. These data suggest that lysozyme has, at least, a bimodal action on C. albicans, killing the organism at higher concentrations and modulating Sap metabolism at lower concentrations.
Persistent Identifierhttp://hdl.handle.net/10722/55439
ISSN
2015 Impact Factor: 2.269
2015 SCImago Journal Rankings: 1.060
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorWu, Ten_HK
dc.contributor.authorSamaranayake, LPen_HK
dc.contributor.authorLeung, WKen_HK
dc.contributor.authorSullivan, PAen_HK
dc.date.accessioned2009-08-06T03:37:08Z-
dc.date.available2009-08-06T03:37:08Z-
dc.date.issued1999en_HK
dc.identifier.citationJournal Of Medical Microbiology, 1999, v. 48 n. 8, p. 721-730en_HK
dc.identifier.issn0022-2615en_HK
dc.identifier.urihttp://hdl.handle.net/10722/55439-
dc.description.abstractLysozyme (muramidase) is a non-specific, antimicrobial protein ubiquitous in human mucosal secretions such as saliva. Although its antibacterial and antifungal activities are well recognised, there are no data on the specific concentrations necessary to affect the growth of Candida albicans or about the effect of lysozyme on the production of secreted aspartyl proteinase (Sap), a putative virulence factor of C. albicans. Five Sap-producing isolates of C. albicans were cultured in YCB-BSA medium with various concentrations of lysozyme to examine its effect on yeast cell growth, ultrastructural cellular topography and extracellular and intracellular Sap concentration and activity. Lysozyme was candidacidal at high concentrations and decreased significantly the extracellular Sap concentration at sublethal doses, accompanied by intracellular accumulation of the enzyme. At low concentrations of lysozyme (c. 10 μg/ml). Sap activity decreased more than two-fold and Sap concentration decreased five-fold without any appreciable effect on cell growth or viability. Ultrastructural investigations showed ballooned cells and cells with invaginations (expecially present near bud scars), indicating that cell-wall components may be possible targets for this enzyme. All concentrations of lysozyme tested were well within physiologically attainable levels. These data suggest that lysozyme has, at least, a bimodal action on C. albicans, killing the organism at higher concentrations and modulating Sap metabolism at lower concentrations.en_HK
dc.languageengen_HK
dc.publisherSociety for General Microbiology. The Journal's web site is located at http://jmm.sgmjournals.orgen_HK
dc.relation.ispartofJournal of Medical Microbiologyen_HK
dc.rightsThis is an author manuscript that has been accepted for publication in Journal of Medical Microbiology, copyright Society for General Microbiology, but has not been copy-edited, formatted or proofed. Cite this article as appearing in Journal of Medical Microbiology. This version of the manuscript may not be duplicated or reproduced, other than for personal use or within the rule of 'Fair Use of Copyrighted Materials' (section 17, Title 17, US Code), without permission from the copyright owner, Society for General Microbiology. The Society for General Microbiology disclaims any responsibility or liability for errors or omissions in this version of the manuscript or in any version derived from it by any other parties. The final copy-edited, published article, which is the version of record, can be found at http://jmm.sgmjournals.org, and is freely available without a subscription.en_HK
dc.rightsThis work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.-
dc.subject.meshAspartic Endopeptidases - antagonists & inhibitors - metabolism - secretionen_HK
dc.subject.meshCandida albicans - cytology - enzymology - ultrastructureen_HK
dc.subject.meshMuramidase - metabolism - pharmacologyen_HK
dc.subject.meshAnti-Infective Agents - pharmacologyen_HK
dc.subject.meshExtracellular Space - drug effects - enzymologyen_HK
dc.titleInhibition of growth and secreted aspartyl proteinase production in Candida albicans by lysozymeen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0022-2615&volume=48&issue=8&spage=721&epage=730&date=1999&atitle=Inhibition+of+growth+and+secreted+aspartyl+proteinase+production+in+Candida+albicans+by+lysozymeen_HK
dc.identifier.emailSamaranayake, LP:lakshman@hku.hken_HK
dc.identifier.emailLeung, WK:ewkleung@hkucc.hku.hken_HK
dc.identifier.authoritySamaranayake, LP=rp00023en_HK
dc.identifier.authorityLeung, WK=rp00019en_HK
dc.description.naturepublished_or_final_versionen_HK
dc.identifier.doi10.1099/00222615-48-8-721-
dc.identifier.pmid10450995-
dc.identifier.scopuseid_2-s2.0-0032878759en_HK
dc.identifier.hkuros41782-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0032878759&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume48en_HK
dc.identifier.issue8en_HK
dc.identifier.spage721en_HK
dc.identifier.epage730en_HK
dc.identifier.isiWOS:000081722100003-
dc.publisher.placeUnited Kingdomen_HK
dc.identifier.scopusauthoridWu, T=9237315300en_HK
dc.identifier.scopusauthoridSamaranayake, LP=7102761002en_HK
dc.identifier.scopusauthoridLeung, WK=25224691800en_HK
dc.identifier.scopusauthoridSullivan, PA=7402033666en_HK

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats