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Article: HIV protease inhibitors differentially inhibit adhesion of Candida albicans to acrylic surfaces

TitleHIV protease inhibitors differentially inhibit adhesion of Candida albicans to acrylic surfaces
Authors
KeywordsAcrylic
Adhesion
Candida Spp.
HIV
Protease Inhibitors
Secreted Aspartyl Proteinases
Issue Date2010
PublisherWiley-Blackwell Verlag GmbH. The Journal's web site is located at http://www.blackwellpublishing.com/journals/MYC
Citation
Mycoses, 2010, v. 53 n. 6, p. 488-494 How to Cite?
AbstractHighly active antiretroviral therapy (HAART), using HIV protease inhibitors, is commonly used in the management of HIV infection. HIV protease inhibitors also have a direct effect on a key virulence factor of Candida albicans, its secreted aspartyl proteinase (Sap). Although protease inhibitors can attenuate Candida adhesion to human epithelial cells, their effects on adhesion to acrylic substances, which is a common component of oral appliances, is unknown. This study investigated whether protease inhibitors affect C. albicans adhesion to acrylic substances. C. albicans suspensions were pretreated with different concentrations of saquinavir, ritonavir or indinavir for 1 h and allowed to adhere on acrylic strips, which had been pretreated with pooled human saliva for 30 min, for another hour in the presence of each drug. The test groups showed a significantly lower degree of adhesion than the controls. Adhesion was reduced by 50% at drug concentrations of 100, 100 and 20 μmol l-1 for saquinavir, ritonavir and indinavir respectively. In conclusion, protease inhibitors attenuated C. albicans adhesion to an acrylic surface in vitro in a dose-dependent manner, and different protease inhibitors exhibited different degrees of inhibition. © 2009 Blackwell Verlag GmbH.
Persistent Identifierhttp://hdl.handle.net/10722/134975
ISSN
2015 Impact Factor: 2.332
2015 SCImago Journal Rankings: 0.921
ISI Accession Number ID
Funding AgencyGrant Number
University of Hong Kong, Hong Kong200607176077
Funding Information:

This research was supported by the Committee for Research and Conference Grant (project code: 200607176077) of the University of Hong Kong, Hong Kong. The authors express their appreciation to Merck (Rahway, NJ, USA) for supplying indinavir and to Dr Trevor Lane for editorial assistance. No conflict of interest exists for any of the authors.

References

 

DC FieldValueLanguage
dc.contributor.authorTsang, CSPen_HK
dc.contributor.authorHong, Ien_HK
dc.date.accessioned2011-07-27T01:25:15Z-
dc.date.available2011-07-27T01:25:15Z-
dc.date.issued2010en_HK
dc.identifier.citationMycoses, 2010, v. 53 n. 6, p. 488-494en_HK
dc.identifier.issn0933-7407en_HK
dc.identifier.urihttp://hdl.handle.net/10722/134975-
dc.description.abstractHighly active antiretroviral therapy (HAART), using HIV protease inhibitors, is commonly used in the management of HIV infection. HIV protease inhibitors also have a direct effect on a key virulence factor of Candida albicans, its secreted aspartyl proteinase (Sap). Although protease inhibitors can attenuate Candida adhesion to human epithelial cells, their effects on adhesion to acrylic substances, which is a common component of oral appliances, is unknown. This study investigated whether protease inhibitors affect C. albicans adhesion to acrylic substances. C. albicans suspensions were pretreated with different concentrations of saquinavir, ritonavir or indinavir for 1 h and allowed to adhere on acrylic strips, which had been pretreated with pooled human saliva for 30 min, for another hour in the presence of each drug. The test groups showed a significantly lower degree of adhesion than the controls. Adhesion was reduced by 50% at drug concentrations of 100, 100 and 20 μmol l-1 for saquinavir, ritonavir and indinavir respectively. In conclusion, protease inhibitors attenuated C. albicans adhesion to an acrylic surface in vitro in a dose-dependent manner, and different protease inhibitors exhibited different degrees of inhibition. © 2009 Blackwell Verlag GmbH.en_HK
dc.languageengen_US
dc.publisherWiley-Blackwell Verlag GmbH. The Journal's web site is located at http://www.blackwellpublishing.com/journals/MYCen_HK
dc.relation.ispartofMycosesen_HK
dc.rightsThe definitive version is available at www3.interscience.wiley.com-
dc.subjectAcrylicen_HK
dc.subjectAdhesionen_HK
dc.subjectCandida Spp.en_HK
dc.subjectHIVen_HK
dc.subjectProtease Inhibitorsen_HK
dc.subjectSecreted Aspartyl Proteinasesen_HK
dc.subject.meshAcrylates-
dc.subject.meshAntifungal Agents - pharmacology-
dc.subject.meshCandida albicans - drug effects - physiology-
dc.subject.meshCell Adhesion - drug effects-
dc.subject.meshHIV Protease Inhibitors - pharmacology-
dc.titleHIV protease inhibitors differentially inhibit adhesion of Candida albicans to acrylic surfacesen_HK
dc.typeArticleen_HK
dc.identifier.emailTsang, CSP:csptsang@hkucc.hku.hken_HK
dc.identifier.authorityTsang, CSP=rp00026en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1111/j.1439-0507.2009.01743.xen_HK
dc.identifier.pmid19538521-
dc.identifier.scopuseid_2-s2.0-77958101558en_HK
dc.identifier.hkuros186659en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-77958101558&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume53en_HK
dc.identifier.issue6en_HK
dc.identifier.spage488en_HK
dc.identifier.epage494en_HK
dc.identifier.eissn1439-0507-
dc.identifier.isiWOS:000282568800005-
dc.publisher.placeGermanyen_HK
dc.identifier.scopusauthoridTsang, CSP=7202936002en_HK
dc.identifier.scopusauthoridHong, I=37034048200en_HK
dc.identifier.citeulike8017547-

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