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Article: The relationship between the acid and alkaline phosphatase activity and the adherence of clinical isolates of Candida parapsilosis to human buccal epithelial cells

TitleThe relationship between the acid and alkaline phosphatase activity and the adherence of clinical isolates of Candida parapsilosis to human buccal epithelial cells
Authors
KeywordsAcid phosphatase
Adherence
Alkaline phosphatase
Buccal epithelial cells
Candida parapsilosis
Issue Date1999
PublisherWiley-Blackwell Publishing, Inc. The Journal's web site is located at http://www.blackwellpublishing.com/journals/APMIS
Citation
Apmis, 1999, v. 107 n. 11, p. 1034-1042 How to Cite?
AbstractCandida parapsilosis is an emerging fungal pathogen implicated in many diseases, especially in compromised hosts. Candidal colonization and infection depends on the initial ability to adhere to host surfaces, which in turn depends upon the cell wall components and the allied structures of both the host and the fungus. Examination of a miscellaneous collection of 24 C parapsilosis isolates, from both superficial and deep infections, for their potential pathogenic traits displayed a relationship between the phosphatase activity measured with p-nitrophenol phosphate and adhesion of the yeasts to human buccal epithelial cells (BECs). Significant intraspecies differences were seen in both the alkaline and acid phosphatase activity as well as in their adhesion to BECs (p<0.0001). The acid phosphatase activity of the superficial isolates was significantly greater (152%) than that of the systemic isolates (p=0.0352). A highly significant positive correlation was also established between the yeast adhesion to BECs and both the acid (r=0.88, p<0.0001) and alkaline (r=0.9, p<0.0001) phosphatase activity. These relationships, described here for the first time, imply that phosphatases of Candida species may play a crucial role in potentiating their virulence.
Persistent Identifierhttp://hdl.handle.net/10722/66470
ISSN
2023 Impact Factor: 2.2
2023 SCImago Journal Rankings: 0.687
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorFernanado, PHPen_HK
dc.contributor.authorPanagoda, GJen_HK
dc.contributor.authorSamaranayake, LPen_HK
dc.date.accessioned2010-09-06T05:46:38Z-
dc.date.available2010-09-06T05:46:38Z-
dc.date.issued1999en_HK
dc.identifier.citationApmis, 1999, v. 107 n. 11, p. 1034-1042en_HK
dc.identifier.issn0903-4641en_HK
dc.identifier.urihttp://hdl.handle.net/10722/66470-
dc.description.abstractCandida parapsilosis is an emerging fungal pathogen implicated in many diseases, especially in compromised hosts. Candidal colonization and infection depends on the initial ability to adhere to host surfaces, which in turn depends upon the cell wall components and the allied structures of both the host and the fungus. Examination of a miscellaneous collection of 24 C parapsilosis isolates, from both superficial and deep infections, for their potential pathogenic traits displayed a relationship between the phosphatase activity measured with p-nitrophenol phosphate and adhesion of the yeasts to human buccal epithelial cells (BECs). Significant intraspecies differences were seen in both the alkaline and acid phosphatase activity as well as in their adhesion to BECs (p<0.0001). The acid phosphatase activity of the superficial isolates was significantly greater (152%) than that of the systemic isolates (p=0.0352). A highly significant positive correlation was also established between the yeast adhesion to BECs and both the acid (r=0.88, p<0.0001) and alkaline (r=0.9, p<0.0001) phosphatase activity. These relationships, described here for the first time, imply that phosphatases of Candida species may play a crucial role in potentiating their virulence.en_HK
dc.languageengen_HK
dc.publisherWiley-Blackwell Publishing, Inc. The Journal's web site is located at http://www.blackwellpublishing.com/journals/APMISen_HK
dc.relation.ispartofAPMISen_HK
dc.subjectAcid phosphatase-
dc.subjectAdherence-
dc.subjectAlkaline phosphatase-
dc.subjectBuccal epithelial cells-
dc.subjectCandida parapsilosis-
dc.subject.meshAcid Phosphatase - metabolismen_HK
dc.subject.meshAlkaline Phosphatase - metabolismen_HK
dc.subject.meshCandida - enzymology - isolation & purification - pathogenicityen_HK
dc.subject.meshCandidiasis - microbiologyen_HK
dc.subject.meshCell Adhesionen_HK
dc.subject.meshCheek - microbiologyen_HK
dc.subject.meshEpithelial Cells - microbiologyen_HK
dc.subject.meshHumansen_HK
dc.subject.meshMaleen_HK
dc.subject.meshMouth Mucosa - microbiologyen_HK
dc.subject.meshVirulenceen_HK
dc.titleThe relationship between the acid and alkaline phosphatase activity and the adherence of clinical isolates of Candida parapsilosis to human buccal epithelial cellsen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0903-4641&volume=107&spage=1034&epage=42&date=1999&atitle=The+relationship+between+the+acid+and+alkaline+phosphatase+activity+and+the+adherence+of+clinical+isolates+of+Candida+parapsilosis+to+human+buccal+epithelial+cellsen_HK
dc.identifier.emailSamaranayake, LP:lakshman@hku.hken_HK
dc.identifier.authoritySamaranayake, LP=rp00023en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1111/j.1699-0463.1999.tb01507.x-
dc.identifier.pmid10598876-
dc.identifier.scopuseid_2-s2.0-0032711653en_HK
dc.identifier.hkuros47501en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0032711653&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume107en_HK
dc.identifier.issue11en_HK
dc.identifier.spage1034en_HK
dc.identifier.epage1042en_HK
dc.identifier.isiWOS:000084053000009-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridFernanado, PHP=6504508052en_HK
dc.identifier.scopusauthoridPanagoda, GJ=6507149433en_HK
dc.identifier.scopusauthoridSamaranayake, LP=7102761002en_HK
dc.identifier.issnl0903-4641-

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