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Conference Paper: Phosphoproteomics of candida biofilms

TitlePhosphoproteomics of candida biofilms
Authors
Issue Date2011
PublisherThe International Association for Dental Research.
Citation
The 89th General Session and Exhibition of IADR/AADR/CADR, San Diego, CA., 16-19 March 2011. How to Cite?
AbstractOBJECTIVES: Biofilm formation is a major virulent attribute of Candida species, which is directly related to therapeutic failure. Protein phosphorylation is a key reversible modification that regulates signaling networks. Traditionally protein phosphorylation has been studied by small number of proteins. However, recent advent in phosphoproteomics technologies has opened a new avenue for researchers to identify and quantify the phosphorylation of proteome in global scale. This study aimed to analyze the phosphoproteomics of different species of Candida under biofilm mode of growth. METHODS: Initially, biofilm formation of C. albicans, C. dubliniensis, C. krusei and C. tropicalis were studied for their growth kinetics and antifungal susceptibility. Next, proteins lysate was extracted from 48 h Candida biofilms using optimized extraction method. Proteins were separated by two-dimensional gel electrophoresis and phosphorylated proteins were stained with ProQ-Diamond stain, followed by Typhoon scanning. Next, total proteome maps were obtained with staining quantitative SYPRO Ruby fluorescent die followed by silver staining. Phophoyrylated proteins were identified by tandem mass spectrometry (MS/MS) using denovo sequencing of peptides. Phosphorylation sites were confirmed by spectral analysis. RESULTS: Differential proteomics and phosphor-proteomics maps were obtained for all Candida species, which showed both generic and specific patterns. There were 20, 17, 14, 14 phosphorylated proteins in the C. albicans, C. dubliniensis, C. krusei and C. tropicalis, respectively. Pil1p was heavily phosphorylated indicating its active role in the biofilm mode. CONCLUSION: We unraveled for the first time the phosphoproteomics of Candida biofilms with the generic and specific patterns among different Candida species, which facilitate developing targeted anti-fungal strategies against Candida biofilms (Supported by HKU funding 200907176121 for CJS and 20080717617 for LPS).
DescriptionSession - Candida albicans: abstract no. 1724
Persistent Identifierhttp://hdl.handle.net/10722/133370

 

DC FieldValueLanguage
dc.contributor.authorSeneviratne, CJen_US
dc.contributor.authorWong, SSWen_US
dc.contributor.authorWang, Yen_US
dc.contributor.authorJin, LJen_US
dc.contributor.authorSamaranayake, LPen_US
dc.date.accessioned2011-05-11T08:33:28Z-
dc.date.available2011-05-11T08:33:28Z-
dc.date.issued2011en_US
dc.identifier.citationThe 89th General Session and Exhibition of IADR/AADR/CADR, San Diego, CA., 16-19 March 2011.en_US
dc.identifier.urihttp://hdl.handle.net/10722/133370-
dc.descriptionSession - Candida albicans: abstract no. 1724-
dc.description.abstractOBJECTIVES: Biofilm formation is a major virulent attribute of Candida species, which is directly related to therapeutic failure. Protein phosphorylation is a key reversible modification that regulates signaling networks. Traditionally protein phosphorylation has been studied by small number of proteins. However, recent advent in phosphoproteomics technologies has opened a new avenue for researchers to identify and quantify the phosphorylation of proteome in global scale. This study aimed to analyze the phosphoproteomics of different species of Candida under biofilm mode of growth. METHODS: Initially, biofilm formation of C. albicans, C. dubliniensis, C. krusei and C. tropicalis were studied for their growth kinetics and antifungal susceptibility. Next, proteins lysate was extracted from 48 h Candida biofilms using optimized extraction method. Proteins were separated by two-dimensional gel electrophoresis and phosphorylated proteins were stained with ProQ-Diamond stain, followed by Typhoon scanning. Next, total proteome maps were obtained with staining quantitative SYPRO Ruby fluorescent die followed by silver staining. Phophoyrylated proteins were identified by tandem mass spectrometry (MS/MS) using denovo sequencing of peptides. Phosphorylation sites were confirmed by spectral analysis. RESULTS: Differential proteomics and phosphor-proteomics maps were obtained for all Candida species, which showed both generic and specific patterns. There were 20, 17, 14, 14 phosphorylated proteins in the C. albicans, C. dubliniensis, C. krusei and C. tropicalis, respectively. Pil1p was heavily phosphorylated indicating its active role in the biofilm mode. CONCLUSION: We unraveled for the first time the phosphoproteomics of Candida biofilms with the generic and specific patterns among different Candida species, which facilitate developing targeted anti-fungal strategies against Candida biofilms (Supported by HKU funding 200907176121 for CJS and 20080717617 for LPS).-
dc.languageengen_US
dc.publisherThe International Association for Dental Research.-
dc.relation.ispartofGeneral Session and Exhibition of IADR/AADR/CADR, 2011en_US
dc.titlePhosphoproteomics of candida biofilmsen_US
dc.typeConference_Paperen_US
dc.identifier.emailSeneviratne, CJ: jaya@hku.hken_US
dc.identifier.emailWong, SSW: sarahwong87@gmail.comen_US
dc.identifier.emailWang, Y: yuwanghk@hku.hken_US
dc.identifier.emailJin, LJ: ljjin@hkucc.hku.hken_US
dc.identifier.emailSamaranayake, LP: lakshman@hku.hken_US
dc.identifier.authoritySeneviratne, CJ=rp01372en_US
dc.identifier.authorityWang, Y=rp00239en_US
dc.identifier.authorityJin, LJ=rp00028en_US
dc.identifier.authoritySamaranayake, LP=rp00023en_US
dc.description.naturelink_to_OA_fulltext-
dc.identifier.hkuros185051en_US
dc.publisher.placeUnited States-
dc.description.otherThe 89th General Session and Exhibition of IADR/AADR/CADR, San Diego, CA., 16-19 March 2011.-

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