Bader, Oliver

[["dc.bibliographiccitation.journal","Mycoses"],["dc.bibliographiccitation.volume","55"],["dc.contributor.author","Bader, Oliver"],["dc.contributor.author","Schwarz, A."],["dc.contributor.author","Kraneveld, Eefje A."],["dc.contributor.author","Tangwattanachuleeporn, Marut"],["dc.contributor.author","Schmidt, P."],["dc.contributor.author","Jacobsen, Mette D."],["dc.contributor.author","Gross, U."],["dc.contributor.author","de Groot, Piet W. J."],["dc.contributor.author","Weig, Michael S."],["dc.date.accessioned","2018-11-07T09:09:43Z"],["dc.date.available","2018-11-07T09:09:43Z"],["dc.date.issued","2012"],["dc.format.extent","143"],["dc.identifier.isi","000305069800445"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/26326"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.publisher.place","Hoboken"],["dc.relation.issn","0933-7407"],["dc.title","Karyotypic and phenotypic plasticity of the Candida glabrata strain CBS138/ATCC2001"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Mycoses"],["dc.bibliographiccitation.volume","55"],["dc.contributor.author","de Boer, Albert D."],["dc.contributor.author","Kraneveld, Eefje A."],["dc.contributor.author","Gomez Molero, E."],["dc.contributor.author","Bader, Oliver"],["dc.contributor.author","Sanchez Virosta, P."],["dc.contributor.author","Weig, Michael S."],["dc.contributor.author","de Groot, Piet W. J."],["dc.date.accessioned","2018-11-07T09:09:42Z"],["dc.date.available","2018-11-07T09:09:42Z"],["dc.date.issued","2012"],["dc.format.extent","26"],["dc.identifier.isi","000305069800087"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/26318"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.publisher.place","Hoboken"],["dc.relation.issn","0933-7407"],["dc.title","Surface moieties involved in adhesion of the pathogenic yeast C. glabrata"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Frontiers in Cellular and Infection Microbiology"],["dc.bibliographiccitation.volume","11"],["dc.contributor.author","Fernández-Pereira, Jordan"],["dc.contributor.author","Alvarado, María"],["dc.contributor.author","Gómez-Molero, Emilia"],["dc.contributor.author","Dekker, Henk L."],["dc.contributor.author","Blázquez-Muñoz, María Teresa"],["dc.contributor.author","Eraso, Elena"],["dc.contributor.author","Bader, Oliver"],["dc.contributor.author","de Groot, Piet W. J."],["dc.date.accessioned","2022-01-11T14:06:12Z"],["dc.date.available","2022-01-11T14:06:12Z"],["dc.date.issued","2021"],["dc.description.abstract","Candida glabrata is among the most prevalent causes of candidiasis. Unlike Candida albicans , it is not capable of changing morphology between yeast and hyphal forms but instead has developed other virulence factors. An important feature is its unprecedented large repertoire of predicted cell wall adhesins, which are thought to enable adherence to a variety of surfaces under different conditions. Here, we analyzed the wall proteome of PEU1221, a high biofilm-forming clinical strain isolated from an infected central venous catheter, under biofilm-forming conditions. This isolate shows increased incorporation of putative adhesins, including eight proteins that were not detected in walls of reference strain ATCC 2001, and of which Epa22, Awp14, and Awp2e were identified for the first time. The proteomics data suggest that cluster III adhesin Awp14 is relatively abundant in PEU1221. Phenotypic studies with awp14Δ deletion mutants showed that Awp14 is not responsible for the high biofilm formation of PEU1221 onto polystyrene. However, awp14Δ mutant cells in PEU1221 background showed a slightly diminished binding to chitin and seemed to sediment slightly slower than the parental strain suggesting implication in fungal cell-cell interactions. By structural modeling, we further demonstrate similarity between the ligand-binding domains of cluster III adhesin Awp14 and those of cluster V and VI adhesins. In conclusion, our work confirms the increased incorporation of putative adhesins, such as Awp14, in high biofilm-forming isolates, and contributes to decipher the precise role of these proteins in the establishment of C. glabrata infections."],["dc.description.abstract","Candida glabrata is among the most prevalent causes of candidiasis. Unlike Candida albicans , it is not capable of changing morphology between yeast and hyphal forms but instead has developed other virulence factors. An important feature is its unprecedented large repertoire of predicted cell wall adhesins, which are thought to enable adherence to a variety of surfaces under different conditions. Here, we analyzed the wall proteome of PEU1221, a high biofilm-forming clinical strain isolated from an infected central venous catheter, under biofilm-forming conditions. This isolate shows increased incorporation of putative adhesins, including eight proteins that were not detected in walls of reference strain ATCC 2001, and of which Epa22, Awp14, and Awp2e were identified for the first time. The proteomics data suggest that cluster III adhesin Awp14 is relatively abundant in PEU1221. Phenotypic studies with awp14Δ deletion mutants showed that Awp14 is not responsible for the high biofilm formation of PEU1221 onto polystyrene. However, awp14Δ mutant cells in PEU1221 background showed a slightly diminished binding to chitin and seemed to sediment slightly slower than the parental strain suggesting implication in fungal cell-cell interactions. By structural modeling, we further demonstrate similarity between the ligand-binding domains of cluster III adhesin Awp14 and those of cluster V and VI adhesins. In conclusion, our work confirms the increased incorporation of putative adhesins, such as Awp14, in high biofilm-forming isolates, and contributes to decipher the precise role of these proteins in the establishment of C. glabrata infections."],["dc.identifier.doi","10.3389/fcimb.2021.790465"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/97854"],["dc.notes.intern","DOI-Import GROB-507"],["dc.relation.eissn","2235-2988"],["dc.title","Characterization of Awp14, A Novel Cluster III Adhesin Identified in a High Biofilm-Forming Candida glabrata Isolate"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","611"],["dc.bibliographiccitation.issue","8"],["dc.bibliographiccitation.journal","Yeast"],["dc.bibliographiccitation.lastpage","624"],["dc.bibliographiccitation.volume","27"],["dc.contributor.author","de Boer, Albert D."],["dc.contributor.author","de Groot, Piet W. J."],["dc.contributor.author","Weindl, Guenther"],["dc.contributor.author","Schaller, Martin"],["dc.contributor.author","Riedel, Dietmar"],["dc.contributor.author","Diez-Orejas, Rosalia"],["dc.contributor.author","Klis, Frans M."],["dc.contributor.author","de Koster, Chris G."],["dc.contributor.author","Dekker, Henk L."],["dc.contributor.author","Gross, Uwe"],["dc.contributor.author","Bader, Oliver"],["dc.contributor.author","Weig, Michael S."],["dc.date.accessioned","2018-11-07T08:41:15Z"],["dc.date.available","2018-11-07T08:41:15Z"],["dc.date.issued","2010"],["dc.description.abstract","The glycosylphosphatidylinositol-modified protein Rhd3/Pga29 of the human pathogen Candida albicans belongs to a family of cell wall proteins that are widespread among Candida species but are not found in other fungi. Pga29 is covalently linked to the beta-1,3-glucan framework of the cell wall via beta-1,6-glucan. It is a small and abundant O-glycosylated protein and requires the protein-O-mannosyl transferase Pmt1 for glycosylation. Furthermore, Pga29 is strongly expressed in yeast cells but is downregulated in hyphae. Removal of the PGA29 gene in C. albicans leads to a significant reduction of cell wall mannan; however, Pga29 does not seem to have a major role in maintaining cell wall integrity. In addition, adhesion capacity and hyphae formation appear normal in pga29 deletion mutants. Importantly, the pga29 deletion mutant is less virulent, and infection of reconstituted human epithelium with the pga29 mutant results in a diminished induction of proinfiammatory cytokines, such as GM-CSF, TNF, IL-6 and IL-8. We propose that the reduced virulence of the pga29 mutant is a consequence of altered surface properties, resulting in altered fungal recognition. (C) Copyright 2010 John Wiley & Sons, Ltd."],["dc.identifier.doi","10.1002/yea.1790"],["dc.identifier.isi","000281227000017"],["dc.identifier.pmid","20533408"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/19423"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.relation.issn","0749-503X"],["dc.title","The Candida albicans cell wall protein Rhd3/Pga29 is abundant in the yeast form and contributes to virulence"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","UNSP fov098"],["dc.bibliographiccitation.issue","8"],["dc.bibliographiccitation.journal","FEMS Yeast Research"],["dc.bibliographiccitation.volume","15"],["dc.contributor.author","Gomez-Molero, Emilia"],["dc.contributor.author","de Boer, Albert D."],["dc.contributor.author","Dekker, Henk L."],["dc.contributor.author","Moreno-Martinez, Ana"],["dc.contributor.author","Kraneveld, Eefje A."],["dc.contributor.author","Ichsan, Ichsan"],["dc.contributor.author","Chauhan, Neeraj"],["dc.contributor.author","Weig, Michael S."],["dc.contributor.author","de Soet, Johannes J."],["dc.contributor.author","de Koster, Chris G."],["dc.contributor.author","Bader, Oliver"],["dc.contributor.author","de Groot, Piet W. J."],["dc.date.accessioned","2018-11-07T09:48:08Z"],["dc.date.available","2018-11-07T09:48:08Z"],["dc.date.issued","2015"],["dc.description.abstract","Attachment to human host tissues or abiotic medical devices is a key step in the development of infections by Candida glabrata. The genome of this pathogenic yeast codes for a large number of adhesins, but proteomic work using reference strains has shown incorporation of only few adhesins in the cell wall. By making inventories of the wall proteomes of hyperadhesive clinical isolates and reference strain CBS138 using mass spectrometry, we describe the cell wall proteome of C. glabrata and tested the hypothesis that hyperadhesive isolates display differential incorporation of adhesins. Two clinical strains (PEU382 and PEU427) were selected, which both were hyperadhesive to polystyrene and showed high surface hydrophobicity. Cell wall proteome analysis under biofilm-forming conditions identified a core proteome of about 20 proteins present in all C. glabrata strains. In addition, 12 adhesin-like wall proteins were identified in the hyperadherent strains, including six novel adhesins (Awp8-13) of which only Awp12 was also present in CBS138. We conclude that the hyperadhesive capacity of these two clinical C. glabrata isolates is correlated with increased and differential incorporation of cell wall adhesins. Future studies should elucidate the role of the identified proteins in the establishment of C. glabrata infections."],["dc.identifier.doi","10.1093/femsyr/fov098"],["dc.identifier.isi","000367341100015"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/35247"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Oxford Univ Press"],["dc.relation.issn","1567-1364"],["dc.relation.issn","1567-1356"],["dc.title","Proteomic analysis of hyperadhesive Candida glabrata clinical isolates reveals a core wall proteome and differential incorporation of adhesins"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","33"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Journal of Fungi"],["dc.bibliographiccitation.volume","7"],["dc.contributor.author","Gómez-Molero, Emilia"],["dc.contributor.author","De-la-Pinta, Iker"],["dc.contributor.author","Fernández-Pereira, Jordan"],["dc.contributor.author","Groß, Uwe"],["dc.contributor.author","Weig, Michael"],["dc.contributor.author","Quindós, Guillermo"],["dc.contributor.author","de Groot, Piet W. J."],["dc.contributor.author","Bader, Oliver"],["dc.date.accessioned","2021-04-14T08:29:40Z"],["dc.date.available","2021-04-14T08:29:40Z"],["dc.date.issued","2021"],["dc.identifier.doi","10.3390/jof7010033"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/82960"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.relation.eissn","2309-608X"],["dc.title","Candida parapsilosis Colony Morphotype Forecasts Biofilm Formation of Clinical Isolates"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1951"],["dc.bibliographiccitation.issue","11"],["dc.bibliographiccitation.journal","Eukaryotic Cell"],["dc.bibliographiccitation.lastpage","1964"],["dc.bibliographiccitation.volume","7"],["dc.contributor.author","de Groot, Piet W. J."],["dc.contributor.author","Kraneveld, Eefje A."],["dc.contributor.author","Yin, Qing Yuan"],["dc.contributor.author","Dekker, Henk L."],["dc.contributor.author","Gross, Uwe"],["dc.contributor.author","Crielaard, Wim"],["dc.contributor.author","de Koster, Chris G."],["dc.contributor.author","Bader, Oliver"],["dc.contributor.author","Klis, Frans M."],["dc.contributor.author","Weig, Michael S."],["dc.date.accessioned","2018-11-07T11:09:23Z"],["dc.date.available","2018-11-07T11:09:23Z"],["dc.date.issued","2008"],["dc.description.abstract","The cell wall of the human pathogen Candida glabrata governs initial host-pathogen interactions that underlie the establishment of fungal infections. With the aim of identifying species-specific features that may directly relate to its virulence, we have investigated the cell wall of C. glabrata using a multidisciplinary approach that combines microscopy imaging, biochemical studies, bioinformatics, and tandem mass spectrometry. Electron microscopy revealed a bilayered wall structure in which the outer layer is packed with mannoproteins. Biochemical studies showed that C. glabrata walls incorporate 50% more protein than Saccharomyces cerevisiae walls and, consistent with this, have a higher mannose/glucose ratio. Evidence is presented that C. glabrata walls contain glycosylphosphatidylinositol (GPI) proteins, covalently bound to the wall 1,6-beta-glucan, as well as proteins linked through a mild-alkali-sensitive linkage to 1,3-beta-glucan. A comprehensive genome-wide in silico inspection showed that in comparison to other fungi, C. glabrata contains an exceptionally large number, 67, of genes encoding adhesin-like GPI proteins. Phylogenetically these adhesin-like proteins form different clusters, one of which is the lectin-like EPA family. Mass spectrometric analysis identified 23 cell wall proteins, including 4 novel adhesin-like proteins, Awp1/2/3/4, and Epa6, which is involved in adherence to human epithelia and biofilm formation. Importantly, the presence of adhesin-like proteins in the wall depended on the growth stage and on the genetic background used, and this was reflected in alterations in adhesion capacity and cell surface hydrophobicity. We propose that the large repertoire of adhesin(-like) genes of C. glabrata contributes to its adaptability and virulence."],["dc.description.sponsorship","DFG [WE 3537/1-2]; EU [LSHB-CT-2004-511952]"],["dc.identifier.doi","10.1128/EC.00284-08"],["dc.identifier.isi","000260623300009"],["dc.identifier.pmid","18806209"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/52999"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Soc Microbiology"],["dc.relation.issn","1535-9786"],["dc.relation.issn","1535-9778"],["dc.title","The Cell Wall of the Human Pathogen Candida glabrata: Differential Incorporation of Novel Adhesin-Like Wall Proteins"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","470"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Eukaryotic Cell"],["dc.bibliographiccitation.lastpage","481"],["dc.bibliographiccitation.volume","12"],["dc.contributor.author","de Groot, Piet W. J."],["dc.contributor.author","Bader, Oliver"],["dc.contributor.author","de Boer, Albert D."],["dc.contributor.author","Weig, Michael S."],["dc.contributor.author","Chauhan, Neeraj"],["dc.date.accessioned","2018-11-07T09:26:40Z"],["dc.date.available","2018-11-07T09:26:40Z"],["dc.date.issued","2013"],["dc.description.abstract","Understanding the pathogenesis of an infectious disease is critical for developing new methods to prevent infection and diagnose or cure disease. Adherence of microorganisms to host tissue is a prerequisite for tissue invasion and infection. Fungal cell wall adhesins involved in adherence to host tissue or abiotic medical devices are critical for colonization leading to invasion and damage of host tissue. Here, with a main focus on pathogenic Candida species, we summarize recent progress made in the field of adhesins in human fungal pathogens and underscore the importance of these proteins in establishment of fungal diseases."],["dc.identifier.doi","10.1128/EC.00364-12"],["dc.identifier.isi","000316805100001"],["dc.identifier.pmid","23397570"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/30349"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Soc Microbiology"],["dc.relation.issn","1535-9786"],["dc.relation.issn","1535-9778"],["dc.title","Adhesins in Human Fungal Pathogens: Glue with Plenty of Stick"],["dc.type","review"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","International Journal of Medical Microbiology"],["dc.bibliographiccitation.volume","303"],["dc.contributor.author","Tangwattanachuleeporn, Marut"],["dc.contributor.author","Bader, Oliver"],["dc.contributor.author","de Groot, Piet W. J."],["dc.contributor.author","Schwarzmueller, T."],["dc.contributor.author","Kuchler, K."],["dc.contributor.author","Gross, U."],["dc.contributor.author","Weig, Michael S."],["dc.date.accessioned","2018-11-07T09:20:05Z"],["dc.date.available","2018-11-07T09:20:05Z"],["dc.date.issued","2013"],["dc.format.extent","15"],["dc.identifier.isi","000331497600047"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/28793"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Elsevier Gmbh, Urban & Fischer Verlag"],["dc.publisher.place","Jena"],["dc.relation.conference","65th Annual Meeting of the German-Society-for-Hygiene-and-Microbiology (DGHM) e V / Annual Meeting of the German-Society-for-Infectious-Diseases (DGI) e V"],["dc.relation.eventlocation","Univ Rostock, Rostock, GERMANY"],["dc.relation.issn","1618-0607"],["dc.relation.issn","1438-4221"],["dc.title","Studies on the role of the GPI-anchored Ecm33 protein family in Candida glabrata"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","493"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Pathogens"],["dc.bibliographiccitation.volume","10"],["dc.contributor.author","Moreno-Martínez, Ana Esther"],["dc.contributor.author","Gómez-Molero, Emilia"],["dc.contributor.author","Sánchez-Virosta, Pablo"],["dc.contributor.author","Dekker, Henk L."],["dc.contributor.author","de Boer, Albert"],["dc.contributor.author","Eraso, Elena"],["dc.contributor.author","Bader, Oliver"],["dc.contributor.author","de Groot, Piet W. J."],["dc.date.accessioned","2021-06-01T09:42:40Z"],["dc.date.available","2021-06-01T09:42:40Z"],["dc.date.issued","2021"],["dc.description.abstract","Candida parapsilosis is among the most frequent causes of candidiasis. Clinical isolates of this species show large variations in colony morphotype, ranging from round and smooth to a variety of non-smooth irregular colony shapes. A non-smooth appearance is related to increased formation of pseudohyphae, higher capacity to form biofilms on abiotic surfaces, and invading agar. Here, we present a comprehensive study of the cell wall proteome of C. parapsilosis reference strain CDC317 and seven clinical isolates under planktonic and sessile conditions. This analysis resulted in the identification of 40 wall proteins, most of them homologs of known Candida albicans cell wall proteins, such as Gas, Crh, Bgl2, Cht2, Ecm33, Sap, Sod, Plb, Pir, Pga30, Pga59, and adhesin family members. Comparative analysis of exponentially growing and stationary phase planktonic cultures of CDC317 at 30 °C and 37 °C revealed only minor variations. However, comparison of smooth isolates to non-smooth isolates with high biofilm formation capacity showed an increase in abundance and diversity of putative wall adhesins from Als, Iff/Hyr, and Hwp families in the latter. This difference depended more strongly on strain phenotype than on the growth conditions, as it was observed in planktonic as well as biofilm cells. Thus, in the set of isolates analyzed, the high biofilm formation capacity of non-smooth C. parapsilosis isolates with elongated cellular phenotypes correlates with the increased surface expression of putative wall adhesins in accordance with their proposed cellular function."],["dc.identifier.doi","10.3390/pathogens10040493"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/85318"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-425"],["dc.relation.eissn","2076-0817"],["dc.title","High Biofilm Formation of Non-Smooth Candida parapsilosis Correlates with Increased Incorporation of GPI-Modified Wall Adhesins"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]