0000000000323316

AUTHOR

Antonio Caminero

showing 3 related works from this author

Identification ofCandida albicanswall mannoproteins covalently linked by disulphide and/or alkali-sensitive bridges

2014

This paper describes the results obtained by analysing the human pathogen Candida albicans cell wall subproteome by mass spectrometry, using extraction procedures aimed at releasing proteins bound by disulphide bridges (RAE-CWP) or alkali-labile ester linkages (ALS-CWP). Ten of the total proteins released from the wall by β-ME and/or NaOH contained a potential signal peptide, lacked a GPI cell wall hydrophobic C-terminal domain and were identified as true wall proteins by in silico analysis, whereas four additional proteins were identified as bound to the plasma membrane. The results surprisingly demonstrated that, in addition to the expected RAE-CWP and ALS-CWP proteins, 16 GPI proteins we…

Signal peptidebiologyIn silicoBioengineeringbiology.organism_classificationMass spectrometryApplied Microbiology and BiotechnologyBiochemistryCorpus albicansCell wallMembraneBiochemistryCovalent bondGeneticsCandida albicanshuman activitiesBiotechnologyYeast
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Analysis of the 3H8 antigen of Candida albicans reveals new aspects of the organization of fungal cell wall proteins.

2017

The walls of both, yeast and mycelial cells of Candida albicans possess a species-specific antigen that is recognized by a monoclonal antibody (MAb 3H8). This antigen can be extracted in the form of a very high Mr complex, close or over 106 Da, by treatment, with β-1,3-glucanase, β mercaptoethanol or dithothreitol, or mild alkali, but not by saturated hydrogen fluoride (HF) in pyridine, suggesting that the complex is bound to wall β-1,3 glucans, and to proteins by disulfide bonds, but not to β-1,6 glucans. Through its sensitivity to trypsin and different deglycosylation procedures, it was concluded that the epitope is associated to a glycoprotein containing N-glycosidic, but not O-glycosidi…

0301 basic medicineAntigens FungalMacromolecular SubstancesApplied Microbiology and BiotechnologyMicrobiologyEpitopeMass SpectrometryCell wall03 medical and health sciencesAntigenCell WallCandida albicansmedicineCandida albicansPolyacrylamide gel electrophoresisAntibodies FungalMannanchemistry.chemical_classificationbiologyAntibodies MonoclonalGeneral Medicinebiology.organism_classificationTrypsinMicroscopy Electron030104 developmental biologyBiochemistrychemistryElectrophoresis Polyacrylamide GelGlycoproteinmedicine.drugFEMS yeast research
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TheGCA1gene encodes a glycosidase-like protein in the cell wall ofCandida albicans

2016

Candida albicans Gca1p is a putative glucoamylase enzyme which contains 946 amino acids, 11 putative sites for N -glycosylation and 9 for O -glycosylation. Gca1p was identified in β-mercaptoethanol extracts from isolated cell walls of strain C. albicans SC5314 and it is involved in carbohydrate metabolism. The significance and the role of this protein within the cell wall structure were studied in the corresponding mutants. The homozygous mutant showed that GCA1 was not an essential gene for cell viability. Subsequent phenotypic analysis performed in the mutants obtained did not show significant difference in the behavior of mutant when compared with the wild strain SC5314. Zymoliase, Calco…

0301 basic medicineGlycosylationGlycoside HydrolasesGenes Fungal030106 microbiologyMutantCalcofluor-whiteApplied Microbiology and BiotechnologyMicrobiologyCell wallGene Knockout Techniques03 medical and health scienceschemistry.chemical_compoundGlucosidesCell WallCandida albicansCandida albicanschemistry.chemical_classificationMicrobial ViabilitybiologyGeneral Medicinebiology.organism_classificationMolecular biologyEnzyme assayCorpus albicansEnzymechemistryBiochemistrybiology.proteinFEMS Yeast Research
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