Masanta, Wycliffe Omurwa

[["dc.bibliographiccitation.artnumber","4244"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Scientific Reports"],["dc.bibliographiccitation.volume","9"],["dc.contributor.author","Emele, Matthias Frederik"],["dc.contributor.author","Možina, Sonja Smole"],["dc.contributor.author","Lugert, Raimond"],["dc.contributor.author","Bohne, Wolfgang"],["dc.contributor.author","Masanta, Wycliffe Omurwa"],["dc.contributor.author","Riedel, Thomas"],["dc.contributor.author","Groß, Uwe"],["dc.contributor.author","Bader, Oliver"],["dc.contributor.author","Zautner, Andreas Erich"],["dc.date.accessioned","2019-07-09T11:50:14Z"],["dc.date.available","2019-07-09T11:50:14Z"],["dc.date.issued","2019"],["dc.description.abstract","Besides Campylobacter jejuni, Campylobacter coli is the most common bacterial cause of gastroenteritis worldwide. C. coli is subdivided into three clades, which are associated with sample source. Clade 1 isolates are associated with acute diarrhea in humans whereas clade 2 and 3 isolates are more commonly obtained from environmental waters. The phylogenetic classification of an isolate is commonly done using laborious multilocus sequence typing (MLST). The aim of this study was to establish a proteotyping scheme using MALDI-TOF MS to offer an alternative to sequence-based methods. A total of 97 clade-representative C. coli isolates were analyzed by MALDI-TOF-based intact cell mass spectrometry (ICMS) and evaluated to establish a C. coli proteotyping scheme. MLST was used as reference method. Different isoforms of the detectable biomarkers, resulting in biomarker mass shifts, were associated with their amino acid sequences and included into the C. coli proteotyping scheme. In total, we identified 16 biomarkers to differentiate C. coli into the three clades and three additional sub-clades of clade 1. In this study, proteotyping has been successfully adapted to C. coli. The established C. coli clades and sub-clades can be discriminated using this method. Especially the clinically relevant clade 1 isolates can be differentiated clearly."],["dc.identifier.doi","10.1038/s41598-019-40842-w"],["dc.identifier.pmid","30862911"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/15886"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/59727"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.relation.issn","2045-2322"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.subject.ddc","610"],["dc.title","Proteotyping as alternate typing method to differentiate Campylobacter coli clades"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","1800083"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","PROTEOMICS – Clinical Applications"],["dc.bibliographiccitation.volume","13"],["dc.contributor.author","Masanta, Wycliffe O."],["dc.contributor.author","Zautner, Andreas E."],["dc.contributor.author","Lugert, Raimond"],["dc.contributor.author","Bohne, Wolfgang"],["dc.contributor.author","Gross, Uwe"],["dc.contributor.author","Leha, Andreas"],["dc.contributor.author","Dakna, Mohammed"],["dc.contributor.author","Lenz, Christof"],["dc.date.accessioned","2019-07-09T11:51:53Z"],["dc.date.available","2019-07-09T11:51:53Z"],["dc.date.issued","2018"],["dc.description.abstract","PURPOSE: Bile acids are crucial components of the intestinal antimicrobial defense and represent a significant stress factor for enteric pathogens. Adaptation processes of Campylobacter jejuni to this hostile environment are analyzed in this study by a proteomic approach. EXPERIMENTAL DESIGN: Proteome profiling by label-free mass spectrometry (SWATH-MS) has been used to characterize the adaptation of C. jejuni to sublethal concentrations of seven bile acids. RESULTS: The bile acids with the lowest inhibitory concentration (IC50 ), deoxycholic and chenodeoxycholic acid, induce the most significant proteome changes. Overall a downregulation of all basic biosynthetic pathways and a general decrease in the transcription machinery are found. Concurrently, an induction of factors involved in detoxification of reactive oxygen species, protein folding, and bile acid exporting efflux pumps is detected. Exposure to deoxycholic and chenodeoxycholic acid results in an increased expression of components of the more energy-efficient aerobic respiration pathway, while the anaerobic branches of the electron transport chain are down-expressed. CONCLUSIONS AND CLINICAL RELEVANCE: The results show that C. jejuni has a differentiated system of adaptation to bile acid stresses. The findings enhance the understanding of the pathogenesis of campylobacteriosis, especially for survival of C. jejuni in the human intestine, and may provide clues to future medical treatment."],["dc.identifier.doi","10.1002/prca.201800083"],["dc.identifier.pmid","30246935"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/16217"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/60032"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.subject.ddc","610"],["dc.title","Proteome Profiling by Label‐Free Mass Spectrometry Reveals Differentiated Response of Campylobacter jejuni 81–176 to Sublethal Concentrations of Bile Acids"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]