2025
Comprehensive genomic and evolutionary analysis of biofilm matrix clusters and proteins in the Vibrio genus
Yang Y, Yan J, Olson R, Jiang X. Comprehensive genomic and evolutionary analysis of biofilm matrix clusters and proteins in the Vibrio genus. MSystems 2025, 10: e00060-25. PMID: 40207939, PMCID: PMC12090793, DOI: 10.1128/msystems.00060-25.Peer-Reviewed Original ResearchConceptsGene clusterVibrio speciesEvolutionary analysisBiofilm dispersalBiofilm matrix proteinsVibrio cholerae</i>Genetic modificationTail proteinsVibrio genusCholera pathogenIdentified genesGene groupsVibrio cholerae</i>.Host functionsEvolutionary patternsBiofilm diversityBiofilm formationBiofilm proteinsBiofilm matrixVibrioBiofilm developmentEngineered biofilmsGenusStructural domainsAcute diarrheal diseaseNon-disruptive matrix turnover is a conserved feature of biofilm aggregate growth in paradigm pathogenic species
Reichhardt C, Matwichuk M, Lewerke L, Jacobs H, Yan J, Parsek M. Non-disruptive matrix turnover is a conserved feature of biofilm aggregate growth in paradigm pathogenic species. MBio 2025, 16: e03935-24. PMID: 39982068, PMCID: PMC11898600, DOI: 10.1128/mbio.03935-24.Peer-Reviewed Original ResearchConceptsSynthesize EPSBiofilm aggregatesBiofilm matrixBiofilm matrix exopolysaccharidesBiofilm-forming speciesBiofilm matrix compositionStudy of biofilmsMatrix exopolysaccharidesVibrio cholerae</i>.Cellular biomassPathogenic speciesModel organismsBacterial speciesExtracellular DNAExopolysaccharideBiofilm stabilityMulticellular aggregatesCell-free matricesBiofilmCell-free formSpeciesMatrix turnoverAggregate peripheryBacteriaMatrix components
2024
Vibrio cholerae RbmB is an α-1,4-polysaccharide lyase with biofilm-disrupting activity against Vibrio polysaccharide (VPS)
Weerasekera R, Moreau A, Huang X, Nam K, Hinbest A, Huynh Y, Liu X, Ashwood C, Pepi L, Paulson E, Cegelski L, Yan J, Olson R. Vibrio cholerae RbmB is an α-1,4-polysaccharide lyase with biofilm-disrupting activity against Vibrio polysaccharide (VPS). PLOS Pathogens 2024, 20: e1012750. PMID: 39621768, PMCID: PMC11637428, DOI: 10.1371/journal.ppat.1012750.Peer-Reviewed Original ResearchVibrio polysaccharideBiofilm dispersalHuman pathogen Vibrio choleraeV. cholerae biofilmsPathogen Vibrio choleraeBiofilm disruption activityFormation of biofilmsVibrio coralliilyticusPolysaccharide lyasesLyase mechanismV. choleraeVibrio choleraeBiofilm matrixPathogenic bacteriaRbmBAntibacterial enzymesSecreted macromoleculesSolid-state NMRGlycolytic enzymesFluorescence-based biochemical assayBiofilmBiochemical assaysEnzymeSecreted glycosidasesDouble bondOuter membrane vesicles and the outer membrane protein OmpU govern Vibrio cholerae biofilm matrix assembly
Potapova A, Garvey W, Dahl P, Guo S, Chang Y, Schwechheimer C, Trebino M, Floyd K, Phinney B, Liu J, Malvankar N, Yildiz F. Outer membrane vesicles and the outer membrane protein OmpU govern Vibrio cholerae biofilm matrix assembly. MBio 2024, 15: e03304-23. PMID: 38206049, PMCID: PMC10865864, DOI: 10.1128/mbio.03304-23.Peer-Reviewed Original ResearchConceptsBiofilm matrix assemblyOuter membrane proteinsOuter membrane protein OmpUOuter membrane vesiclesBiofilm formationBiofilm matrixMatrix assemblyMatrix proteinsBiofilm architectureExtracellular DNAPresence of outer membrane proteinsCausative agent of choleraMembrane vesiclesAgent of choleraBiofilm matrix proteinsBiofilm matrix componentsVibrio cholerae</i>Single-cell force spectroscopyCell surface adhesion forceMatrix proteomeVibrio cholerae</i>.OmpUHuman pathogensMicrobial communitiesEnvironmental survival
2022
Molecular Mechanism of Vibrio cholerae biofilm adhesion
Weerasekera R, Hinbest A, Nero T, Huang X, Yan J, Olson R. Molecular Mechanism of Vibrio cholerae biofilm adhesion. The FASEB Journal 2022, 36 DOI: 10.1096/fasebj.2022.36.s1.l7499.Peer-Reviewed Original ResearchΒ-prism domainV. cholerae biofilmsBiofilm matrixAbiotic surfacesCommunity of microorganismsComplex N-glycansΒ-propeller domainHost colonizationSequence identityAdhesion proteinsDistinct functionsMolecular mechanismsN-glycansBacterial cellsFunctional assaysHost surfaceVirulence factorsVibrio choleraeProteinMain proteinsV. choleraeSpecific adhesion moleculesBiofilmsBAP1Cholerae
2016
The BR domain of PsrP interacts with extracellular DNA to promote bacterial aggregation; structural insights into pneumococcal biofilm formation
Schulte T, Mikaelsson C, Beaussart A, Kikhney A, Deshmukh M, Wolniak S, Pathak A, Ebel C, Löfling J, Fogolari F, Henriques-Normark B, Dufrêne YF, Svergun D, Nygren PÅ, Achour A. The BR domain of PsrP interacts with extracellular DNA to promote bacterial aggregation; structural insights into pneumococcal biofilm formation. Scientific Reports 2016, 6: 32371. PMID: 27582320, PMCID: PMC5007671, DOI: 10.1038/srep32371.Peer-Reviewed Original ResearchConceptsPneumococcal biofilm formationBiofilm formationExtracellular DNAPneumococcal serine-rich repeat proteinRich repeat proteinElectrophoretic mobility shift assaysHuman pathogen Streptococcus pneumoniaeAdhesive matrix moleculesMobility shift assaysMicrobial surface componentsMajor human pathogen Streptococcus pneumoniaeN-terminal regionNon-globular structuresSerine-rich repeat proteinPathogen Streptococcus pneumoniaeHelical DNA structureRepeat proteinsHeterologous expressionCircular dichroism studiesBR domainShift assaysStructural insightsBiofilm matrixIntermolecular β-sheetsBacterial aggregation
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