2024
Coinfection and clinical impact of enterotoxigenic Escherichia coli harboring diverse toxin variants and colonization factors: 2017-2022
Amin M, Akhtar M, Khan Z, Islam T, Firoj G, Begum Y, Rahman S, Afrad M, Bhuiyan T, Chowdhury F, Faruque A, Ryan E, Qadri F, Khan A. Coinfection and clinical impact of enterotoxigenic Escherichia coli harboring diverse toxin variants and colonization factors: 2017-2022. International Journal Of Infectious Diseases 2024, 151: 107365. PMID: 39694230, PMCID: PMC11798591, DOI: 10.1016/j.ijid.2024.107365.Peer-Reviewed Original ResearchEnterotoxigenic Escherichia coliCo-InfectionVibrio choleraeEnterotoxigenic Escherichia coli infectionDiarrheal Disease Surveillance SystemLikelihood of feverRisk of vomitingColonization factorsOverburden healthcare systemsShigella sppV. choleraeToxin variantsSalmonella sppEnteric pathogensClinical outcomesClinical manifestationsClinical impactIntravenous fluidsRisk factorsIllness severityVibrioPatientsRotavirusDisease surveillance systemsInfectionVibrio 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 bond
2023
New Insights into Vibrio cholerae Biofilms from Molecular Biophysics to Microbial Ecology
Tai J, Ferrell M, Yan J, Waters C. New Insights into Vibrio cholerae Biofilms from Molecular Biophysics to Microbial Ecology. Advances In Experimental Medicine And Biology 2023, 1404: 17-39. PMID: 36792869, PMCID: PMC10726288, DOI: 10.1007/978-3-031-22997-8_2.Peer-Reviewed Original ResearchConceptsV. cholerae biofilmsBacterial signal transduction networkSignal transduction networksBiofilm formationVibrio cholerae biofilmsKey model systemV. choleraeEcological roleMicrobial ecologyTransduction networksBiofilm maturationEnvironmental survivalCholera pathogenesisMolecular biophysicsRegulatory systemVibrio choleraeEl Tor biotypeBacterial surface attachmentRecent insightsModel systemBiofilmsLife cycleSurface attachmentCholeraeCentral function
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
2021
CO 2 -Driven diffusiophoresis for maintaining a bacteria-free surface
Shim S, Khodaparast S, Lai CY, Yan J, Ault JT, Rallabandi B, Shardt O, Stone HA. CO 2 -Driven diffusiophoresis for maintaining a bacteria-free surface. Soft Matter 2021, 17: 2568-2576. PMID: 33514979, DOI: 10.1039/d0sm02023k.Peer-Reviewed Original ResearchConceptsWild-type V. choleraeCell shapeBacterial cellsDirectional migrationV. choleraeCO2 gradientNonzero surface chargeP. aeruginosaCellsCO2 sourcesFlagellaCO2 concentration gradientBacteriaCholeraeDirectional responseBacteria-free surfaceGram stainMotilityAnti-biofouling surfacesConcentration gradientGradientAeruginosa
2016
Chemoproteomic profiling of host and pathogen enzymes active in cholera
Hatzios SK, Abel S, Martell J, Hubbard T, Sasabe J, Munera D, Clark L, Bachovchin DA, Qadri F, Ryan ET, Davis BM, Weerapana E, Waldor MK. Chemoproteomic profiling of host and pathogen enzymes active in cholera. Nature Chemical Biology 2016, 12: 268-274. PMID: 26900865, PMCID: PMC4765928, DOI: 10.1038/nchembio.2025.Peer-Reviewed Original Research
2010
Toxin Mediated Diarrhea in the 21st Century: The Pathophysiology of Intestinal Ion Transport in the Course of ETEC, V. cholerae and Rotavirus Infection
Kopic S, Geibel JP. Toxin Mediated Diarrhea in the 21st Century: The Pathophysiology of Intestinal Ion Transport in the Course of ETEC, V. cholerae and Rotavirus Infection. Toxins 2010, 2: 2132-2157. PMID: 22069677, PMCID: PMC3153279, DOI: 10.3390/toxins2082132.Peer-Reviewed Original ResearchConceptsEpisodes of diarrheaIntestinal ion transportSpecific therapeutic approachesMajor healthcare concernRotavirus infectionTherapeutic approachesV. choleraeCommon enterotoxinInfectious agentsPathophysiological processesInfectious diseasesDiarrheaHealthcare concernCellular mechanismsLethal effectsPathophysiologyYearsInfectionCholeraeRotavirusDiseaseETEC
2007
The structural basis of cyclic diguanylate signal transduction by PilZ domains
Benach J, Swaminathan SS, Tamayo R, Handelman SK, Folta‐Stogniew E, Ramos JE, Forouhar F, Neely H, Seetharaman J, Camilli A, Hunt JF. The structural basis of cyclic diguanylate signal transduction by PilZ domains. The EMBO Journal 2007, 26: 5153-5166. PMID: 18034161, PMCID: PMC2140105, DOI: 10.1038/sj.emboj.7601918.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBacterial ProteinsBinding SitesCrystallography, X-RayCyclic GMPHumansMiceModels, MolecularMolecular ConformationMolecular Sequence DataPhylogenyProtein BindingProtein Structure, QuaternaryProtein Structure, SecondaryProtein Structure, TertiarySequence AlignmentSequence Homology, Amino AcidSignal TransductionVibrio choleraeConceptsPilZ domain-containing proteinsPilZ domainDomain-containing proteinsN-terminal domainConformational switchSecond messenger cyclic diguanylateBeta-barrel foldN-terminal loopEvolutionary diversificationCyclic diguanylateSignal transductionBioinformatics analysisStructural basisInteraction surfaceSessile growthEffector pathwaysVibrio choleraeProteinV. choleraeGMPCholeraeDomainClose appositionDiguanylateEubacteria
1999
The Vibrio cholerae O139 Calcutta Bacteriophage CTXφ Is Infectious and Encodes a Novel Repressor
Davis B, Kimsey H, Chang W, Waldor M. The Vibrio cholerae O139 Calcutta Bacteriophage CTXφ Is Infectious and Encodes a Novel Repressor. Journal Of Bacteriology 1999, 181: 6779-6787. PMID: 10542181, PMCID: PMC94144, DOI: 10.1128/jb.181.21.6779-6787.1999.Peer-Reviewed Original Research
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