N-Terminal Gly224–Gly411 Domain in Listeria Adhesion Protein Interacts with Host Receptor Hsp60 英文参考文献.docVIP

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N-Terminal Gly224–Gly411 Domain in Listeria Adhesion Protein Interacts with Host Receptor Hsp60 英文参考文献.doc

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N-Terminal Gly224–Gly411 Domain in Listeria Adhesion Protein Interacts with Host Receptor Hsp60 英文参考文献

N-TerminalGly224–Gly411 DomaininListeriaAdhesion ProteinInteractswithHostReceptorHsp60 BalamuruganJagadeesan1,AmyE.FleishmanLittlejohn1,2,MaryAnneRoshniAmalaradjou1,AtulK. Singh1,KrishnaK.Mishra1,DavidLa3,DaisukeKihara2,3,4,ArunK.Bhunia1,2,5 * 1Molecular Food Microbiology Laboratory, Department of Food Science, Purdue University, West Lafayette, Indiana, United States of America, 2Purdue University InterdisciplinaryLifeSciencesProgram,PurdueUniversity,WestLafayette,Indiana,UnitedStatesofAmerica,3DepartmentofBiologicalSciences,PurdueUniversity,West Lafayette,Indiana,UnitedStatesofAmerica,4DepartmentofComputerScience,PurdueUniversity,WestLafayette,Indiana,UnitedStatesofAmerica,5Departmentof ComparativePathobiology,PurdueUniversity,WestLafayette,Indiana,UnitedStatesofAmerica Abstract Background:Listeriaadhesionprotein(LAP)isahousekeepingbifunctionalenzymeconsistingofN-terminalacetaldehyde dehydrogenase (ALDH) and C-terminal alcohol dehydrogenase (ADH). It aids Listeria monocytogenes in crossing the epithelialbarrierthroughaparacellularroutebyinteractingwithitshostreceptor,heatshockprotein60(Hsp60).Togain insightintothebindinginteractionbetweenLAPandHsp60,LAPsubdomain(s)participatingintheHsp60interactionwere investigated. Methods:UsingaModBasestructuralmodel,LAPwasdividedinto4putativesubdomains:theALDHregioncontainsN1 (Met1–Pro223) and N2 (Gly224–Gly411), and the ADH region contains C1 (Gly412–Val648) and C2 (Pro649–Val866). Each subdomainwasclonedandoverexpressedinEscherichiacoliandpurified.Purifiedsubdomainswereusedinligandoverlay, immunofluorescence, and bead-based epithelial cell adhesion assays to analyze each domain’s affinity toward Hsp60 proteinorhumanileocecalepithelialHCT-8cells. Results:TheN2subdomainexhibitedthegreatestaffinityforHsp60withaK of9.5062.6nM.TheK offull-lengthLAP D D (7.260.5nM)toHsp60wascomparabletotheN2value.Microspheres(1 mmdiameter)coatedwithN2subdomainshowed significantly (P,0.05) higher binding to HCT-8 cells than beads co