Please use this identifier to cite or link to this item: https://ir.swu.ac.th/jspui/handle/123456789/14957
Full metadata record
DC FieldValueLanguage
dc.contributor.authorSakolvaree Y.
dc.contributor.authorManeewatch S.
dc.contributor.authorJiemsup S.
dc.contributor.authorKlaysing B.
dc.contributor.authorTongtawe P.
dc.contributor.authorSrimanote P.
dc.contributor.authorSaengjaruk P.
dc.contributor.authorBanyen S.
dc.contributor.authorTapchaisri P.
dc.contributor.authorChonsa-nguan M.
dc.contributor.authorChaicumpa W.
dc.date.accessioned2021-04-05T04:32:13Z-
dc.date.available2021-04-05T04:32:13Z-
dc.date.issued2007
dc.identifier.issn0125877X
dc.identifier.other2-s2.0-34250897884
dc.identifier.urihttps://ir.swu.ac.th/jspui/handle/123456789/14957-
dc.identifier.urihttps://www.scopus.com/inward/record.uri?eid=2-s2.0-34250897884&partnerID=40&md5=3de8bb1a6da33498cf7753d12ffff957
dc.description.abstractIn this study, proteomes of two pathogenic Leptospira spp., namely L. interrogans, serogroup Icterohaemorrhagiae, serovar Copenhageni and L. borgpetersenii, serogroup Tarassovi, serovar Tarassovi, were revealed by using two dimensional gel electrophoresis (2DE)-based-proteomics. Bacterial cells were disrupted in a lysis buffer containing 30 mM Tris, 2 M thiourea, 7 M urea, 4% CHAPS, 2% IPG buffer pH 3-10 and protease inhibitors and then subjected to sonication in order to solubilize as much as possible the bacterial proteins. The 2DE-separated components of both Leptospira homogenates were blotted individually onto membranes and antigenic components (immunomes) were revealed by probing the blots with immune serum of a mouse readily immunized with the homogenate of L. interrogans, serogroup Icterohaemorrhagiae, serovar Copenhageni. The immunogenic proteins of the two pathogenic Leptospira spp. could be grouped into 10 groups. These are: 1) proteins involved in the bacterial transcription and translation including beta subunit transcription anti-termination protein of DNA polymerase III, elongation factors Tu and Ts, and tRNA (guanine-N1)-methyltransferase; 2) proteins functioning as enzymes for metabolisms and nutrient acquisition including acetyl-Co-A acetyltransferase, putative glutamine synthetase, glyceraldehyde-3-phospahte dehydrogenase, NifU-like protein, 3-oxoacyl-(acyl-carrier-protein) reductase, oxidoreductase, sphingomyelinase C precursor, spermidine synthase, beta subunit of succinyl-CoA synthetase, and succinate dehydrogenase iron-sulfur subunit; 3) proteins/enzymes necessary for energy and electron transfer, i.e. electron transfer flavoprotein, and proton-translocating transhydrogenase; 4) enzymes for degradation of misfolded proteins, i.e. ATP-dependent Cip protease; 5) molecular chaperone, i.e. 60 kDa chaperonin; 6) signal transduction system, i.e. response regulator; 7) protein involved in immune evasion in host, i.e. peroxiredoxin; 8) cell structure proteins including MreB (cytoskeletal) and flagellin/ periplasmic flagellin; 9) lipoproteins/outer membrane proteins: LipL32, LipL41, LipL45 and OmpL1; and 10) various hypothetical proteins. Many immunogenic proteins are common to both Leptospira spp. These proteins not only are the diagnostic targets but also have potential as candidates of a broad spectrum leptospirosis vaccine especially the surface exposed components which should be vulnerable to the host immune effector factors.
dc.subject3 [(3 cholamidopropyl)dimethylammonio] 1 propanesulfonic acid
dc.subject3 oxoacyl acyl carrier protein synthase
dc.subjectacetyl coenzyme A acetyltransferase
dc.subjectbacterial protein
dc.subjectbacterial vaccine
dc.subjectchaperone
dc.subjectchaperonin
dc.subjectDNA directed DNA polymerase gamma
dc.subjectelongation factor Ts
dc.subjectelongation factor Tu
dc.subjectendopeptidase Clp
dc.subjectflavoprotein
dc.subjectgene product
dc.subjectglutamate ammonia ligase
dc.subjectglyceraldehyde 3 phosphate dehydrogenase
dc.subjectleptospirosis vaccine
dc.subjectlipoprotein
dc.subjectnicotinamide adenine dinucleotide (phosphate) transhydrogenase
dc.subjectNifU like protein
dc.subjectouter membrane protein
dc.subjectoxidoreductase
dc.subjectproteinase inhibitor
dc.subjectproteome
dc.subjectspermidine synthase
dc.subjectsphingomyelin phosphodiesterase
dc.subjectsuccinate dehydrogenase
dc.subjectsuccinyl coenzyme A synthetase
dc.subjecttransfer RNA methyltransferase
dc.subjectunclassified drug
dc.subjecturea
dc.subjectarticle
dc.subjectbacterial cell
dc.subjectblood analysis
dc.subjectcell disruption
dc.subjectcontrolled study
dc.subjectdrug design
dc.subjectdrug targeting
dc.subjectelectron transport
dc.subjectenergy transfer
dc.subjectgenetic transcription and translation
dc.subjecthomogenate
dc.subjectimmune response
dc.subjectimmunoblotting
dc.subjectLeptospira
dc.subjectLeptospira borgpetersenii
dc.subjectLeptospira interrogans
dc.subjectleptospirosis
dc.subjectmale
dc.subjectmouse
dc.subjectnonhuman
dc.subjectnucleotide sequence
dc.subjectprotein analysis
dc.subjectprotein degradation
dc.subjectprotein folding
dc.subjectprotein function
dc.subjectprotein targeting
dc.subjectsignal transduction
dc.subjectspecies difference
dc.subjecttwo dimensional gel electrophoresis
dc.subjectultrasound
dc.subjectAmino Acid Sequence
dc.subjectAnimals
dc.subjectAntigens, Bacterial
dc.subjectBlotting, Western
dc.subjectElectrophoresis, Gel, Two-Dimensional
dc.subjectLeptospira
dc.subjectLeptospira interrogans serovar icterohaemorrhagiae
dc.subjectLeptospirosis
dc.subjectMale
dc.subjectMice
dc.subjectMice, Inbred BALB C
dc.subjectMolecular Sequence Data
dc.subjectProteome
dc.subjectProteomics
dc.titleProteome and immunome of pathogenic Leptospira spp. revealed by 2DE and 2DE-immunoblotting with immune serum
dc.typeArticle
dc.rights.holderScopus
dc.identifier.bibliograpycitationAsian Pacific Journal of Allergy and Immunology. Vol 25, No.1 (2007), p.53-73
Appears in Collections:Scopus 1983-2021

Files in This Item:
There are no files associated with this item.


Items in SWU repository are protected by copyright, with all rights reserved, unless otherwise indicated.