Proteomic Analysis of Excretory-Secretory Products of Heligmosomoides polygyrus Assessed with Next-Generation Sequencing Transcriptomic Information 英文参考文献.docVIP
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Proteomic Analysis of Excretory-Secretory Products of Heligmosomoides polygyrus Assessed with Next-Generation Sequencing Transcriptomic Information 英文参考文献
ProteomicAnalysisofExcretory-SecretoryProductsof
HeligmosomoidespolygyrusAssessedwithNext-
GenerationSequencingTranscriptomicInformation
YovanyMoreno1,Pierre-PaulGros2,MifongTam2,MarielaSegura2,RajeshValanparambil2,TimothyG.
Geary1,MaryM.Stevenson2*
1InstituteofParasitologyandCentreforHostParasiteInteractions,McGillUniversity,Ste-AnnedeBellevue,Quebec,Canada,2CentrefortheStudyofHostResistance
andCentreforHostParasiteInteractions,TheResearchInstituteofMcGillUniversityHealthCentreandDepartmentofMedicine,McGillUniversity,Montreal,Quebec,
Canada
Abstract
The murine parasite Heligmosomoides polygyrus is a convenient experimental model to study immune responses and
pathologyassociatedwithgastrointestinalnematodeinfections.Theexcretory-secretoryproducts(ESP)producedbythis
parasitehavepotentimmunomodulatoryactivity,buttheprotein(s)responsiblehasnotbeendefined.Identificationofthe
proteincompositionofESPderivedfromH.polygyrusandotherrelevantnematodespecieshasbeenhamperedbythelack
of genomic sequence information required for proteomic analysis based on database searches. To overcome this, a
transcriptome next generation sequencing (RNA-seq) de novo assembly containing 33,641 transcripts was generated,
annotated,andusedtointerrogatemassspectrometry(MS)dataderivedfrom1D-SDSPAGEandLC-MS/MSanalysisofESP.
Using the database generated from the 6 open reading frames deduced from the RNA-seq assembly and conventional
identificationprograms,209proteinswereidentifiedinESPincludinghomologuesofvitellogenins,retinol-andfattyacid-
bindingproteins,globins,andtheallergenV5/Tpx-1-relatedfamilyofproteins.Severalpotentialimmunomodulators,such
as macrophage migration inhibitory factor, cysteine protease inhibitors, galectins, C-type lectins, peroxiredoxin, and
glutathioneS-transferase,werealsoidentified.ComparativeanalysisofproteinannotationsbasedontheRNA-seqassembly
and proteomics revealed processes and proteins that may contribute to the functional specialization of ESP, including
proteins in
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