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dc.contributor.authorFrancischetti, Ivo M.B.-
dc.contributor.authorAssumpção, Teresa C.F.-
dc.contributor.authorMa, Dongying-
dc.contributor.authorLi, Yuan-
dc.contributor.authorVicente, Eliane C.-
dc.contributor.authorUieda, Wilson-
dc.contributor.authorRibeiro, José M.C.-
dc.date.accessioned2014-05-27T11:28:53Z-
dc.date.accessioned2016-10-25T18:46:55Z-
dc.date.available2014-05-27T11:28:53Z-
dc.date.available2016-10-25T18:46:55Z-
dc.date.issued2013-04-06-
dc.identifierhttp://dx.doi.org/10.1016/j.jprot.2013.01.009-
dc.identifier.citationJournal of Proteomics, v. 82, p. 288-319.-
dc.identifier.issn1874-3919-
dc.identifier.issn1876-7737-
dc.identifier.urihttp://hdl.handle.net/11449/75076-
dc.identifier.urihttp://acervodigital.unesp.br/handle/11449/75076-
dc.description.abstractVampire bats are notorious for being the sole mammals that strictly feed on fresh blood for their survival. While their saliva has been historically associated with anticoagulants, only one antihemostatic (plasminogen activator) has been molecularly and functionally characterized. Here, RNAs from both principal and accessory submaxillary (submandibular) salivary glands of Desmodus rotundus were extracted, and ~. 200. million reads were sequenced by Illumina. The principal gland was enriched with plasminogen activators with fibrinolytic properties, members of lipocalin and secretoglobin families, which bind prohemostatic prostaglandins, and endonucleases, which cleave neutrophil-derived procoagulant NETs. Anticoagulant (tissue factor pathway inhibitor, TFPI), vasodilators (PACAP and C-natriuretic peptide), and metalloproteases (ADAMTS-1) were also abundantly expressed. Members of the TSG-6 (anti-inflammatory), antigen 5/CRISP, and CCL28-like (antimicrobial) protein families were also sequenced. Apyrases (which remove platelet agonist ADP), phosphatases (which degrade procoagulant polyphosphates), and sphingomyelinase were found at lower transcriptional levels. Accessory glands were enriched with antimicrobials (lysozyme, defensin, lactotransferrin) and protease inhibitors (TIL-domain, cystatin, Kazal). Mucins, heme-oxygenase, and IgG chains were present in both glands. Proteome analysis by nano LC-MS/MS confirmed that several transcripts are expressed in the glands. The database presented herein is accessible online at http://exon.niaid.nih.gov/transcriptome/D_rotundus/Supplemental-web.xlsx. These results reveal that bat saliva emerges as a novel source of modulators of vascular biology. Biological significance: Vampire bat saliva emerges as a novel source of antihemostatics which modulate several aspects of vascular biology. © 2013.en
dc.format.extent288-319-
dc.language.isoeng-
dc.sourceScopus-
dc.subjectBat ecology-
dc.subjectDesmodus rotundus-
dc.subjectHematophagy-
dc.subjectIllumina-
dc.subjectProteome-
dc.subjectVampire bat-
dc.subjectADAMTS1 protein-
dc.subjectapyrase-
dc.subjectcystatin-
dc.subjectdefensin-
dc.subjectendonuclease-
dc.subjectheme oxygenase-
dc.subjecthypophysis adenylate cyclase activating polypeptide-
dc.subjectimmunoglobulin G-
dc.subjectlactoferrin-
dc.subjectlipocalin-
dc.subjectlysozyme-
dc.subjectmessenger RNA-
dc.subjectmucin-
dc.subjectnatriuretic peptide type C-
dc.subjectphosphatase-
dc.subjectplasminogen activator-
dc.subjectprostaglandin-
dc.subjectproteinase inhibitor-
dc.subjectproteome-
dc.subjectRNA-
dc.subjectsecretoglobin-
dc.subjectsphingomyelin phosphodiesterase-
dc.subjecttissue factor pathway inhibitor-
dc.subjecttranscriptome-
dc.subjectamino acid sequence-
dc.subjectanimal experiment-
dc.subjectbat-
dc.subjectfibrinolysis-
dc.subjectgene sequence-
dc.subjectliquid chromatography-
dc.subjectmass spectrometry-
dc.subjectnonhuman-
dc.subjectpriority journal-
dc.subjectprotein analysis-
dc.subjectprotein binding-
dc.subjectprotein expression-
dc.subjectrabies-
dc.subjectsubmandibular gland-
dc.titleThe Vampirome: Transcriptome and proteome analysis of the principal and accessory submaxillary glands of the vampire bat Desmodus rotundus, a vector of human rabiesen
dc.typeoutro-
dc.contributor.institutionNational Institutes of Health-
dc.contributor.institutionProjeto Morcegos Brasileiros and Unorp/Unipos-
dc.contributor.institutionUniversidade Estadual Paulista (UNESP)-
dc.description.affiliationLaboratory of Malaria and Vector Research National Institute of Allergy and Infectious Diseases National Institutes of Health, Rockville, MD 20892-
dc.description.affiliationEcoRefugius Projeto Morcegos Brasileiros and Unorp/Unipos, 15080-080, São Jose do Rio Preto, Sao Paulo State-
dc.description.affiliationDepartamento de Zoologia Instituto de Biociências Universidade Estadual Paulista (UNESP), 18618-970, Botucatu, São Paulo State-
dc.description.affiliationUnespDepartamento de Zoologia Instituto de Biociências Universidade Estadual Paulista (UNESP), 18618-970, Botucatu, São Paulo State-
dc.identifier.doi10.1016/j.jprot.2013.01.009-
dc.identifier.wosWOS:000319643300020-
dc.rights.accessRightsAcesso restrito-
dc.relation.ispartofJournal of Proteomics-
dc.identifier.scopus2-s2.0-84876353910-
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