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The proteome map of the escamolera ant (Liometopum apiculatum Mayr) larvae reveals immunogenic proteins and several hexamerin proteoforms

dc.contributor.authorHuerta Ocampo, José Ángel
dc.contributor.authorGarcía Muñoz, María Soledad
dc.contributor.authorVelarde Salcedo, Aida Jimena
dc.contributor.authorHernández Domínguez, Eric Edmundo
dc.contributor.authorGonzález-Escobar, Jorge Luis
dc.contributor.authorBarrera Pacheco, Alberto
dc.contributor.authorGrajales Lagunes, Alicia
dc.contributor.authorBarba de la Rosa, Ana Paulina
dc.date.accessioned2019-09-12T17:36:28Z
dc.date.available2019-09-12T17:36:28Z
dc.date.issued2018
dc.identifier.citationJosé A. Huerta-Ocampo, María S. García-Muñoz, Aída J. Velarde-Salcedo, Eric E. Hernández-Domínguez, Jorge L. González-Escobar, Alberto Barrera-Pacheco, Alicia Grajales-Lagunes, Ana P. Barba de la Rosa, The proteome map of the escamolera ant (Liometopum apiculatum Mayr) larvae reveals immunogenic proteins and several hexamerin proteoforms, Comparative Biochemistry and Physiology Part D: Genomics and Proteomics, Volume 28, 2018, Pages 107-121.
dc.identifier.urihttp://hdl.handle.net/11627/5207
dc.description.abstract"The larvae of escamolera ant (Liometopum apiculatum Mayr) have been considered a delicacy since Pre-Hispanic times. The increased demand for this stew has led to massive collection of ant nests. Yet biological aspects of L. apiculatum larvae remain unknown, and mapping the proteome of this species is important for understanding its biological characteristics. Two-dimensional gel electrophoresis (2-DE) followed by liquid chromatography-tandem mass spectrometry (LC-MS/MS) analysis was used to characterize the larvae proteome profile. From 380 protein spots analyzed, 174 were identified by LC-MS/MS and homology search against the Hymenoptera subset of the NCBInr protein database using the Mascot search engine. Peptide de novo sequencing and homology-based alignment allowed the identification of 36 additional protein spots. Identified proteins were classified by cellular location, molecular function, and biological process according to the Gene Ontology annotation. Immunity- and defense-related proteins were identified including PPIases, FK506, PEBP, and chitinases. Several hexamerin proteoforms were identified and the cDNA of the most abundant protein detected in the 2-DE map was isolated and characterized. L. apiculatum hexamerin (LaHEX, GeneBank accession no. MH256667) contains an open reading frame of 2199?bp encoding a polypeptide of 733 amino acid residues with a calculated molecular mass of 82.41?kDa. LaHEX protein is more similar to HEX110 than HEX70 from Apis mellifera. Down-regulation of LaHEX was observed throughout ant development. This work represents the first proteome map as well as the first hexamerin characterized from L. apiculatum larvae."
dc.publisherElsevier
dc.rightsAttribution-NonCommercial-NoDerivatives 4.0 Internacional
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/
dc.subjectEscamoles
dc.subjectPeptide de novo sequencing
dc.subjectGene ontology
dc.subjectLC-MS/MS
dc.subjectqRT-PCR
dc.subjectTwo-dimensional gel electrophoresis
dc.subject.classificationBIOLOGÍA MOLECULAR
dc.titleThe proteome map of the escamolera ant (Liometopum apiculatum Mayr) larvae reveals immunogenic proteins and several hexamerin proteoforms
dc.typearticle
dc.identifier.doihttps://doi.org/10.1016/j.cbd.2018.07.004
dc.rights.accessAcceso Abierto


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Attribution-NonCommercial-NoDerivatives 4.0 Internacional
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