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Escamoles; Gene ontology; LC-MS/MS; Peptide de novo sequencing; qRT-PCR; Two-dimensional gel electrophoresis actin interacting protein 1; alpha tropomyosin; amino acid; calreticulin; complementary DNA; copper zinc superoxide dismutase; elongation factor 1alpha; elongation factor 1beta; elongation factor 2; enolase; ferritin; fk 506 binding protein 14; glyceraldehyde 3 phosphate dehydrogenase; heat shock protein; hemocyanin; myelin basic protein; myophilin; peroxiredoxin 1; phosphoglycerate kinase; profilin; protein; proteome; retinal dehydrogenase; selenium binding protein; stathmin; timbetasin; transferrin; triosephosphate isomerase; ubiquitin; unclassified drug; voltage dependent anion channel; insect protein; proteome; storage proteins, Insecta; amino acid sequence; ant; Article; biological phenomena and functions concerning the entire organism; down regulation; gene ontology; larva; Liometopum apiculatum; liquid chromatography-mass spectrometry; molecular weight; nonhuman; open reading frame; phylogenetic tree; phylogeny; priority journal; protein analysis; protein database; proteomics; two dimensional gel electrophoresis; animal; ant; chemistry; immunity; immunology; larva; liquid chromatography; procedures; tandem mass spectrometry; Amino Acid Sequence; Animals; Ants; Chromatography, Liquid; Electrophoresis, Gel, Two-Dimensional; Immunity; Insect Proteins; Larva; Proteome; Proteomics; Tandem Mass Spectrometry
amino acid, 65072-01-7; copper zinc superoxide dismutase, 149394-67-2; enolase, 9014-08-8; ferritin, 9007-73-2; glyceraldehyde 3 phosphate dehydrogenase, 9001-50-7; hemocyanin, 9013-72-3; phosphoglycerate kinase, 9001-83-6; profilin, 131383-86-3; protein, 67254-75-5; retinal dehydrogenase, 37250-99-0; stathmin, 126880-56-6; timbetasin, 77591-33-4, 77642-24-1, 1346423-89-9; transferrin, 82030-93-1; triosephosphate isomerase, 9023-78-3; ubiquitin, 60267-61-0; Insect Proteins; Proteome; storage proteins, Insecta
The proteome map of the escamolera ant (Liometopum apiculatum Mayr) larvae reveals immunogenic proteins and several hexamerin proteoforms
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. © 2018 Elsevier Inc.
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Comparative Biochemistry and Physiology - Part D: Genomics and Proteomics