Dataset Information

The mitochondrial genome of a social wasp, Vespa simillima simillima (Hymenoptera: Vespidae).

ABSTRACT: We analyzed the complete mitochondrial genome of a social wasp, Vespa simillima simillima from South Korea prior to a systematic study on Korean Vespidae. The mitogenome is 16,740 bp in length, includes 13 protein-coding genes (PCGs), 22 tRNAs, 2 rRNAs, and a 228 bp short A + T-rich region. The overall base composition is 82.0% AT and 18.0% GC. The maximum-likelihood analysis suggested that V. s. simillima is closely related to V. bicolor, another species of Vespidae.

SUBMITTER: Choi MB

PROVIDER: S-EPMC7748423 | biostudies-literature | 2019 Dec

REPOSITORIES: biostudies-literature

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The mitochondrial genome of a social wasp, Vespa simillima simillima (Hymenoptera: Vespidae).

Choi Moon-Bo MB Ha Young-Ho YH Kim Il-Kown IK Oh Seung Hwan SH Kim Chang-Jun CJ

Mitochondrial DNA. Part B, Resources 20191213 1

We analyzed the complete mitochondrial genome of a social wasp, Vespa simillima simillima from South Korea prior to a systematic study on Korean Vespidae. The mitogenome is 16,740 bp in length, includes 13 protein-coding genes (PCGs), 22 tRNAs, 2 rRNAs, and a 228 bp short A + T-rich region. The overall base composition is 82.0% AT and 18.0% GC. The maximum-likelihood analysis suggested that V. s. simillima is closely related to V. bicolor, another specie ...[more]

PMID: 33366515

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Project description:Background Between 9.3 and 28.5% of world population are estimated to be allergic to the protein components of Hymenoptera venom and among them, the hyaluronidase (HYAL) is one of the most important, although the nature of its IgE binding epitopes is unknown. Methods Enzyme was purified from P. paulista venom by cation exchange chromatography in AKTA-FPLC system with a Hiprep CM FF column. Fractions with HYAL activity were pooled, lyophilized, dialyzed against distilled water in presence of protease inhibitor (PMSF) and subjected to SDS-PAGE 15%. The only protein bands visualized were submitted to tryptic digestion and to MALDI-ToF/ToF mass spectrometry. Digested peptides produced were compared with partial/complete protein sequences from Data Bank including with the HYAL (Q9U6V9) of Polistes annularis venom used as model. Western blotting was performed with Pp-HYAL-specific antibody to test the identity of pure protein. Results All analysis performed identified the pure protein as an HYAL present in P.paulista venom, which also had its cDNA sequence (GI:302201582) cloned and determined in previous studies, being its high similarity with the Polistes annularis enzyme already confirmed. The mature allergenic protein has 338 amino acids and a molecular weight of 39 KDa. The same allergen is known in other insects, venoms and immunological cross reactivity may sometimes be observed among closely related species. Here, the immunoblotting assay revealed that the Pp-HYAL-specific antibody used recognized the correspondent protein in the purified fraction and in the crude venom of P. paulista, but not in the Apis mellifera and Solenopsis invicta venoms. Conclusions The methodology used was able to purify the allergen, which is a key step in the characterization of its binding epitopes. Such knowledge has direct implications in accuracy of diagnostic procedures and strategies for specific immunotherapy of allergic patients to the venom of this insect. Funding: Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP).

Dataset Information

The mitochondrial genome of a social wasp, Vespa simillima simillima (Hymenoptera: Vespidae).

Publications

The mitochondrial genome of a social wasp, <i>Vespa simillima simillima</i> (Hymenoptera: Vespidae).

Similar Datasets

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