Molecular Characterization and Phylogenetic Analysis of Flightin Gene in Vespa basalis (Hymenoptera, Vespidae)

TL;DR

This paper studies the flightin gene in a dangerous hornet species, revealing its molecular structure and evolutionary relationships.

Contribution

The paper provides the first molecular characterization of the flightin gene in Vespa basalis and its phylogenetic placement.

Findings

The flightin gene in Vespa basalis encodes a 150-amino acid protein with a molecular weight of 18.05 kDa and an isoelectric point of 5.84.

Phylogenetic analysis shows Vespa basalis is closely related to Vespa mandarinia, despite contrasting mitochondrial sequence data.

The flightin protein lacks transmembrane topology and contains four functional site patterns.

Abstract

We conducted a study on flightin, a vital protein found in insect flight muscles, with a specific focus on the social wasp Vespa basalis, which is a dangerous hornet species. Using sequence analysis techniques, we successfully obtained an 1189 bp cDNA sequence encoding the flightin protein consisting of 150 amino acids. According to our analysis, the molecular weight and isoelectric point of the amino acid sequence are 18.05 kDa and 5.84, respectively. The protein lacks a transmembrane topology structure, and we identified four patterns of functional sites. Conducting phylogenetic analysis on 38 species, including 8 Vespidae species, revealed a close evolutionary relationship between Vespa basalis and Vespa mandarinia. These findings warrant further investigation, especially considering the contrasting information obtained from the analysis of mitochondrial sequences.

Flight is a complex physiological process requiring precise coordination of muscular contraction. A key protein in insect flight is flightin, which plays an integral role in the flight muscles. This research sought to evaluate the flight competence of the social wasp V. basalis by characterizing the molecular components involved. Our study focused on Vespa basalis, one of the most dangerous hornet species, utilizing PCR to obtain a partial cDNA sequence of the flightin protein. We then employed phylogenetic and sequence analysis to gain insights into this protein in flight-related adaptations. The cDNA has an 1189-base pair sequence including an open reading frame (453 bp) encoding 150 amino acids. Analyzing the deduced amino acid sequence using an online tool revealed a molecular weight of 18.05 kDa, an isoelectric point of 5.84, four functional site patterns, and no transmembrane topology. We constructed a phylogenetic tree of flightin based on 38 species. Our analysis indicated that V. basalis is most closely related to V. mandarinia; this alignment is consistent with their similar aggressive behavior, but their evolutionary relationship, based on mitochondrial sequences, presents a contrast. These initial findings on the flightin gene in V. basalis lay the groundwork for future functional studies to elucidate its specific role in flight adaptations and explore its potential as a target for pest management strategies.

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