Protein structural differences in Cytochrome c oxidase subunit 1 of two Heterogynis species as a new approach for species delimitation

Marija Vidović1*, Vladislava Galović2

1Institute of Molecular Genetics and Genetic Engineering, Laboratory for Plant Molecular Biology, University of Belgrade, Vojvode Stepe 444a, Belgrade, Serbia

2University of Novi Sad, Institute of Lowland Forestry and Environment (ILFE), Antona Čehova 13, 21000 Novi Sad, Serbia

mvidovic [at] imgge.bg.ac.rs

Abstract

Insects are the most diverse group in the animal kingdom, accounting for about two-thirds of all animals. Cytochrome c oxidase subunit 1 (COI) is the most commonly used marker gene for animal species delineation. However, the accuracy of this approach crucially depends on the degree of overlap between the intra- and interspecific variations.

Recently, we have identified a new species, Heterogynis serbica sp. n. (Lepidoptera: Zygaenoidea, Heterogynidae) found on the Mt. Kopaonik, Republic of Serbia, Balkan Peninsula. This was done by integrating taxonomic approach using morpho-anatomical characteristics by comparative scanning electron microscopy (SEM), linear wing morphometry and COI-based DNA barcoding [1]. In this study, we have used a set of bioinformatics tools available online, to determine the differences in secondary and tertiary structure of the COI proteins from H. serbica sp. n. and H. zikici. We also compared the amino acid distribution and COI motif profiles between the two species. Our results provide strong evidence that protein structure of COI can help with COI-based DNA barcoding for taxon-specific purposes of species identification and delimitation studies. Millions of COI DNA sequences deposited in the public domain (which are still growing) carry huge potential for a comprehensive assessment of genetic variation in COI among insects by using here described analysis.

Keywords: cytochrome c oxidase subunit 1, Heterogynidae, Heterogynis sp., Lepidoptera, conserved protein motif, protein sequence, secondary and tertiary protein structure, transmembrane helices.

Acknowledgements: This work was funded by the Ministry of Science, Technological Development and Innovation, Republic of Serbia (Contract No. 451-03-47/2023-01/ 200042; 451-03-47/2023-01/200197).

Comments are closed.