# Comprehensive Analysis of the UGT Gene Superfamily in Spodoptera frugiperda

**Authors:** Yang Liu, Minghui Guan, Kunliang Zou, Tonghan Wang, Haiyang Wang, Lu Sun, Bo Feng, Jiali Ding, Xiang Gao, Yongfu Wang, Degong Wu, Junli Du

PMC · DOI: 10.3390/insects16060601 · Insects · 2025-06-06

## TL;DR

This study identifies 48 UGT genes in the fall armyworm, revealing their roles in detoxification and metabolism, and suggests their potential for pest control strategies.

## Contribution

The discovery of 48 UGT genes in Spodoptera frugiperda and their expression patterns provides new insights into detoxification mechanisms in this pest.

## Key findings

- 48 UGT genes were identified in Spodoptera frugiperda, including 23 tandem duplication pairs.
- UGT genes show stage-specific and tissue-specific expression, suggesting roles in digestion and detoxification.
- Phylogenetic analysis indicates a closer evolutionary relationship between S. frugiperda and Spodoptera litura.

## Abstract

The fall armyworm is a major pest that causes significant damage to crops. To better understand how this insect copes with harmful substances, we investigated a group of genes known as UDP-glycosyltransferases (UGTs), which play key roles in toxin removal. Through computational analysis, we identified 48 UGT genes in the fall armyworm, some of which appear to have expanded through gene duplication. These genes predominantly encode proteins characterized by α-helical secondary structures. We also observed variations in gene organization and protein sequences. Comparative analysis with other insects revealed that the fall armyworm is closely related to Spodoptera litura. Several UGT genes showed stage-specific and tissue-specific expression patterns during larval development, indicating their involvement in the digestion, detoxification, and transport of important molecules. This study enhances our understanding of the fall armyworm’s survival mechanisms and could contribute to developing new strategies for pest management.

UDP-glycosyltransferases (UGTs) are widely distributed enzymes in living organisms that catalyze the transfer of glycosyl groups from donor molecules to acceptor molecules’ glycoside ligands. These enzymes are pivotal for detoxifying and eliminating both endogenous and exogenous toxic substances in insects. In this study, bioinformatics methods were used to analyze the UGT gene superfamily in the fall armyworm (Spodoptera frugiperda), resulting in the identification of 48 UGT genes located across 10 chromosomes, including 23 tandem duplication pairs. The predicted SfUGT proteins mainly exhibit α-helical secondary structures. Intron numbers varied significantly, with high diversity observed in amino acid sequences. Phylogenetic analysis grouped UGT genes from three insect species into three distinct subfamilies, revealing a closer evolutionary relationship between S. frugiperda and Spodoptera litura, supported by a greater number of orthologous genes. Expression profiling showed that SfUGT16 and SfUGT21 are highly expressed in the first and fourth larval instars, respectively; SfUGT16 is predominantly expressed in the Malpighian tubules and midgut, implying roles in digestion, metabolism, and detoxification. Meanwhile, SfUGT21, SfUGT30, and SfUGT48 exhibited elevated expression in the hemolymph, suggesting functions in metabolism and transport, whereas SfUGT40 showed high expression in both the midgut and hemolymph, indicating involvement in detoxification and metabolic processes. These findings provide a foundation for further exploration of the biological functions of the UGT gene family.

## Linked entities

- **Genes:** SLC35A2 (solute carrier family 35 member A2) [NCBI Gene 7355]
- **Proteins:** SLC35A2 (solute carrier family 35 member A2)
- **Species:** Spodoptera frugiperda (taxon 7108), Spodoptera litura (taxon 69820)

## Full-text entities

- **Species:** Spodoptera litura (species) [taxon 69820], Spodoptera frugiperda (fall armyworm, species) [taxon 7108]

## Full text

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## Figures

7 figures with captions in the complete paper: https://tomesphere.com/paper/PMC12193703/full.md

## References

51 references — full list in the complete paper: https://tomesphere.com/paper/PMC12193703/full.md

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Source: https://tomesphere.com/paper/PMC12193703