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. 2022 Nov 1:13:1014225.
doi: 10.3389/fgene.2022.1014225. eCollection 2022.

Comprehensive analysis of lysine lactylation in Frankliniella occidentalis

Dong An  1 , Liyun Song  1 , Ying Li  1 , Lili Shen  1 , Pu Miao  2 , Yujie Wang  2 , Dongyang Liu  3 , Lianqiang Jiang  3 , Fenglong Wang  1 , Jinguang Yang  1
Affiliations

Comprehensive analysis of lysine lactylation in Frankliniella occidentalis

Dong An et al. Front Genet. .

Abstract

Western flower thrips (Frankliniella occidentalis) are among the most important pests globally that transmit destructive plant viruses and infest multiple commercial crops. Lysine lactylation (Klac) is a recently discovered novel post-translational modification (PTM). We used liquid chromatography-mass spectrometry to identify the global lactylated proteome of F. occidentalis, and further enriched the identified lactylated proteins using Kyoto Encyclopedia of Genes and Genomes (KEGG) and Gene Ontology (GO). In the present study, we identified 1,458 Klac sites in 469 proteins from F. occidentalis. Bioinformatics analysis showed that Klac was widely distributed in F. occidentalis proteins, and these Klac modified proteins participated in multiple biological processes. GO and KEGG enrichment analysis revealed that Klac proteins were significantly enriched in multiple cellular compartments and metabolic pathways, such as the ribosome and carbon metabolism pathways. Two Klac proteins were found to be involved in the regulation of the TSWV (Tomato spotted wilt virus) transmission in F. occidentalis. This study provides a systematic report and a rich dataset of lactylation in F. occidentalis proteome for potential studies on the Klac protein of this notorious pest.

Keywords: carbon metabolism; lysine lactylation; post-translational modification; ribosome; western flower thrips (Frankliniella occidentalis).

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Conflict of interest statement

Authors PM and YW were employed by Luoyang City Company of Henan Province Tobacco Company. Authors DL and LJ were employed by Liangshan State Company of Sichuan Province Tobacco Company. The remaining authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest.

Figures

FIGURE 1
FIGURE 1
Protein lysine lactylation assay of F. occidentalis. (A) Technical route of Klac assay. (B) Mass error range for all identified Klac peptides (The error distribution for Klac peptides is close to 0, and the vast majority are less than 0.02 Da). (C) Klac peptide length range (Most of the peptides are distributed in 7–20 amino acids, which conform to the general rules based on trypsin enzymatic hydrolysis and HCD fragmentation). (D) Number of Klac sites in the protein of F. occidentalis (Most of the Klac proteins have less than three modification sites).
FIGURE 2
FIGURE 2
Analysis of related properties of Klac peptides in F. occidentalis. (A) Analysis of specific amino acid enrichment ± 10 flanking the Klac site (position 0). Lactylation motifs were constructed using the MOMO program. The central K (position 0) represents lactated lysine. Letters of different heights represent the frequency of occurrence of a particular amino acid. (B) The heat map represents the degree of enrichment of amino acids around the Klac site. Red indicates high frequency and green means low frequency. (C) Identification of the frequency of occurrence of different secondary structures (α-helix, β-strand and coil structures) in the resulting Klac proteins. (D) Surface accessibility of predicted Klac sites.
FIGURE 3
FIGURE 3
Pie chart showing Gene Ontology analysis of F. occidentalis proteins with Klac modifications. (A) Klac proteins classified according to biological process. (B) Klac proteins classified according to cellular component. (C) Klac proteins classified according to molecular function.
FIGURE 4
FIGURE 4
Systematic enrichment analysis of Klac proteins in F. occidentalis. (A) Klac proteins enrichment analysis based on the KEGG pathway. (B) Protein domain-based Klac proteins enrichment analysis.
FIGURE 5
FIGURE 5
KEGG pathway enrichment analysis of proteins with Klac modifications. (A) Klac proteins were involved in the ribosomes. (B) Klac proteins were involved in carbon metabolism. Proteins with Klac modifications are highlighted in red.
FIGURE 6
FIGURE 6
Protein-protein interaction (PPI) network analysis of Klac proteins in F. occidentalis. The interaction network of STRING was visualized in Cytoscape (version 3.3.0). The size of the nodes corresponds directly to the number of Klac sites per protein. This group of proteins was highly associated with ribosomes.
FIGURE 7
FIGURE 7
Schematic representation of the three-dimensional structures of two proteins in F. occidentalis involved in the transmission of TSWV. (A) EndoCP-GN. (B) Cyclophilin. Structure predicted by I-TASSER. Identified Klac sites were highlighted in red.
See this image and copyright information in PMC

References

    1. Aweya J. J., Zhuang K., Liu Y., Fan J., Yao D., Wang F., et al. (2022). The ARM repeat domain of hemocyanin interacts with MKK4 to modulate antimicrobial peptides expression. iScience 25, 103958. 10.1016/j.isci.2022.103958 - DOI - PMC - PubMed
    1. Badillo-Vargas I. E., Chen Y., Martin K. M., Rotenberg D., Whitfield A. E. (2019). Discovery of novel thrips vector proteins that bind to the viral attachment protein of the plant bunyavirus tomato spotted wilt virus. J. Virol. 93, 21. 10.1128/JVI.00699-19 - DOI - PMC - PubMed
    1. Brooks G. A. (2002). Lactate shuttles in nature. Biochem. Soc. Trans. 30, 258–264. 10.1042/bst0300258 - DOI - PubMed
    1. Burmester T. (2002). Origin and evolution of arthropod hemocyanins and related proteins. J. Comp. Physiol. B 172, 95–107. 10.1007/s00360-001-0247-7 - DOI - PubMed
    1. Chatzivassiliou E. K. (2008). Management of the spread of tomato spotted wilt virus in tobacco crops with insecticides based on estimates of thrips infestation and virus incidence. Plant Dis. 92, 1012–1020. 10.1094/PDIS-92-7-1012 - DOI - PubMed

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