Abstract

Mucins play a variety of roles; for example, in vertebrates, mucins lubricate epithelial surfaces and protect tissue from physical and biological damage, however, knowledge of insect mucins is limited. Here, we identified an eggshell-related mucin-like protein, NlESMuc, in the brown planthopper (BPH), Nilaparvata lugens. NlESMuc was specifically expressed in the follicular cells from the egg chambers of the ovarioles. RNA interference (RNAi) was used to perform functional analysis of NlESMuc. Adult female BPH with NlESMuc knockdown had significantly reduced fecundity, including more difficult oviposition, lower egg production, and eggs that could not hatch. Scanning electron microscopy showed that, in NlESMuc knocked-down BPH, the ultrastructure of the eggshells of fully developed oocytes was loose, and the cross-section showed many small droplets of about 0.1-μm diameter. Based on the results, it is concluded that NlESMuc is an eggshell-related protein and essential for normal oviposition. Our findings help to provide new targets for pesticide design and RNAi-based BPH control and will also provide new insights into insect eggshells and insect mucins.

Highlights

  • The brown planthopper (BPH), Nilaparvata lugens, is one of the most serious rice pests in Asia

  • The NlESMuc complementary DNA sequence was obtained from the N. lugens transcriptome database, cloned, and was verified by sequencing

  • We investigated the potential role of a mucin-like protein, NlESMuc, in BPH

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Summary

Introduction

The brown planthopper (BPH), Nilaparvata lugens, is one of the most serious rice pests in Asia. It feeds exclusively on rice, damaging rice directly by sucking plant sap and by transmitting two viruses, rice ragged stunt virus and rice grassy stunt virus. Mucins are a group of high–molecular weight glycoproteins that are abundant in vertebrate respiratory and digestive tract, and are classified as membrane-associated or secreted mucins (Wagner et al, 2018). Their molecular weights and protein sequences vary considerably, mucins are characterized by extended, tandem-repeated sequences rich in proline (Pro), serine (Ser), and threonine (Thr) and that are heavily substituted by O-linked oligosaccharides.

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