Abstract

BackgroundThe black soldier fly (Hermetia illucens) has significant economic potential. The larvae can be used in financially viable waste management systems, as they are voracious feeders able to efficiently convert low-quality waste into valuable biomass. However, most studies on H. illucens in recent decades have focused on optimizing their breeding and bioconversion conditions, while information on their biology is limited.MethodsAbout 200 fifth instar well-fed larvae were sacrificed in this work. The liquid chromatography-tandem mass spectrometry and scanning electron microscopy were employed in this study to perform a proteomic and ultrastructural analysis of the peritrophic matrix (PM) of H. illucens larvae.ResultsA total of 565 proteins were identified in the PM samples of H. illucen, of which 177 proteins were predicted to contain signal peptides, bioinformatics analysis and manual curation determined 88 proteins may be associated with the PM, with functions in digestion, immunity, PM modulation, and others. The ultrastructure of the H. illucens larval PM observed by scanning electron microscopy shows a unique diamond-shaped chitin grid texture.ConclusionsIt is the first and most comprehensive proteomics research about the PM of H. illucens larvae to date. All the proteins identified in this work has been discussed in details, except several unnamed or uncharacterized proteins, which should not be ignored and need further study. A comparison of the ultrastructure between H. illucens larval PM and those of other insects as observed by SEM indicates that the PM displays diverse textures on an ultra-micro scale and we suscept a unique diamond-shaped chitin grid texture may help H. illucens larval to hold more food. This work deepens our understanding of the molecular architecture and ultrastructure of the H. illucens larval PM.

Highlights

  • The black soldier fly (Hermetia illucens) has significant economic potential

  • Proteomic analysis identified a total of 565 proteins from the peritrophic matrix (PM) samples of H. illucens (Table S1)

  • Since PM is a non-cellular structure, the proteins in the PM are mostly released from the microvilli of the columnar midgut cells into the extracellular space through apocrine secretion

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Summary

Introduction

The black soldier fly (Hermetia illucens) has significant economic potential. The larvae can be used in financially viable waste management systems, as they are voracious feeders able to efficiently convert low-quality waste into valuable biomass. Most studies on H. illucens in recent decades have focused on optimizing their breeding and bioconversion conditions, while information on their biology is limited. The peritrophic matrix (PM) is an acellular, semipermeable structure lining the digestive tracts of certain invertebrates to encase food particles, as first reported in lepidopteran larvae [1, 2]. The more common, Type II PM is a highly ordered, 1–3 layers, sleeve-like structure secreted by a group of cells at the junction of the foregut and midgut. The PM is thought to be homologous to mucus secretions in the mammalian digestive tract [6], acting as a physical barrier to protect the midgut from rough food particles and digestive enzymes [7]. To understand how the PM performs these essential functions, one must study its molecular architecture [11]

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