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Special Issue "Molecular Ecology, Physiology and Biochemistry of Insects"

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Biology".

Deadline for manuscript submissions: 30 November 2019

Special Issue Editor

Guest Editor
Prof. Dr. Klaus H. Hoffmann

Animal Ecology I, University of Bayreuth, 95440 Bayreuth, Germany
Website | E-Mail
Interests: insect biochemistry and physiology; molecular ecology; invertebrate development and reproduction; invertebrate hormones; neuropeptides

Special Issue Information

Dear Colleagues,

Of all the zoological classes, insects are the most numerous in species and the most varied in structure. Estimates of the number of species vary from 1 to 10 million, and 1018 individuals are estimated to be alive at any given moment. Insects are relatively ancient and have survived more or less unchanged in their basic winged form during the last 300 million years. Due to their adaptability in behavior, physiology, and biochemistry to changing environmental conditions, insects have successfully colonized habitats stretching from arid deserts to the Arctic and Antarctic and from freshwater brooks to hot springs and saline.

Knowledge of the physiology and biochemistry of insects developed extensively at the end of the 20th century. The reasons for this increased interest in insect physiology and biochemistry were that insects can be useful as model systems for experimental studies of principles, but also as economic models. Mechanisms of environmental adaptation in growth and development, energy metabolism, or respiration to temperature, oxygen tension, food supply or salt concentrations were the focus of interest. It was the time of “Physiological Ecology”.

About 30 years later, the omics era gives us the opportunity to gain deeper insight into the different aspects of insect physiology and environmental adaptation, for example, by silencing or overexpressing candidate genes of interest. A major challenge in current entomology is to integrate different levels of organization, from cellular mechanisms to functions in ecosystems. The rapid development of molecular techniques for studying physiological functions of genes will revolutionize entomology not only of so-called model organisms like Drosophila, but in general. When we understand how physiological processes are regulated and at what time, we will be able to manipulate them, thereby providing new attractive opportunities for practical applications, for example, in an ecologically friendly insect pest control.

We invite you to contribute original research articles and critical reviews on both basic and applied approaches in insect molecular biology. Articles on the molecular mechanisms of insect–plant interactions, and systems of insect communication in general, are also welcome.

Prof. Dr. Klaus H. Hoffmann
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All papers will be peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. International Journal of Molecular Sciences is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 1800 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • Insect development and reproduction
  • Molecular endocrinology/neuropeptides
  • Insect immunity
  • Photoperiodism
  • Cold hardiness
  • Global climate change
  • Insect aging
  • Insect–plant interactions
  • Molecular interactions of insects with microorganisms
  • Chemical communication
  • Biochemistry of insect venoms
  • Insect genomics and proteomics
  • Genetic engineering
  • Molecular evolution/population genetics
  • Insect biotechnology

Published Papers (4 papers)

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Research

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Open AccessArticle
Molecular Characterization of Ca2+/Calmodulin-Dependent Protein Kinase II Isoforms in Three Rice Planthoppers—Nilaparvata lugens, Laodelphax striatellus, and Sogatella furcifera
Int. J. Mol. Sci. 2019, 20(12), 3014; https://doi.org/10.3390/ijms20123014
Received: 23 May 2019 / Revised: 13 June 2019 / Accepted: 18 June 2019 / Published: 20 June 2019
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Abstract
This study reports the identification of splice variants for the calcium/calmodulin-dependent protein kinase II (CaMKII) gene from Nilaparvata lugens, Laodelphax striatellus, and Sogatella furcifera. CaMKII is a multifunctional serine/threonine protein kinase that transduces Ca2+ signals in cells [...] Read more.
This study reports the identification of splice variants for the calcium/calmodulin-dependent protein kinase II (CaMKII) gene from Nilaparvata lugens, Laodelphax striatellus, and Sogatella furcifera. CaMKII is a multifunctional serine/threonine protein kinase that transduces Ca2+ signals in cells to control a range of cellular processes in the nervous system and muscular tissue. Sequence analysis showed that CaMKII was 99.0% identical at the amino acid level among three rice planthoppers, with the exception of a variable region located in the association domain. Four kinds of 20–81 amino acid “inserts” were found in the variable region. The phylogenetic tree of the deduced amino acid sequences showed that the NlCaMKII isoforms were more closely related to the LsCaMKII isoforms and were slightly distinct from SfCaMKII. CaMKII-E was the dominant type among the five main isoforms. CaMKII genes were constitutively expressed in various nymphal and adult stages and in tested tissues with the predominant transcription occurring in the head. There was no major tissue specificity of isoform expression, but the expression pattern and relative abundance of isoforms varied when compared with the RT-PCR between tissues. In addition, RNAi in N. lugens with dsRNA at a concentration of 200 ng nymph−1 induced a mortality of 77.7% on the 10th day and a reduction in the mRNA expression level of 67.2%. Unlike the holometabolous insect Helicoverpa armigera, the knockdown of NlCaMKII did not suppress the expression of 20E response genes, such as ECR, USP1, and HR3, in N. lugens. These results indicate that the role of CaMKII in hemimetabolous insects may be different from that in holometabolous insects. Full article
(This article belongs to the Special Issue Molecular Ecology, Physiology and Biochemistry of Insects)
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Open AccessArticle
The Direct Interaction between E93 and Kr-h1 Mediated Their Antagonistic Effect on Ovary Development of the Brown Planthopper
Int. J. Mol. Sci. 2019, 20(10), 2431; https://doi.org/10.3390/ijms20102431
Received: 3 April 2019 / Revised: 13 May 2019 / Accepted: 14 May 2019 / Published: 16 May 2019
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Abstract
The juvenile hormone (JH) signalling and ecdysone signalling pathways are crucial endocrine signalling pathways that orchestrate the metamorphosis of insects. The metamorphic process, the morphological change from the immature to adult forms, is orchestrated by the dramatic reduction of JH and downstream transcription [...] Read more.
The juvenile hormone (JH) signalling and ecdysone signalling pathways are crucial endocrine signalling pathways that orchestrate the metamorphosis of insects. The metamorphic process, the morphological change from the immature to adult forms, is orchestrated by the dramatic reduction of JH and downstream transcription factors. The Krüppel-homologue 1 (Kr-h1), a downstream transcription factor of the JH signalling pathway, represses E93 expression with an anti-metamorphic effect. However, the biochemical interaction between Kr-h1 and E93 and how the interaction regulates ovary development, a sensitive readout for endocrine regulation, remain unknown. In brown planthopper, Nilaparvata lugens, we found that the downregulation of Kr-h1 partially recovered the deteriorating effect of E93 knock-down on metamorphosis. Dual knock down of E93 and Kr-h1 increased ovary development and the number of eggs laid when compared to the effects of the knock down of E93 alone, indicating that the knock down of Kr-h1 partially recovered the deteriorating effect of the E93 knock-down on ovary development. In summary, our results indicated that E93 and Kr-h1 have antagonistic effects on regulating metamorphosis and ovary development. We tested the biochemical interaction between these two proteins and found that these molecules interact directly. Kr-h1 V and E93 II undergo strong and specific interactions, indicating that the potential interacting domain may be located in these two regions. We inferred that the nuclear receptor interaction motif (NR-box) and helix-turn-helix DNA binding motifs of the pipsqueak family (RHF1) are candidate domains responsible for the protein–protein interaction between E93 and Kr-h1. Moreover, the HA-tagged E93 and FLAG-tagged Kr-h1 were co-localized in the nucleus, and the expression of E93 was increased when Kr-h1 was downregulated, supporting that these two proteins may interact antagonistically. JH and ecdysone signalling are critical for the control of ovary development and pest populations. Our result is important for understanding the interactions between E93 and related proteins, which makes it possible to identify potential targets and develop new pesticides for pest management. Full article
(This article belongs to the Special Issue Molecular Ecology, Physiology and Biochemistry of Insects)
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Open AccessArticle
P-element Somatic Inhibitor Protein Binding a Target Sequence in dsx Pre-mRNA Conserved in Bombyx mori and Spodoptera litura
Int. J. Mol. Sci. 2019, 20(9), 2361; https://doi.org/10.3390/ijms20092361
Received: 15 April 2019 / Revised: 10 May 2019 / Accepted: 10 May 2019 / Published: 13 May 2019
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Abstract
Bombyx mori doublesex (Bmdsx) functions as a double-switch gene in the final step of the sex-determination cascade in the silkworm Bombyx mori. The P-element somatic inhibitor (PSI) protein in B. mori interacts with Bmdsx pre-mRNA in CE1 as an exonic [...] Read more.
Bombyx mori doublesex (Bmdsx) functions as a double-switch gene in the final step of the sex-determination cascade in the silkworm Bombyx mori. The P-element somatic inhibitor (PSI) protein in B. mori interacts with Bmdsx pre-mRNA in CE1 as an exonic splicing silencer to promote male-specific splicing of Bmdsx. However, the character of the interaction between BmPSI and Bmdsx pre-mRNA remains unclear. Electrophoretic mobility shift assay (EMSA) results showed that the four KH_1 motifs in BmPSI are all essential for the binding, especially the former two KH_1 motifs. Three active sites (I116, L127, and IGGI) in the KH_1 motif were found to be necessary for the binding through EMSA, circular dichroism (CD) spectroscopy, and isothermal titration calorimetry (ITC). The PSI homologous protein in S. litura (SlPSI) was purified and the binding of SlPSI and CE1 was verified. Compared with BmPSI, the mutant SlPSI proteins of I116 and IGGI lost their ability to bind to CE1. In conclusion, the binding of PSI and dsx pre-mRNA are generally conserved in both B. mori and S. litura. These findings provide clues for sex determination in Lepidoptera. Full article
(This article belongs to the Special Issue Molecular Ecology, Physiology and Biochemistry of Insects)
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Review

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Open AccessReview
Insect ATP-Binding Cassette (ABC) Transporters: Roles in Xenobiotic Detoxification and Bt Insecticidal Activity
Int. J. Mol. Sci. 2019, 20(11), 2829; https://doi.org/10.3390/ijms20112829
Received: 22 May 2019 / Revised: 6 June 2019 / Accepted: 6 June 2019 / Published: 10 June 2019
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Abstract
ATP-binding cassette (ABC) transporters, a large class of transmembrane proteins, are widely found in organisms and play an important role in the transport of xenobiotics. Insect ABC transporters are involved in insecticide detoxification and Bacillus thuringiensis (Bt) toxin perforation. The complete ABC transporter [...] Read more.
ATP-binding cassette (ABC) transporters, a large class of transmembrane proteins, are widely found in organisms and play an important role in the transport of xenobiotics. Insect ABC transporters are involved in insecticide detoxification and Bacillus thuringiensis (Bt) toxin perforation. The complete ABC transporter is composed of two hydrophobic transmembrane domains (TMDs) and two nucleotide binding domains (NBDs). Conformational changes that are needed for their action are mediated by ATP hydrolysis. According to the similarity among their sequences and organization of conserved ATP-binding cassette domains, insect ABC transporters have been divided into eight subfamilies (ABCA–ABCH). This review describes the functions and mechanisms of ABC transporters in insecticide detoxification, plant toxic secondary metabolites transport and insecticidal activity of Bt toxin. With improved understanding of the role and mechanisms of ABC transporter in resistance to insecticides and Bt toxins, we can identify valuable target sites for developing new strategies to control pests and manage resistance and achieve green pest control. Full article
(This article belongs to the Special Issue Molecular Ecology, Physiology and Biochemistry of Insects)
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Int. J. Mol. Sci. EISSN 1422-0067 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
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