Water bound in elytra of the Weevil Liparus glabrirostris (Küster, 1849) by NMR and sorption isotherm (Coleoptera: Curculionidae)

Scanning electron microscopy micrograms of the elytra of Liparus glabrirostris showed a different dorsal and ventral surface and a multilayered inner structure. Hydration kinetics, sorption isotherm, and proton free induction decays are measured for hydrated elytra of the weevil species Liparus glabrirostris (Coleoptera: Curculionidae) in the atmosphere with controlled humidity. Very tightly bound water fraction with the mass Δ m/$m_0$ = 0.037 ± 0.004, and very short hydration time, tightly bound water Δ m/$m_0$ = 0.034 ± 0.009, and hydration time $t_1^{h}$ = (3.31 ± 0.93) h, and finally loosely bound water fraction with $t_2^{h}$ = (25.5 ± 7.8) h were distinguished. The sorption isotherm is sigmoidal in form, with the mass of water saturating primary water binding sites equal of Δ M/$m_0$ = 0.036. The proton free induction decays show the presence of solid signal (well fitted by a Gaussian function) from elytra ($T_{2G}$* ≈ 18 μs), the immobilized water fraction ($T_{2L_1}$* ≈ 120 μs) and mobile water pool ($T_{2 L_2}$* ≈ 300 μs). The hydration dependence of the water bound in elytra of L. glabrirostris, L/S is linear showing the absence of water-soluble solid fraction and negligible content of water pool "sealed" in pores of the structure

The species status of the Otiorhynchus clavipes (Bonsdorff, 1785) species group (Coleoptera: Curculionidae) : an integrative approach using molecular, morphological, ecological, and biogeographical data

The species of the Otiorhynchus clavipes (Bonsdorff, 1785) group (Coleoptera: Curculionidae) treated here, are characterized by their unusually high phenotypical variation, which often caused taxonomic problems and controversies. Molecular markers COI and EF1-$\alpha$, karyological analysis, as well as morphological, biogeographical and ecological data are used to study weevils collected in the Alps, Carpathians, Sudetes and different areas of Germany. In the investigated populations of the flightless species O. fagi Gyllenhal, 1834 and O. clavipes, we detected an interspecific genetic distance of 11.3-15.8% (COI) and 3.1-3.7% (EF1-$\alpha$) depending on geographical distance. The phylogenetic trees indicate that both species are monophyletic and that they were correctly delimited from each other. Both species have also separate geographical ranges in Central Europe. Male specimens differ in the morphology of the aedeagus and the last abdominal sternite. Our study supports the legitimacy of species delimitation of O. fagi and O. clavipes as separate species, which can be treated as stable taxonomic hypotheses. The determination of the species status required the re-examination of spe cies ranges and allowed together with data on biology and altitudinal preferences a better biogeographical and ecological characterization of the species

Isolation, identification, and bioinformatic analysis of antibacterial proteins and peptides from immunized hemolymph of red palm weevil Rhynchophorus ferrugineus

Red palm weevil (Rhynchophorus ferrugineus Olivier, 1791, Coleoptera: Curculionidae) is a destructive pest of palms, rapidly extending its native geographical range and causing large economic losses worldwide. The present work describes isolation, identification, and bioinformatic analysis of antibacterial proteins and peptides from the immunized hemolymph of this beetle. In total, 17 different bactericidal or bacteriostatic compounds were isolated via a series of high-pressure liquid chromatography steps, and their partial amino acid sequences were determined by N-terminal sequencing or by mass spectrometry. The bioinformatic analysis of the results facilitated identification and description of corresponding nucleotide coding sequences for each peptide and protein, based on the recently published R. ferrugineus transcriptome database. The identified compounds are represented by several well-known bactericidal factors: two peptides similar to defensins, one cecropin-A1-like peptide, and one attacin-B-like protein. Interestingly, we have also identified some unexpected compounds comprising five isoforms of pheromone-binding proteins as well as seven isoforms of odorant-binding proteins. The particular role of these factors in insect response to bacterial infection needs further investigation