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Peter L Davies - One of the best experts on this subject based on the ideXlab platform.

  • Characterization and cloning of a Tenebrio molitor hemolymph protein with sequence similarity to Insect odorant-binding Proteins.
    Insect biochemistry and molecular biology, 2001
    Co-Authors: Laurie A Graham, Yihcherng Liou, John G. Baust, Wei Tang, T S Reid, Peter L Davies
    Abstract:

    The yellow mealworm beetle, Tenebrio molitor, produces a number of moderately abundant low molecular weight hemolymph Proteins ( approximately 12 kDa) which behave in a similar manner during purification and share antigenic epitopes. The cDNA sequence of the major component (THP12) was determined and the deduced protein sequence was found to be similar to those of Insect odorant-binding Proteins. Southern blot analysis suggests that at least some of the diversity in this family of Proteins is encoded at the gene level. Both northern and western blot analysis indicate that THP12 is present in a variety of developmental stages and both sexes. THP12 was originally classified as an antifreeze protein, but the lack of antifreeze activity in the recombinant protein, as well as the clear separation of the antifreeze activity from THP12 following HPLC purification, has ruled out this function. The abundance of THP12, the similarity of THP12 to Insect odorant-binding Proteins, and the presence of hydrophobic cavities inside the protein (Rothemund et al., A new class of hexahelical Insect Proteins revealed as putative carriers of small hydrophobic ligands. Structure, 7 (1999) 1325-1332.) suggest that THP12 may function to carry non-water soluble compounds in the hemolymph. THP12 is also similar, particularly in structurally important regions, to other Insect Proteins from non-sensory tissues, suggesting the existence of a large family of carrier Proteins which may perform diverse functions throughout the Insect.

  • characterization and cloning of a tenebrio molitor hemolymph protein with sequence similarity to Insect odorant binding Proteins
    Insect Biochemistry and Molecular Biology, 2001
    Co-Authors: Laurie A Graham, Scott T Reid, Yihcherng Liou, John G. Baust, Wei Tang, Peter L Davies
    Abstract:

    Abstract The yellow mealworm beetle, Tenebrio molitor , produces a number of moderately abundant low molecular weight hemolymph Proteins (∼12 kDa) which behave in a similar manner during purification and share antigenic epitopes. The cDNA sequence of the major component (THP12) was determined and the deduced protein sequence was found to be similar to those of Insect odorant-binding Proteins. Southern blot analysis suggests that at least some of the diversity in this family of Proteins is encoded at the gene level. Both northern and western blot analysis indicate that THP12 is present in a variety of developmental stages and both sexes. THP12 was originally classified as an antifreeze protein, but the lack of antifreeze activity in the recombinant protein, as well as the clear separation of the antifreeze activity from THP12 following HPLC purification, has ruled out this function. The abundance of THP12, the similarity of THP12 to Insect odorant-binding Proteins, and the presence of hydrophobic cavities inside the protein (Rothemund et al., A new class of hexahelical Insect Proteins revealed as putative carriers of small hydrophobic ligands. Structure, 7 (1999) 1325–1332.) suggest that THP12 may function to carry non-water soluble compounds in the hemolymph. THP12 is also similar, particularly in structurally important regions, to other Insect Proteins from non-sensory tissues, suggesting the existence of a large family of carrier Proteins which may perform diverse functions throughout the Insect.

  • A new class of hexahelical Insect Proteins revealed as putative carriers of small hydrophobic ligands.
    Structure, 1999
    Co-Authors: Sven Rothemund, Yihcherng Liou, Peter L Davies, Eberhard Krause, Frank D. Sönnichsen
    Abstract:

    Abstract Background: THP12 is an abundant and extraordinarily hydrophilic hemolymph protein from the mealworm Tenebrio molitor and belongs to a group of small Insect Proteins with four highly conserved cysteine residues. Despite their sequence homology to odorant-binding Proteins and pheromone-binding Proteins, the function of these Proteins is unclear. Results: The first three-dimensional structure of THP12 has been determined by multidimensional NMR spectroscopy. The protein has a nonbundle helical structure consisting of six α helices. The arrangement of the α helices has a ‘baseball glove' shape. In addition to the hydrophobic core, electrostatic interactions make contributions to the overall stability of the protein. NMR binding studies demonstrated the binding of small hydrophobic ligands to the single hydrophobic groove in THP12. Comparing the structure of THP12 with the predicted secondary structure of homologs reveals a common fold for this new class of Insect Proteins. A search with the program DALI revealed extensive similarity between the three-dimensional structure of THP12 and the N-terminal domain (residues 1–95) of recoverin, a member of the family of calcium-binding EF-hand Proteins. Conclusions: Although the biological function of this new class of Proteins is as yet undetermined, a general role as α -helical carrier Proteins for small hydrophobic ligands, such as fatty acids or pheromones, is proposed on the basis of NMR-shift perturbation spectroscopy.

Yuan Brad H Kim - One of the best experts on this subject based on the ideXlab platform.

  • pre treated mealworm larvae and silkworm pupae as a novel protein ingredient in emulsion sausages
    Innovative Food Science and Emerging Technologies, 2016
    Co-Authors: Hyunwook Kim, Derico Setyabrata, Owen G. Jones, Yongjae Lee, Yuan Brad H Kim
    Abstract:

    Abstract The objective of this study was to determine the effects of adding pre-treated mealworm larvae ( Tenebrio molitor ) and silkworm pupae ( Bombyx mori ) flours on nutritional, physicochemical and textural properties of emulsion sausages. Whole freeze-dried Insects were sequentially ground, defatted, and acid-hydrolyzed. Control sausage was formulated with 60% lean pork, 20% ice and 20% back fat, and Insect treatments were prepared with replacement of 10% lean pork by each pre-treated Insect flour. Defatting and/or acid hydrolysis significantly increased the protein content of two Insect flours, but acid hydrolysis slightly decreased protein solubility ( P  = 0.002). The addition of pre-treated Insect flours had no impact on protein solubility of emulsion sausages, but increased cooking yield and hardness in a similar extent, regardless of pre-treating methods and Insect types ( P  > 0.05). Our results suggest that through separation processing, mealworm larvae and silkworm pupae can be further optimized as a novel protein ingredient for emulsified meat products. Industrial Relevance This study evaluated the nutritional and technological properties of pre-treated edible Insects as a novel non-meat ingredient for the meat emulsion application. The results of the present study suggest that edible Insect Proteins can be practically utilized as a non-meat food ingredient in processed meat products or potentially other food applications without compromising the nutritional and technological properties of the products.

Laurie A Graham - One of the best experts on this subject based on the ideXlab platform.

  • Characterization and cloning of a Tenebrio molitor hemolymph protein with sequence similarity to Insect odorant-binding Proteins.
    Insect biochemistry and molecular biology, 2001
    Co-Authors: Laurie A Graham, Yihcherng Liou, John G. Baust, Wei Tang, T S Reid, Peter L Davies
    Abstract:

    The yellow mealworm beetle, Tenebrio molitor, produces a number of moderately abundant low molecular weight hemolymph Proteins ( approximately 12 kDa) which behave in a similar manner during purification and share antigenic epitopes. The cDNA sequence of the major component (THP12) was determined and the deduced protein sequence was found to be similar to those of Insect odorant-binding Proteins. Southern blot analysis suggests that at least some of the diversity in this family of Proteins is encoded at the gene level. Both northern and western blot analysis indicate that THP12 is present in a variety of developmental stages and both sexes. THP12 was originally classified as an antifreeze protein, but the lack of antifreeze activity in the recombinant protein, as well as the clear separation of the antifreeze activity from THP12 following HPLC purification, has ruled out this function. The abundance of THP12, the similarity of THP12 to Insect odorant-binding Proteins, and the presence of hydrophobic cavities inside the protein (Rothemund et al., A new class of hexahelical Insect Proteins revealed as putative carriers of small hydrophobic ligands. Structure, 7 (1999) 1325-1332.) suggest that THP12 may function to carry non-water soluble compounds in the hemolymph. THP12 is also similar, particularly in structurally important regions, to other Insect Proteins from non-sensory tissues, suggesting the existence of a large family of carrier Proteins which may perform diverse functions throughout the Insect.

  • characterization and cloning of a tenebrio molitor hemolymph protein with sequence similarity to Insect odorant binding Proteins
    Insect Biochemistry and Molecular Biology, 2001
    Co-Authors: Laurie A Graham, Scott T Reid, Yihcherng Liou, John G. Baust, Wei Tang, Peter L Davies
    Abstract:

    Abstract The yellow mealworm beetle, Tenebrio molitor , produces a number of moderately abundant low molecular weight hemolymph Proteins (∼12 kDa) which behave in a similar manner during purification and share antigenic epitopes. The cDNA sequence of the major component (THP12) was determined and the deduced protein sequence was found to be similar to those of Insect odorant-binding Proteins. Southern blot analysis suggests that at least some of the diversity in this family of Proteins is encoded at the gene level. Both northern and western blot analysis indicate that THP12 is present in a variety of developmental stages and both sexes. THP12 was originally classified as an antifreeze protein, but the lack of antifreeze activity in the recombinant protein, as well as the clear separation of the antifreeze activity from THP12 following HPLC purification, has ruled out this function. The abundance of THP12, the similarity of THP12 to Insect odorant-binding Proteins, and the presence of hydrophobic cavities inside the protein (Rothemund et al., A new class of hexahelical Insect Proteins revealed as putative carriers of small hydrophobic ligands. Structure, 7 (1999) 1325–1332.) suggest that THP12 may function to carry non-water soluble compounds in the hemolymph. THP12 is also similar, particularly in structurally important regions, to other Insect Proteins from non-sensory tissues, suggesting the existence of a large family of carrier Proteins which may perform diverse functions throughout the Insect.

Yihcherng Liou - One of the best experts on this subject based on the ideXlab platform.

  • Characterization and cloning of a Tenebrio molitor hemolymph protein with sequence similarity to Insect odorant-binding Proteins.
    Insect biochemistry and molecular biology, 2001
    Co-Authors: Laurie A Graham, Yihcherng Liou, John G. Baust, Wei Tang, T S Reid, Peter L Davies
    Abstract:

    The yellow mealworm beetle, Tenebrio molitor, produces a number of moderately abundant low molecular weight hemolymph Proteins ( approximately 12 kDa) which behave in a similar manner during purification and share antigenic epitopes. The cDNA sequence of the major component (THP12) was determined and the deduced protein sequence was found to be similar to those of Insect odorant-binding Proteins. Southern blot analysis suggests that at least some of the diversity in this family of Proteins is encoded at the gene level. Both northern and western blot analysis indicate that THP12 is present in a variety of developmental stages and both sexes. THP12 was originally classified as an antifreeze protein, but the lack of antifreeze activity in the recombinant protein, as well as the clear separation of the antifreeze activity from THP12 following HPLC purification, has ruled out this function. The abundance of THP12, the similarity of THP12 to Insect odorant-binding Proteins, and the presence of hydrophobic cavities inside the protein (Rothemund et al., A new class of hexahelical Insect Proteins revealed as putative carriers of small hydrophobic ligands. Structure, 7 (1999) 1325-1332.) suggest that THP12 may function to carry non-water soluble compounds in the hemolymph. THP12 is also similar, particularly in structurally important regions, to other Insect Proteins from non-sensory tissues, suggesting the existence of a large family of carrier Proteins which may perform diverse functions throughout the Insect.

  • characterization and cloning of a tenebrio molitor hemolymph protein with sequence similarity to Insect odorant binding Proteins
    Insect Biochemistry and Molecular Biology, 2001
    Co-Authors: Laurie A Graham, Scott T Reid, Yihcherng Liou, John G. Baust, Wei Tang, Peter L Davies
    Abstract:

    Abstract The yellow mealworm beetle, Tenebrio molitor , produces a number of moderately abundant low molecular weight hemolymph Proteins (∼12 kDa) which behave in a similar manner during purification and share antigenic epitopes. The cDNA sequence of the major component (THP12) was determined and the deduced protein sequence was found to be similar to those of Insect odorant-binding Proteins. Southern blot analysis suggests that at least some of the diversity in this family of Proteins is encoded at the gene level. Both northern and western blot analysis indicate that THP12 is present in a variety of developmental stages and both sexes. THP12 was originally classified as an antifreeze protein, but the lack of antifreeze activity in the recombinant protein, as well as the clear separation of the antifreeze activity from THP12 following HPLC purification, has ruled out this function. The abundance of THP12, the similarity of THP12 to Insect odorant-binding Proteins, and the presence of hydrophobic cavities inside the protein (Rothemund et al., A new class of hexahelical Insect Proteins revealed as putative carriers of small hydrophobic ligands. Structure, 7 (1999) 1325–1332.) suggest that THP12 may function to carry non-water soluble compounds in the hemolymph. THP12 is also similar, particularly in structurally important regions, to other Insect Proteins from non-sensory tissues, suggesting the existence of a large family of carrier Proteins which may perform diverse functions throughout the Insect.

  • A new class of hexahelical Insect Proteins revealed as putative carriers of small hydrophobic ligands.
    Structure, 1999
    Co-Authors: Sven Rothemund, Yihcherng Liou, Peter L Davies, Eberhard Krause, Frank D. Sönnichsen
    Abstract:

    Abstract Background: THP12 is an abundant and extraordinarily hydrophilic hemolymph protein from the mealworm Tenebrio molitor and belongs to a group of small Insect Proteins with four highly conserved cysteine residues. Despite their sequence homology to odorant-binding Proteins and pheromone-binding Proteins, the function of these Proteins is unclear. Results: The first three-dimensional structure of THP12 has been determined by multidimensional NMR spectroscopy. The protein has a nonbundle helical structure consisting of six α helices. The arrangement of the α helices has a ‘baseball glove' shape. In addition to the hydrophobic core, electrostatic interactions make contributions to the overall stability of the protein. NMR binding studies demonstrated the binding of small hydrophobic ligands to the single hydrophobic groove in THP12. Comparing the structure of THP12 with the predicted secondary structure of homologs reveals a common fold for this new class of Insect Proteins. A search with the program DALI revealed extensive similarity between the three-dimensional structure of THP12 and the N-terminal domain (residues 1–95) of recoverin, a member of the family of calcium-binding EF-hand Proteins. Conclusions: Although the biological function of this new class of Proteins is as yet undetermined, a general role as α -helical carrier Proteins for small hydrophobic ligands, such as fatty acids or pheromones, is proposed on the basis of NMR-shift perturbation spectroscopy.

Luciana Galetto - One of the best experts on this subject based on the ideXlab platform.

  • Evidence suggesting interactions between immunodominant membrane protein Imp of Flavescence dorée phytoplasma and protein extracts from distantly related Insect species.
    Journal of Applied Microbiology, 2019
    Co-Authors: Valeria Trivellone, Cristina Marzachi, Matteo Ripamonti, Elisa Angelini, Luisa Filippin, Marika Rossi, Luciana Galetto
    Abstract:

    Aims In this study, binding between the immunodominant membrane protein Imp of the 16SrV-D phytoplasma associated with Flavescence doree disease (FD-Dp) and Insect Proteins of vectors and non-vectors of FD-Dp was tested. Methods and results Six Auchenorrhyncha species, from distantly related groups were selected: Scaphoideus titanus, Euscelidius variegatus, Macrosteles quadripunctulatus, Zyginidia pullula (Cicadomorpha), Ricania speculum and Metcalfa pruinosa (Fulgoromorpha). The vector status of each species was retrieved from the literature or determined by transmission trials in this study. A His-tagged partial Imp protein and a rabbit polyclonal antibody were synthesized and used for Western and Far-Western dot Blot (FWdB) experiments. Total native and membrane Proteins (MP) were extracted from entire bodies and organs (gut and salivary glands) of each Insect species. FWdB showed decreasing interaction intensities of Imp fusion protein with total Proteins from entire bodies of S. titanus, E. variegatus (competent vectors) and M. quadripunctulatus (non-vector), while no interaction signal was detected with the other three species (non-vectors). A strong signal detected upon interaction of FD-D Imp and MP from guts of closely related Insects supports the role of this organ as the first barrier to ensure successful transmission. Conclusions Our results showed that specific Imp binding, correlated with vector status, is involved in interactions between FD-Dp and Insect Proteins. Significance and impact of the study Integrating knowledge on host-pathogen protein-protein interactions and on Insect phylogeny would help to identify the actual range of vectors of phytoplasma strains of economic importance.

  • the major antigenic membrane protein of candidatus phytoplasma asteris selectively interacts with atp synthase and actin of leafhopper vectors
    PLOS ONE, 2011
    Co-Authors: Luciana Galetto, Domenico Bosco, Raffaella Balestrini, Andrea Genre, Jacqueline Fletcher, Cristina Marzachi
    Abstract:

    Phytoplasmas, uncultivable phloem-limited phytopathogenic wall-less bacteria, represent a major threat to agriculture worldwide. They are transmitted in a persistent, propagative manner by phloem-sucking Hemipteran Insects. Phytoplasma membrane Proteins are in direct contact with hosts and are presumably involved in determining vector specificity. Such a role has been proposed for phytoplasma transmembrane Proteins encoded by circular extrachromosomal elements, at least one of which is a plasmid. Little is known about the interactions between major phytoplasma antigenic membrane protein (Amp) and Insect vector Proteins. The aims of our work were to identify vector Proteins interacting with Amp and to investigate their role in transmission specificity. In controlled transmission experiments, four Hemipteran species were identified as vectors of “Candidatus Phytoplasma asteris”, the chrysanthemum yellows phytoplasmas (CYP) strain, and three others as non-vectors. Interactions between a labelled (recombinant) CYP Amp and Insect Proteins were analysed by far Western blots and affinity chromatography. Amp interacted specifically with a few Proteins from vector species only. Among Amp-binding vector Proteins, actin and both the α and β subunits of ATP synthase were identified by mass spectrometry and Western blots. Immunofluorescence confocal microscopy and Western blots of plasma membrane and mitochondrial fractions confirmed the localisation of ATP synthase, generally known as a mitochondrial protein, in plasma membranes of midgut and salivary gland cells in the vector Euscelidius variegatus. The vector-specific interaction between phytoplasma Amp and Insect ATP synthase is demonstrated for the first time, and this work also supports the hypothesis that host actin is involved in the internalization and intracellular motility of phytoplasmas within their vectors. Phytoplasma Amp is hypothesized to play a crucial role in Insect transmission specificity.

  • In vitro interactions between immunodominant membrane protein of lime witches' broom phytoplasma and leafhopper vector Proteins.
    Bulletin of Insectology, 2011
    Co-Authors: M. Siampour, Luciana Galetto, Cristina Marzachi, Domenico Bosco, Keramat Izadpanah, Assunta Bertaccini, S. Maini
    Abstract:

    Lime witches’ broom phytoplasma (16SrII, LWB) causes major losses to lime cultivation in Iran. The role of its immunodominant membrane protein (IMP) in the specific interaction with vector Proteins was addressed. The carboxy terminal moiety of LWB IMP, coding the extracellular part of the protein, was expressed (LWB f∆IMP) as a tool to study IMP interactions with Insect Proteins. In preliminary affinity chromatography experiments, leafhopper vector Proteins with different sizes interacted with LWB