The Experts below are selected from a list of 207 Experts worldwide ranked by ideXlab platform

Manabu Kamimura - One of the best experts on this subject based on the ideXlab platform.

Chieka Minakuchi - One of the best experts on this subject based on the ideXlab platform.

Michael R Kanost - One of the best experts on this subject based on the ideXlab platform.

  • The Manduca sexta serpinome: Analysis of serpin genes and proteins in the tobacco hornworm.
    Insect biochemistry and molecular biology, 2018
    Co-Authors: Jayne M. Christen, Neal T Dittmer, Haobo Jiang, Xiaolong Cao, Xiufeng Zhang, Michael R Kanost
    Abstract:

    Members of the serpin superfamily of proteins occur in animals, plants, bacteria, archaea and some viruses. They adopt a variety of physiological functions, including regulation of immune system, modulation of apoptosis, hormone transport and acting as storage proteins. Most members of the serpin family are inhibitors of serine proteinases. In this study, we searched the genome of Manduca sexta and identified 32 serpin genes. We analyzed the structure of these genes and the sequences of their encoded proteins. Three M. sexta genes (serpin-1, serpin-15, and serpin-28) have mutually exclusive alternatively spliced exons encoding the carboxyl-terminal reactive center loop of the protein, which is the site of interaction with target proteases. We discovered that MsSerpin-1 has 14 splicing isoforms, including two undiscovered in previous studies. Twenty-eight of the 32 M. sexta serpins include a putative secretion signal peptide and are predicted to be extracellular proteins. Phylogenetic analysis of serpins in M. sexta and Bombyx mori indicates that 17 are orthologous pairs, perhaps carrying out essential physiological functions. Analysis of the reactive center loop and hinge regions of the protein sequences indicates that 16 of the serpin genes encode proteins that may lack proteinase inhibitor activity. Our annotation and analysis of these serpin genes and their transcript profiles should lead to future advances in experimental study of their functions in Insect Biochemistry.

  • multifaceted biological insights from a draft genome sequence of the tobacco hornworm moth manduca sexta
    Insect Biochemistry and Molecular Biology, 2016
    Co-Authors: Michael R Kanost, Haobo Jiang, Estela L Arrese, Yunru Chen, Sanjay Chellapilla, Marian R Goldsmith, Ewald Grossewilde, David G Heckel, Nicolae Herndon, Alexie Papanicolaou
    Abstract:

    Manduca sexta, known as the tobacco hornworm or Carolina sphinx moth, is a lepidopteran Insect that is used extensively as a model system for research in Insect Biochemistry, physiology, neurobiology, development, and immunity. One important benefit of this species as an experimental model is its extremely large size, reaching more than 10 g in the larval stage. M. sexta larvae feed on solanaceous plants and thus must tolerate a substantial challenge from plant allelochemicals, including nicotine. We report the sequence and annotation of the M. sexta genome, and a survey of gene expression in various tissues and developmental stages. The Msex_1.0 genome assembly resulted in a total genome size of 419.4 Mbp. Repetitive sequences accounted for 25.8% of the assembled genome. The official gene set is comprised of 15,451 protein-coding genes, of which 2498 were manually curated. Extensive RNA-seq data from many tissues and developmental stages were used to improve gene models and for insights into gene expression patterns. Genome wide synteny analysis indicated a high level of macrosynteny in the Lepidoptera. Annotation and analyses were carried out for gene families involved in a wide spectrum of biological processes, including apoptosis, vacuole sorting, growth and development, structures of exoskeleton, egg shells, and muscle, vision, chemosensation, ion channels, signal transduction, neuropeptide signaling, neurotransmitter synthesis and transport, nicotine tolerance, lipid metabolism, and immunity. This genome sequence, annotation, and analysis provide an important new resource from a well-studied model Insect species and will facilitate further biochemical and mechanistic experimental studies of many biological systems in Insects.

  • multifaceted biological insights from a draft genome sequence of the tobacco hornworm moth manduca sexta
    Insect Biochemistry and Molecular Biology, 2016
    Co-Authors: Michael R Kanost, Xiaolong Cao, Estela L Arrese, Yunru Chen, Sanjay Chellapilla, Marian R Goldsmith, Ewald Grossewilde, David G Heckel, Nicolae Herndon, Haobo Jiang
    Abstract:

    Manduca sexta, known as the tobacco hornworm or Carolina sphinx moth, is a lepidopteran Insect that is used extensively as a model system for research in Insect Biochemistry, physiology, neurobiology, development, and immunity. One important benefit of this species as an experimental model is its extremely large size, reaching more than 10 g in the larval stage. M. sexta larvae feed on solanaceous plants and thus must tolerate a substantial challenge from plant allelochemicals, including nicotine. We report the sequence and annotation of the M. sexta genome, and a survey of gene expression in various tissues and developmental stages. The Msex_1.0 genome assembly resulted in a total genome size of 419.4 Mbp. Repetitive sequences accounted for 25.8% of the assembled genome. The official gene set is comprised of 15,451 protein-coding genes, of which 2498 were manually curated. Extensive RNA-seq data from many tissues and developmental stages were used to improve gene models and for insights into gene expression patterns. Genome wide synteny analysis indicated a high level of macrosynteny in the Lepidoptera. Annotation and analyses were carried out for gene families involved in a wide spectrum of biological processes, including apoptosis, vacuole sorting, growth and development, structures of exoskeleton, egg shells, and muscle, vision, chemosensation, ion channels, signal transduction, neuropeptide signaling, neurotransmitter synthesis and transport, nicotine tolerance, lipid metabolism, and immunity. This genome sequence, annotation, and analysis provide an important new resource from a well-studied model Insect species and will facilitate further biochemical and mechanistic experimental studies of many biological systems in Insects.

  • erratumerratum to model reactions for Insect cuticle sclerotization cross linking of recombinant cuticular proteins upon their laccase catalyzed oxidative conjugation with catechols Insect Biochemistry and molecular biology 36 2006 353 365
    Insect Biochemistry and Molecular Biology, 2006
    Co-Authors: Richard J Suderman, Neal T Dittmer, Michael R Kanost, Karl J Kramer
    Abstract:

    Erratum to ‘‘Model reactions for Insect cuticle sclerotization: Cross-linking of recombinant cuticular proteins upon their laccase-catalyzed oxidative conjugation with catechols’’ [Insect Biochemistry and Molecular Biology 36 (2006) 353–365] Richard J. Suderman, Neal T. Dittmer, Michael R. Kanost , Karl J. Kramer Department of Biochemistry, 103 Willard Hall, Kansas State University, Manhattan, KS 66506-3706, USA Grain Marketing and Production Research Center, Agricultural Research Service, US Department of Agriculture, Manhattan, KS 66506-2736, USA

  • ErratumErratum to “Model reactions for Insect cuticle sclerotization: Cross-linking of recombinant cuticular proteins upon their laccase-catalyzed oxidative conjugation with catechols”: [Insect Biochemistry and Molecular Biology 36 (2006) 353–365]
    Insect Biochemistry and Molecular Biology, 2006
    Co-Authors: Richard J Suderman, Neal T Dittmer, Michael R Kanost, Karl J Kramer
    Abstract:

    Erratum to ‘‘Model reactions for Insect cuticle sclerotization: Cross-linking of recombinant cuticular proteins upon their laccase-catalyzed oxidative conjugation with catechols’’ [Insect Biochemistry and Molecular Biology 36 (2006) 353–365] Richard J. Suderman, Neal T. Dittmer, Michael R. Kanost , Karl J. Kramer Department of Biochemistry, 103 Willard Hall, Kansas State University, Manhattan, KS 66506-3706, USA Grain Marketing and Production Research Center, Agricultural Research Service, US Department of Agriculture, Manhattan, KS 66506-2736, USA

Haobo Jiang - One of the best experts on this subject based on the ideXlab platform.

  • The Manduca sexta serpinome: Analysis of serpin genes and proteins in the tobacco hornworm.
    Insect biochemistry and molecular biology, 2018
    Co-Authors: Jayne M. Christen, Neal T Dittmer, Haobo Jiang, Xiaolong Cao, Xiufeng Zhang, Michael R Kanost
    Abstract:

    Members of the serpin superfamily of proteins occur in animals, plants, bacteria, archaea and some viruses. They adopt a variety of physiological functions, including regulation of immune system, modulation of apoptosis, hormone transport and acting as storage proteins. Most members of the serpin family are inhibitors of serine proteinases. In this study, we searched the genome of Manduca sexta and identified 32 serpin genes. We analyzed the structure of these genes and the sequences of their encoded proteins. Three M. sexta genes (serpin-1, serpin-15, and serpin-28) have mutually exclusive alternatively spliced exons encoding the carboxyl-terminal reactive center loop of the protein, which is the site of interaction with target proteases. We discovered that MsSerpin-1 has 14 splicing isoforms, including two undiscovered in previous studies. Twenty-eight of the 32 M. sexta serpins include a putative secretion signal peptide and are predicted to be extracellular proteins. Phylogenetic analysis of serpins in M. sexta and Bombyx mori indicates that 17 are orthologous pairs, perhaps carrying out essential physiological functions. Analysis of the reactive center loop and hinge regions of the protein sequences indicates that 16 of the serpin genes encode proteins that may lack proteinase inhibitor activity. Our annotation and analysis of these serpin genes and their transcript profiles should lead to future advances in experimental study of their functions in Insect Biochemistry.

  • multifaceted biological insights from a draft genome sequence of the tobacco hornworm moth manduca sexta
    Insect Biochemistry and Molecular Biology, 2016
    Co-Authors: Michael R Kanost, Haobo Jiang, Estela L Arrese, Yunru Chen, Sanjay Chellapilla, Marian R Goldsmith, Ewald Grossewilde, David G Heckel, Nicolae Herndon, Alexie Papanicolaou
    Abstract:

    Manduca sexta, known as the tobacco hornworm or Carolina sphinx moth, is a lepidopteran Insect that is used extensively as a model system for research in Insect Biochemistry, physiology, neurobiology, development, and immunity. One important benefit of this species as an experimental model is its extremely large size, reaching more than 10 g in the larval stage. M. sexta larvae feed on solanaceous plants and thus must tolerate a substantial challenge from plant allelochemicals, including nicotine. We report the sequence and annotation of the M. sexta genome, and a survey of gene expression in various tissues and developmental stages. The Msex_1.0 genome assembly resulted in a total genome size of 419.4 Mbp. Repetitive sequences accounted for 25.8% of the assembled genome. The official gene set is comprised of 15,451 protein-coding genes, of which 2498 were manually curated. Extensive RNA-seq data from many tissues and developmental stages were used to improve gene models and for insights into gene expression patterns. Genome wide synteny analysis indicated a high level of macrosynteny in the Lepidoptera. Annotation and analyses were carried out for gene families involved in a wide spectrum of biological processes, including apoptosis, vacuole sorting, growth and development, structures of exoskeleton, egg shells, and muscle, vision, chemosensation, ion channels, signal transduction, neuropeptide signaling, neurotransmitter synthesis and transport, nicotine tolerance, lipid metabolism, and immunity. This genome sequence, annotation, and analysis provide an important new resource from a well-studied model Insect species and will facilitate further biochemical and mechanistic experimental studies of many biological systems in Insects.

  • multifaceted biological insights from a draft genome sequence of the tobacco hornworm moth manduca sexta
    Insect Biochemistry and Molecular Biology, 2016
    Co-Authors: Michael R Kanost, Xiaolong Cao, Estela L Arrese, Yunru Chen, Sanjay Chellapilla, Marian R Goldsmith, Ewald Grossewilde, David G Heckel, Nicolae Herndon, Haobo Jiang
    Abstract:

    Manduca sexta, known as the tobacco hornworm or Carolina sphinx moth, is a lepidopteran Insect that is used extensively as a model system for research in Insect Biochemistry, physiology, neurobiology, development, and immunity. One important benefit of this species as an experimental model is its extremely large size, reaching more than 10 g in the larval stage. M. sexta larvae feed on solanaceous plants and thus must tolerate a substantial challenge from plant allelochemicals, including nicotine. We report the sequence and annotation of the M. sexta genome, and a survey of gene expression in various tissues and developmental stages. The Msex_1.0 genome assembly resulted in a total genome size of 419.4 Mbp. Repetitive sequences accounted for 25.8% of the assembled genome. The official gene set is comprised of 15,451 protein-coding genes, of which 2498 were manually curated. Extensive RNA-seq data from many tissues and developmental stages were used to improve gene models and for insights into gene expression patterns. Genome wide synteny analysis indicated a high level of macrosynteny in the Lepidoptera. Annotation and analyses were carried out for gene families involved in a wide spectrum of biological processes, including apoptosis, vacuole sorting, growth and development, structures of exoskeleton, egg shells, and muscle, vision, chemosensation, ion channels, signal transduction, neuropeptide signaling, neurotransmitter synthesis and transport, nicotine tolerance, lipid metabolism, and immunity. This genome sequence, annotation, and analysis provide an important new resource from a well-studied model Insect species and will facilitate further biochemical and mechanistic experimental studies of many biological systems in Insects.

  • manduca sexta prophenoloxidase propo activation requires propo activating proteinase pap and serine proteinase homologs sphs simultaneously
    Insect Biochemistry and Molecular Biology, 2005
    Co-Authors: Snehalata Gupta, Yang Wang, Haobo Jiang
    Abstract:

    In the tobacco hornworm Manduca sexta, proteolytic activation of prophenoloxidase (proPO) is mediated by three proPO-activating proteinases (PAPs) and two serine proteinase homologs (SPHs) (Proceedings of the National Academy of Sciences, USA 95 (1998) 12220-12225; J. Biol. Chem. 278 (2003a) 3552-3561; Insect Biochem. Mol. Biol. 33 (2003b) 1049-1060). While our current data are consistent with the hypothesis that the SPHs serve as a cofactor/anchor for PAPs (Insect Biochemistry and Molecular Biology 33 (2003) 197-208; Insect Biochemistry and Molecular Biology 34 (2004) 731-742), roles of these clip-domain proteins (i.e. PAPs and SPHs) in proPO activation are poorly defined. To better understand this process, we further characterized the activation reaction using proPO, PAP-1 and SPHs. PAP-1 itself cleaved nearly 1/3 of proPO at Arg51 without generating much phenoloxidase (PO) activity. In the presence of SPHs, the cleavage of proPO became more complete while the increase in PO activity was over 20-fold, indicating that the extent of cleavage does not directly correlate with PO activity. Since SPHs and p-amidinophenyl methanesulfonyl fluoride (APMSF)-treated PAP-1 did not generate active PO by interacting with proPO, proteolytic cleavage is critical for proPO activation. After 1/5 of proPO was processed by PAP-1 alone which was then inactivated by M. sexta serpin-1J or APMSF, further incubation of the reaction mixture with SPHs failed to generate active PO either. Thus, SPHs cannot generate PO activity by simply binding to cleaved proPO. M. sexta proPO activation requires active PAP-1 and SPHs at the same time-one for limited proteolysis and the other as a cofactor, perhaps. Gel filtration chromatography and native gel electrophoresis revealed the PAP-SPH, proPO-PAP, and SPH-proPO associations, essential for generating high Mr, active PO at the site of infection.

Yoshiaki Nakagawa - One of the best experts on this subject based on the ideXlab platform.