Michael Kanost - Academia.edu (original) (raw)

Papers by Michael Kanost

Research paper thumbnail of Activation of Lepidopteran Insect Innate Immune Responses by C-Type Immulectins

Research paper thumbnail of Paralytic and Plasmatocyte Spreading Peptide From Manduca sexta

Advances in Experimental Medicine and Biology, 2001

A family of hemolymph peptides with diverse biological activities has been identified in several ... more A family of hemolymph peptides with diverse biological activities has been identified in several Lepidopteran species. These peptides can cause rapid paralysis (Skinner et al., 1991), block growth and development (Hayakawa, 1991), and stimulate plasmatocyte spreading and aggregation (Clark et al., 1997). The 23-residue peptides are produced from larger inactive precursors in plasma. The precursor proteins are rapidly converted by a specific proteolysis to active molecules upon bleeding and perhaps after parasitization or infection.

Research paper thumbnail of Hemolymph Proteinases in Immune Responses of Manduca sexta

Advances in Experimental Medicine and Biology, 2001

Extracellular signal transduction pathways in blood are often composed of cascades of serine prot... more Extracellular signal transduction pathways in blood are often composed of cascades of serine proteinases to amplify rapidly a response to wounding or infection. The vertebrate blood coagulation and complement pathways are the most fully characterized of such proteinase cascades. Serine proteinases also play important roles in defensive responses in hemolymph of arthropods. The hemolymph coagulation system of horseshoe crabs has been very nicely elucidated to function as a complex and intricately regulated proteinase cascade for protection against microbial infection (Kawabata et al., 1996).

Research paper thumbnail of Sequence conservation, phylogenetic relationships, and expression profiles of nondigestive serine proteases and serine protease homologs in Manduca sexta

Insect biochemistry and molecular biology, Jan 19, 2014

Serine protease (SP) and serine protease homolog (SPH) genes in insects encode a large family of ... more Serine protease (SP) and serine protease homolog (SPH) genes in insects encode a large family of proteins involved in digestion, development, immunity, and other processes. While 68 digestive SPs and their close homologs are reported in a companion paper (Kuwar et al., in preparation), we have identified 125 other SPs/SPHs in Manduca sexta and studied their structure, evolution, and expression. Fifty-two of them contain cystine-stabilized structures for molecular recognition, including clip, LDLa, Sushi, Wonton, TSP, CUB, Frizzle, and SR domains. There are nineteen groups of genes evolved from relatively recent gene duplication and sequence divergence. Thirty-five SPs and seven SPHs contain 1, 2 or 5 clip domains. Multiple sequence alignment and molecular modeling of the 54 clip domains have revealed structural diversity of these regulatory modules. Sequence comparison with their homologs in Drosophila melanogaster, Anopheles gambiae and Tribolium castaneum allows us to classify the...

Research paper thumbnail of Expression and Purification of Manduca sexta Prophenoloxidase-Activating Proteinase Precursor (proPAP) from Baculovirus-Infected Insect Cells

Protein Expression and Purification, 2001

Research paper thumbnail of Modulation of Bovine Lymphocyte Response by Salivary Gland Extracts of the Stable Fly,Stomoxys calcitrans(Diptera: Muscidae)

Journal of Medical Entomology, 2002

Research paper thumbnail of An Immunoglobulin Binding Protein (Antigen 5) of the Stable Fly (Diptera: Muscidae) Salivary Gland Stimulates Bovine Immune Responses

Journal of Medical Entomology, 2008

Research paper thumbnail of Prophenoloxidase-activating Proteinase-2 from Hemolymph ofManduca sexta

Journal of Biological Chemistry, 2002

Research paper thumbnail of Manduca sexta Hemolymph Proteinase 21 Activates Prophenoloxidase-activating Proteinase 3 in an Insect Innate Immune Response Proteinase Cascade

Journal of Biological Chemistry, 2007

Research paper thumbnail of Four serine proteinases expressed in Manduca sexta haemocytes

Insect Molecular Biology, 1999

Research paper thumbnail of Primary structure of ribosomal proteins S3 and S7 from Manduca sexta

Insect Molecular Biology, 1996

We have isolated from Manduca sexta full-length cDNAs encoding proteins homologous to human ribos... more We have isolated from Manduca sexta full-length cDNAs encoding proteins homologous to human ribosomal proteins S3 and S7. These are the first ribosomal protein sequences obtained from non-Dipteran insects. M. sexta ribosomal protein S3 has a molecular mass of 26,715 Da. Ribosomal protein S7 has a mass 21,870 Da. Both are basic proteins, with abundant Lys and Arg residues that may interact with ribosomal RNA in the ribosome. Southern blot hybridization suggests the presence of single genes for both ribosomal proteins in the M. sexta genome. Alignments with other S3 and S7 sequences available In the database indicate regions of the ribosomal proteins that have been the most highly conserved in evolution and may point to important functional regions in the proteins. Ribosomal protein S3 appears to be more highly conserved then ribosomal protein S7. This may be due to greater constraints on the structure of S3 because of its dual functions in translation as a ribosomal protein and in DNA repair in the nucleus.

Research paper thumbnail of Nonproteolytic serine proteinase homologs are involved in prophenoloxidase activation in the tobacco hornworm, Manduca sexta

Insect Biochemistry and Molecular Biology, 2003

Research paper thumbnail of Molecular cloning of cDNAs for two pro-phenol oxidase subunits from the malaria vector, Anopheles gambiae1The sequences have been deposited in GenBank under accession numbers AF004915 and AF004916.1

Insect Biochemistry and Molecular Biology, 1997

Research paper thumbnail of Prophenoloxidase-activating proteinase-3 (PAP-3) from Manduca sexta hemolymph: a clip-domain serine proteinase regulated by serpin-1J and serine proteinase homologs

Insect Biochemistry and Molecular Biology, 2003

Research paper thumbnail of An insight into the transcriptome and proteome of the salivary gland of the stable fly, Stomoxys calcitrans

Insect Biochemistry and Molecular Biology, 2009

Research paper thumbnail of Biological activity of Manduca sexta paralytic and plasmatocyte spreading peptide and primary structure of its hemolymph precursor

Insect Biochemistry and Molecular Biology, 1999

Research paper thumbnail of A bacteria-induced, intracellular serpin in granular hemocytes of Manduca sexta

Insect Biochemistry and Molecular Biology, 2001

Research paper thumbnail of Serine proteases and their homologs in the Drosophila melanogaster genome: an initial analysis of sequence conservation and phylogenetic relationships

Research paper thumbnail of Soluble peptidoglycan fragments stimulate antibacterial protein synthesis by fat body from larvae of Manduca sexta

Developmental & Comparative Immunology, 1985

Both hemocytes and fat body from larvae of Manduca sexta, which have been injected with inducers ... more Both hemocytes and fat body from larvae of Manduca sexta, which have been injected with inducers of antibacterial protein synthesis, contain immunoreactive lysozyme. However, fat body is a richer source and has been demonstrated to synthesize and release lysozyme and cecropin-like peptides (bactericidins) in vitro. Fat body secretion of lysozyme and bactericidins is stimulated by addition of soluble peptidoglycan fragments to culture medium. The rate of lysozyme secretion by fat body varies as a function of peptidoglycan inducer concentration. These data are consistent with the hypothesis that, in vivo, bacteria must be phagocytized and partially degraded (processed) by hemocytes to generate a signal (peptidoglycan) that subsequently induces antibacterial protein synthesis by fat body.

Research paper thumbnail of Functional analysis of four processing products from multiple precursors encoded by a lebocin-related gene from Manduca sexta

Developmental & Comparative Immunology, 2010

Research paper thumbnail of Activation of Lepidopteran Insect Innate Immune Responses by C-Type Immulectins

Research paper thumbnail of Paralytic and Plasmatocyte Spreading Peptide From Manduca sexta

Advances in Experimental Medicine and Biology, 2001

A family of hemolymph peptides with diverse biological activities has been identified in several ... more A family of hemolymph peptides with diverse biological activities has been identified in several Lepidopteran species. These peptides can cause rapid paralysis (Skinner et al., 1991), block growth and development (Hayakawa, 1991), and stimulate plasmatocyte spreading and aggregation (Clark et al., 1997). The 23-residue peptides are produced from larger inactive precursors in plasma. The precursor proteins are rapidly converted by a specific proteolysis to active molecules upon bleeding and perhaps after parasitization or infection.

Research paper thumbnail of Hemolymph Proteinases in Immune Responses of Manduca sexta

Advances in Experimental Medicine and Biology, 2001

Extracellular signal transduction pathways in blood are often composed of cascades of serine prot... more Extracellular signal transduction pathways in blood are often composed of cascades of serine proteinases to amplify rapidly a response to wounding or infection. The vertebrate blood coagulation and complement pathways are the most fully characterized of such proteinase cascades. Serine proteinases also play important roles in defensive responses in hemolymph of arthropods. The hemolymph coagulation system of horseshoe crabs has been very nicely elucidated to function as a complex and intricately regulated proteinase cascade for protection against microbial infection (Kawabata et al., 1996).

Research paper thumbnail of Sequence conservation, phylogenetic relationships, and expression profiles of nondigestive serine proteases and serine protease homologs in Manduca sexta

Insect biochemistry and molecular biology, Jan 19, 2014

Serine protease (SP) and serine protease homolog (SPH) genes in insects encode a large family of ... more Serine protease (SP) and serine protease homolog (SPH) genes in insects encode a large family of proteins involved in digestion, development, immunity, and other processes. While 68 digestive SPs and their close homologs are reported in a companion paper (Kuwar et al., in preparation), we have identified 125 other SPs/SPHs in Manduca sexta and studied their structure, evolution, and expression. Fifty-two of them contain cystine-stabilized structures for molecular recognition, including clip, LDLa, Sushi, Wonton, TSP, CUB, Frizzle, and SR domains. There are nineteen groups of genes evolved from relatively recent gene duplication and sequence divergence. Thirty-five SPs and seven SPHs contain 1, 2 or 5 clip domains. Multiple sequence alignment and molecular modeling of the 54 clip domains have revealed structural diversity of these regulatory modules. Sequence comparison with their homologs in Drosophila melanogaster, Anopheles gambiae and Tribolium castaneum allows us to classify the...

Research paper thumbnail of Expression and Purification of Manduca sexta Prophenoloxidase-Activating Proteinase Precursor (proPAP) from Baculovirus-Infected Insect Cells

Protein Expression and Purification, 2001

Research paper thumbnail of Modulation of Bovine Lymphocyte Response by Salivary Gland Extracts of the Stable Fly,Stomoxys calcitrans(Diptera: Muscidae)

Journal of Medical Entomology, 2002

Research paper thumbnail of An Immunoglobulin Binding Protein (Antigen 5) of the Stable Fly (Diptera: Muscidae) Salivary Gland Stimulates Bovine Immune Responses

Journal of Medical Entomology, 2008

Research paper thumbnail of Prophenoloxidase-activating Proteinase-2 from Hemolymph ofManduca sexta

Journal of Biological Chemistry, 2002

Research paper thumbnail of Manduca sexta Hemolymph Proteinase 21 Activates Prophenoloxidase-activating Proteinase 3 in an Insect Innate Immune Response Proteinase Cascade

Journal of Biological Chemistry, 2007

Research paper thumbnail of Four serine proteinases expressed in Manduca sexta haemocytes

Insect Molecular Biology, 1999

Research paper thumbnail of Primary structure of ribosomal proteins S3 and S7 from Manduca sexta

Insect Molecular Biology, 1996

We have isolated from Manduca sexta full-length cDNAs encoding proteins homologous to human ribos... more We have isolated from Manduca sexta full-length cDNAs encoding proteins homologous to human ribosomal proteins S3 and S7. These are the first ribosomal protein sequences obtained from non-Dipteran insects. M. sexta ribosomal protein S3 has a molecular mass of 26,715 Da. Ribosomal protein S7 has a mass 21,870 Da. Both are basic proteins, with abundant Lys and Arg residues that may interact with ribosomal RNA in the ribosome. Southern blot hybridization suggests the presence of single genes for both ribosomal proteins in the M. sexta genome. Alignments with other S3 and S7 sequences available In the database indicate regions of the ribosomal proteins that have been the most highly conserved in evolution and may point to important functional regions in the proteins. Ribosomal protein S3 appears to be more highly conserved then ribosomal protein S7. This may be due to greater constraints on the structure of S3 because of its dual functions in translation as a ribosomal protein and in DNA repair in the nucleus.

Research paper thumbnail of Nonproteolytic serine proteinase homologs are involved in prophenoloxidase activation in the tobacco hornworm, Manduca sexta

Insect Biochemistry and Molecular Biology, 2003

Research paper thumbnail of Molecular cloning of cDNAs for two pro-phenol oxidase subunits from the malaria vector, Anopheles gambiae1The sequences have been deposited in GenBank under accession numbers AF004915 and AF004916.1

Insect Biochemistry and Molecular Biology, 1997

Research paper thumbnail of Prophenoloxidase-activating proteinase-3 (PAP-3) from Manduca sexta hemolymph: a clip-domain serine proteinase regulated by serpin-1J and serine proteinase homologs

Insect Biochemistry and Molecular Biology, 2003

Research paper thumbnail of An insight into the transcriptome and proteome of the salivary gland of the stable fly, Stomoxys calcitrans

Insect Biochemistry and Molecular Biology, 2009

Research paper thumbnail of Biological activity of Manduca sexta paralytic and plasmatocyte spreading peptide and primary structure of its hemolymph precursor

Insect Biochemistry and Molecular Biology, 1999

Research paper thumbnail of A bacteria-induced, intracellular serpin in granular hemocytes of Manduca sexta

Insect Biochemistry and Molecular Biology, 2001

Research paper thumbnail of Serine proteases and their homologs in the Drosophila melanogaster genome: an initial analysis of sequence conservation and phylogenetic relationships

Research paper thumbnail of Soluble peptidoglycan fragments stimulate antibacterial protein synthesis by fat body from larvae of Manduca sexta

Developmental & Comparative Immunology, 1985

Both hemocytes and fat body from larvae of Manduca sexta, which have been injected with inducers ... more Both hemocytes and fat body from larvae of Manduca sexta, which have been injected with inducers of antibacterial protein synthesis, contain immunoreactive lysozyme. However, fat body is a richer source and has been demonstrated to synthesize and release lysozyme and cecropin-like peptides (bactericidins) in vitro. Fat body secretion of lysozyme and bactericidins is stimulated by addition of soluble peptidoglycan fragments to culture medium. The rate of lysozyme secretion by fat body varies as a function of peptidoglycan inducer concentration. These data are consistent with the hypothesis that, in vivo, bacteria must be phagocytized and partially degraded (processed) by hemocytes to generate a signal (peptidoglycan) that subsequently induces antibacterial protein synthesis by fat body.

Research paper thumbnail of Functional analysis of four processing products from multiple precursors encoded by a lebocin-related gene from Manduca sexta

Developmental & Comparative Immunology, 2010