ArticleInsect biochemistry and molecular biology2018
The Manduca sexta serpinome: Analysis of serpin genes and proteins in the tobacco hornworm.
Article in Insect biochemistry and molecular biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 31 citations in OpenAlex.
- Chromosome-Scale Atlas ofGenes · 2026Article
- The role of a viral symbiont in the thermal mismatch of host-parasitoid interactions.The Journal of experimental biology · 2026Article
- U-Net-based reactive center loop-identifier for serpins.Bioinformatics advances · 2026Article
- Article
- Activity of Serpins in Context to Hydrophobic Interaction.Biomolecules · 2025Article
- Innate Immunity in Insects: The Lights and Shadows of Phenoloxidase System Activation.International journal of molecular sciences · 2025Review
- Identification of immunity-related genes distinctly regulated by Manduca sexta Spӓtzle-1/2 and Escherichia coli peptidoglycan.Insect biochemistry and molecular biology · 2024Article
- Serpin-4 Negatively Regulates Prophenoloxidase Activation and Antimicrobial Peptide Synthesis in the Silkworm,International journal of molecular sciences · 2023Article
- An evolutionarily conserved serine protease network mediates melanization and Toll activation inScience advances · 2023Article
- A Genome-Wide Analysis of Serine Protease Inhibitors inInternational journal of molecular sciences · 2023Article
- Serpin-1a and serpin-6 regulate the Toll pathway immune homeostasis by synergistically inhibiting the Spätzle-processing enzyme CLIP2 in silkworm, Bombyx mori.PLoS pathogens · 2023Article
- The Chromosome-Level Genome Assembly of Bean Blossom Thrips (International journal of molecular sciences · 2023Article
- Identification and functional analysis of serine protease inhibitor gene family ofFrontiers in physiology · 2023Article
- Proteomic analysis of pharate pupal molting fluid from the tobacco hornworm, Manduca sexta.Insect biochemistry and molecular biology · 2022Article
- A teratocyte-specific serpin from the endoparasitoid wasp Cotesia vestalis inhibits the prophenoloxidase-activating system of its host Plutella xylostella.Insect molecular biology · 2022Article
- A TIL-Type Serine Protease Inhibitor Involved in Humoral Immune Response of Asian Corn BorerFrontiers in immunology · 2022Article
- Changes in composition and levels of hemolymph proteins during metamorphosis of Manduca sexta.Insect biochemistry and molecular biology · 2020Article
- Hemolymph protease-5 links the melanization and Toll immune pathways in the tobacco hornworm,Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Peptides based on the reactive center loop of Manduca sexta serpin-3 block its protease inhibitory function.Scientific reports · 2020Article
- Inhibition of immune pathway-initiating hemolymph protease-14 by Manduca sexta serpin-12, a conserved mechanism for the regulation of melanization and Toll activation in insects.Insect biochemistry and molecular biology · 2020Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
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.
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