ArticleJournal of peptide science : an official publication of the European Peptide Society2008
Solution structure, antibacterial activity, and expression profile of Manduca sexta moricin.
Article in Journal of peptide science : an official publication of the European Peptide Society, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- Insect Antimicrobial Peptides as Guardians of Immunity and Beyond: A Review.International journal of molecular sciences · 2024Review
- Antimicrobial peptide moricin induces ROS mediated caspase-dependent apoptosis in human triple-negative breast cancer via suppression of notch pathway.Cancer cell international · 2023Article
- Insect Meals and Insect Antimicrobial Peptides as an Alternative for Antibiotics and Growth Promoters in Livestock Production.Pathogens (Basel, Switzerland) · 2023Review
- Insect-pathogen crosstalk and the cellular-molecular mechanisms of insect immunity: uncovering the underlying signaling pathways and immune regulatory function of non-coding RNAs.Frontiers in immunology · 2023Review
- A zone-of-inhibition assay to screen for humoral antimicrobial activity in mosquito hemolymph.Frontiers in cellular and infection microbiology · 2023Article
- Article
- Spotlight on the Selected New Antimicrobial Innate Immune Peptides Discovered During 2015-2019.Current topics in medicinal chemistry · 2020Review
- Molecular Identification of a Moricin Family Antimicrobial Peptide (Px-Mor) FromFrontiers in microbiology · 2019Article
- Isolation and Purification of an Antibacterial Protein from Immune Induced Haemolymph of American Cockroach,Journal of arthropod-borne diseases · 2016Article
- Characterization and regulation of expression of an antifungal peptide from hemolymph of an insect, Manduca sexta.Developmental and comparative immunology · 2016Article
- Co-expression of Dorsal and Rel2 Negatively Regulates Antimicrobial Peptide Expression in the Tobacco Hornworm Manduca sexta.Scientific reports · 2016Article
- A genome-wide analysis of antimicrobial effector genes and their transcription patterns in Manduca sexta.Insect biochemistry and molecular biology · 2015Article
- Insect antimicrobial peptides and their applications.Applied microbiology and biotechnology · 2014Review
- Gloverins of the silkworm Bombyx mori: structural and binding properties and activities.Insect biochemistry and molecular biology · 2013Article
- Functional analysis of two lebocin-related proteins from Manduca sexta.Insect biochemistry and molecular biology · 2012Article
- Pyrosequencing-based expression profiling and identification of differentially regulated genes from Manduca sexta, a lepidopteran model insect.Insect biochemistry and molecular biology · 2011Article
- Article
- Functional analysis of four processing products from multiple precursors encoded by a lebocin-related gene from Manduca sexta.Developmental and comparative immunology · 2010Article
- Immunity in lepidopteran insects.Advances in experimental medicine and biology · 2010Review
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
In response to wounding or infection, insects produce a battery of antimicrobial peptides (AMPs) and other defense molecules to kill the invading pathogens. To study their structures, functions, and transcriptional regulation, we synthesized Manduca sexta moricin, a 42-residue peptide (GKIPVKAIKQAGKVIGKGLRAINIAGTTHDVVSFFRPKKKKH, 4539 Da). The compound exhibited potent antimicrobial activities against a broad spectrum of Gram-positive and Gram-negative bacteria with a minimum inhibitory concentration of 1.4 microM. The mRNA levels of M. sexta moricin increased substantially in fat body and hemocytes after the larvae were challenged with bacterial cells. We determined the solution structure of this AMP by two-dimensional 1H-1H -nuclear magnetic resonance spectroscopy. The tertiary structure is composed of an eight-turn alpha-helix spanning almost the entire peptide. Insights of relationships between the structure and function are also presented.
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