ArticleInsect biochemistry and molecular biology2012
Functional analysis of two lebocin-related proteins from Manduca sexta.
Article in Insect biochemistry and molecular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 39 citations in OpenAlex.
- Proline-Rich Antimicrobial Peptides from Invertebrates.Molecules (Basel, Switzerland) · 2024Review
- Insect Antimicrobial Peptides as Guardians of Immunity and Beyond: A Review.International journal of molecular sciences · 2024Review
- Diversity of Antimicrobial Peptides in Silkworm.Life (Basel, Switzerland) · 2023Review
- The plant toxin 4-methylsulfinylbutyl isothiocyanate decreases herbivore performance and modulates cellular and humoral immunity.PloS one · 2023Article
- Prediction and bioactivity of small-molecule antimicrobial peptides fromFrontiers in microbiology · 2023Article
- A Toll-Spätzle Pathway in the Immune Response ofInsects · 2020Article
- Molecular Cloning, Bioinformatic Analysis, and Expression ofBioMed research international · 2017Article
- Characterization and regulation of expression of an antifungal peptide from hemolymph of an insect, Manduca sexta.Developmental and comparative immunology · 2016Article
- Diversity, evolution and medical applications of insect antimicrobial peptides.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2016Review
- Co-expression of Dorsal and Rel2 Negatively Regulates Antimicrobial Peptide Expression in the Tobacco Hornworm Manduca sexta.Scientific reports · 2016Article
- Molecular cloning and characterization of gloverin from the diamondback moth, Plutella xylostella L. and its interaction with bacterial membrane.World journal of microbiology & biotechnology · 2015Article
- A genome-wide analysis of antimicrobial effector genes and their transcription patterns in Manduca sexta.Insect biochemistry and molecular biology · 2015Article
- Characterization of a novel Manduca sexta beta-1, 3-glucan recognition protein (βGRP3) with multiple functions.Insect biochemistry and molecular biology · 2014Article
- Insect antimicrobial peptides and their applications.Applied microbiology and biotechnology · 2014Review
- Article
- Manduca sexta gloverin binds microbial components and is active against bacteria and fungi.Developmental and comparative immunology · 2012Article
- A Toll-Spätzle pathway in the tobacco hornworm, Manduca sexta.Insect biochemistry and molecular biology · 2012Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Insects produce a group of antimicrobial peptides (AMPs) in response to microbial infections. Most AMPs are synthesized as inactive precursors/pro-proteins and require proteolytic processing to generate small active peptides. Here we report identification and functional analysis of two lebocin-related proteins (Leb-B and Leb-C) from the tobacco hornworm, Manduca sexta. The mRNA levels of Leb-B and Leb-C increased significantly in larval fat body and hemocytes after injection of Escherichia coli, Micrococcus luteus and Saccharomyces cerevisiae. Western blotting using rabbit polyclonal antibody to Leb-B showed accumulation of large protein(s) and small peptide(s) in larval hemolymph after microbial injection. This result and the presence of RXXR motifs in the deduced amino acid sequences led to our postulation that Leb-B/C may be inactive precursors that are processed in larval hemolymph to generate short active peptides. To test this hypothesis, we expressed and purified full-length and various fragments of Leb-B and Leb-C as thioredoxin (TRX) fusion proteins. We found that fusion proteins could be cleaved by induced larval plasma, and the cleavage sites were determined by protein sequencing. Antibacterial activity of peptide fragments was also verified using synthetic peptides, and active M. sexta lebocin peptides were located at the N-termini of Leb-B/C, which are different from Bombyx mori lebocins 1-4 that are located close to the C-termini. In addition, we found that synthetic Leb-B(22-48) peptide not only had higher antibacterial activity but also caused agglutination of E. coli cells. Our results provide valuable information for studying processing of lebocin precursors in lepidopteran insects.
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