{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Krishnan M"],"funding":["National Research Foundation of Korea"],"pagination":["e2115669119"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8915966"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["119(10)"],"pubmed_abstract":["SignificanceSimilar to mammalian TLR4/MD-2, the Toll9/MD-2-like protein complex in the silkworm, <i>Bombyx mori,</i> acts as an innate pattern-recognition receptor that recognizes lipopolysaccharide (LPS) and induces LPS-stimulated expression of antimicrobial peptides such as cecropins. Here, we report that papiliocin, a cecropin-like insect antimicrobial peptide from the swallowtail butterfly, competitively inhibits the LPS-TLR4/MD-2 interaction by directly binding to human TLR4/MD-2. Structural elements in papiliocin, which are important in inhibiting TLR4 signaling via direct binding, are highly conserved among insect cecropins, indicating that its TLR4-antagonistic activity may be related to insect Toll9-mediated immune response against microbial infection. This study highlights the po"],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pubmed_title":["Molecular mechanism underlying the TLR4 antagonistic and antiseptic activities of papiliocin, an insect innate immune response molecule."],"pmcid":["PMC8915966"],"funding_grant_id":["2020R1A2C2005338"],"pubmed_authors":["Jang A","Choi S","Yeon J","Krishnan M","Son K","Jeong MS","Kim Y","Choi J","Lee Y","Shin SY","Jang M"],"additional_accession":[]},"is_claimable":false,"name":"Molecular mechanism underlying the TLR4 antagonistic and antiseptic activities of papiliocin, an insect innate immune response molecule.","description":"SignificanceSimilar to mammalian TLR4/MD-2, the Toll9/MD-2-like protein complex in the silkworm, <i>Bombyx mori,</i> acts as an innate pattern-recognition receptor that recognizes lipopolysaccharide (LPS) and induces LPS-stimulated expression of antimicrobial peptides such as cecropins. Here, we report that papiliocin, a cecropin-like insect antimicrobial peptide from the swallowtail butterfly, competitively inhibits the LPS-TLR4/MD-2 interaction by directly binding to human TLR4/MD-2. Structural elements in papiliocin, which are important in inhibiting TLR4 signaling via direct binding, are highly conserved among insect cecropins, indicating that its TLR4-antagonistic activity may be related to insect Toll9-mediated immune response against microbial infection. This study highlights the po","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Mar","modification":"2025-04-04T20:24:00.53Z","creation":"2025-04-04T20:24:00.53Z"},"accession":"S-EPMC8915966","cross_references":{"pubmed":["35238667"],"doi":["10.1073/pnas.2115669119"]}}