ArticleMolecular immunology2008
A novel ML protein from Manduca sexta may function as a key accessory protein for lipopolysaccharide signaling.
Article in Molecular immunology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 21 citations in OpenAlex.
- Article
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- Identification and functional characterization of the npc-2-like domain containing rust effector protein that suppresses cell death in plants.Molecular biology reports · 2024Article
- Identification and Expression Analysis of Phosphatidylinositol Transfer Proteins Genes in Rice.Plants (Basel, Switzerland) · 2023Article
- Transcriptome Analysis Reveals Early Hemocyte Responses upon In Vivo Stimulation with LPS in the Stick InsectInsects · 2022Article
- An MD-2-related lipid-recognition protein is required for insect reproduction and integument development.Open biology · 2021Article
- Toll9 fromProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Borrelia burgdorferi infection modifies protein content in saliva of Ixodes scapularis nymphs.BMC genomics · 2021Article
- The immune signaling pathways of Manduca sexta.Insect biochemistry and molecular biology · 2015Article
- Comparative analysis of the secretome from a model filarial nematode (Litomosoides sigmodontis) reveals maximal diversity in gravid female parasites.Molecular & cellular proteomics : MCP · 2014Article
- Drosophila melanogaster NPC2 proteins bind bacterial cell wall components and may function in immune signal pathways.Insect biochemistry and molecular biology · 2012Article
- Lipoteichoic acid and lipopolysaccharide can activate antimicrobial peptide expression in the tobacco hornworm Manduca sexta.Developmental and comparative immunology · 2010Article
- Leureptin: a soluble, extracellular leucine-rich repeat protein from Manduca sexta that binds lipopolysaccharide.Insect biochemistry and molecular biology · 2010Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Lipopolysaccharide (LPS) present on the outer membrane of Gram-negative bacteria is one of the most important pathogen-associated molecular patterns and a potent elicitor in innate immunity. In human, TLR4 (Toll-like receptor 4) and MD-2 (myeloid differiation-2) form a receptor complex to transduce the LPS signal into cells. However, in invertebrates, receptors that recognize LPS have not been determined. Here we report the purification, characterization and cDNA cloning of an ML (MD-2-related lipid-recognition) protein from the tobacco hornworm Manduca sexta. The full-length cDNA of this M. sexta ML protein, named MsML-1, is 532bp with an open reading frame of 456bp that encodes a polypeptide of 151 amino acids containing an ML domain. MsML-1 is a secreted glycoprotein and its mRNA is expressed in fat body and hemocytes. The expression level of MsML-1 mRNA in fat body and hemocytes as well as MsML-1 protein in hemolymph are not induced by immune challenge. Recombinant MsML-1 protein specifically binds to LPS from several Gram-negative bacteria and LPS Re mutant, as well as to lipid A, but not to KDO (2-keto-3-deoxyoctonate). Our results suggest that MsML-1 may function as a key accessory protein for LPS signaling in M. sexta against Gram-negative bacterial infection.
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