Molecular basis of non-self recognition by the horseshoe crab lectins. 2002

Shun-ichiro Kawabata, and Ryoko Tsuda
Department of Biology, Faculty of Sciences, Kyushu University, Fukuoka, Japan. skawascb@mbox.nc.kyushu-u.ac.jp

The target molecules of innate immunity are not proteins of direct gene products but the molecular arrays or patterns on pathogens, called pathogen-associated molecular patterns (PAMPs). The self/non-self discrimination by innate immunity through simple ligands universally expressed both on pathogens and hosts, such as monosaccharides and the acetyl group, probably depends on the density or clustering patterns of the ligands. The specific recognition by the horseshoe crab lectins, named tachylectins, with a propeller-like fold or a propeller-like oligomeric arrangement is reinforced by the short distance between the individual binding sites that interact with PAMPs. There is virtually no conformational change in the main or side chains of tachylectins upon binding with the ligands. This low structural flexibility of the propeller structures must be very important for specific interaction with PAMPs.

UI MeSH Term Description Entries
D007109 Immunity Nonsusceptibility to the invasive or pathogenic effects of foreign microorganisms or to the toxic effect of antigenic substances. Immune Process,Immune Response,Immune Processes,Immune Responses,Process, Immune,Response, Immune
D008024 Ligands A molecule that binds to another molecule, used especially to refer to a small molecule that binds specifically to a larger molecule, e.g., an antigen binding to an antibody, a hormone or neurotransmitter binding to a receptor, or a substrate or allosteric effector binding to an enzyme. Ligands are also molecules that donate or accept a pair of electrons to form a coordinate covalent bond with the central metal atom of a coordination complex. (From Dorland, 27th ed) Ligand
D008968 Molecular Conformation The characteristic three-dimensional shape of a molecule. Molecular Configuration,3D Molecular Structure,Configuration, Molecular,Molecular Structure, Three Dimensional,Three Dimensional Molecular Structure,3D Molecular Structures,Configurations, Molecular,Conformation, Molecular,Conformations, Molecular,Molecular Configurations,Molecular Conformations,Molecular Structure, 3D,Molecular Structures, 3D,Structure, 3D Molecular,Structures, 3D Molecular
D001798 Blood Proteins Proteins that are present in blood serum, including SERUM ALBUMIN; BLOOD COAGULATION FACTORS; and many other types of proteins. Blood Protein,Plasma Protein,Plasma Proteins,Serum Protein,Serum Proteins,Protein, Blood,Protein, Plasma,Protein, Serum,Proteins, Blood,Proteins, Plasma,Proteins, Serum
D006434 Hemocytes Any blood or formed element especially in invertebrates. Hemocyte
D006458 Hemolymph The blood/lymphlike nutrient fluid of some invertebrates. Hemolymphs
D006737 Horseshoe Crabs An arthropod subclass (Xiphosura) comprising the North American (Limulus) and Asiatic (Tachypleus) genera of horseshoe crabs. Crabs, Horseshoe,Limulus,Limulus polyphemus,Tachypleus,Xiphosura,Crab, Horseshoe,Horseshoe Crab,Xiphosuras
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D001665 Binding Sites The parts of a macromolecule that directly participate in its specific combination with another molecule. Combining Site,Binding Site,Combining Sites,Site, Binding,Site, Combining,Sites, Binding,Sites, Combining
D037102 Lectins Proteins that share the common characteristic of binding to carbohydrates. Some ANTIBODIES and carbohydrate-metabolizing proteins (ENZYMES) also bind to carbohydrates, however they are not considered lectins. PLANT LECTINS are carbohydrate-binding proteins that have been primarily identified by their hemagglutinating activity (HEMAGGLUTININS). However, a variety of lectins occur in animal species where they serve diverse array of functions through specific carbohydrate recognition. Animal Lectin,Animal Lectins,Isolectins,Lectin,Isolectin,Lectin, Animal,Lectins, Animal

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