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

Journal of Endotoxin Research

Volumn 8, Issue 6, 2002, Pages 437-439

  Kawabata, Shun Ichiro ^a   Tsuda, Ryoko ^a  

^a KYUSHU UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

BOVINE SERUM ALBUMIN; LECTIN;

BINDING SITE; CONFORMATIONAL TRANSITION; LIGAND BINDING; LIMULUS; MOLECULAR RECOGNITION; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN IMMOBILIZATION; PROTEIN INTERACTION; PROTEIN STRUCTURE; REVIEW; SURFACE PLASMON RESONANCE;

ANIMALS; BINDING SITES; BLOOD PROTEINS; HEMOCYTES; HEMOLYMPH; HORSESHOE CRABS; IMMUNITY; LECTINS; LIGANDS; MOLECULAR CONFORMATION;

BOVINAE; DECAPODA (CRUSTACEA); LIMULUS; MEROSTOMATA;

EID: 0036957758     PISSN: 09680519     EISSN: None     Source Type: Journal    
DOI: 10.1179/096805102125001037     Document Type: Review

References (15)

1. Saito T, Kawabata S, Hirata M, Iwanaga S. A novel type of Limulus lectin - L6. J Biol Chem 1995; 270: 14493-14499.
2. Okino N, Kawabata S, Saito T, Hirata M, Iwanaga S. Purification, characterization, and cDNA cloning of a 27-kDa lectin (L10) from horseshoe crab hemocytes. J Biol Chem 1995; 270: 31008-31015.
3. Saito T, Hatada M, Iwanaga S, Kawabata S. A newly identified horseshoe crab lectin with binding specificity to O-antigen of bacterial lipopolysaccharides. J Biol Chem 1997; 272: 30703-30708.
4. Inamori K, Saito T, Iwaki D et al. A newly identified horseshoe crab lectin with specificity for blood group A antigen recognizes specific O-antigens of bacterial lipopolysaccharides. J Biol Chem 1999; 274: 3272-3278.
5. Janeway Jr CA. Approaching the asymptote? Evolution and revolution in immunology. Cold Spring Harbor Symp Quant Biol 1989; 54: 1-13.
6. Gokudan S, Muta T, Tsuda R et al. Horseshoe crab acetyl group-recognizing lectins involved in innate immunity are structurally related to fibrinogen. Proc Natl Acad Sci USA 1999; 96: 10086-10091.
7. Kairies N, Beisel HG, Fuentes-Prior P et al. The 2-Å crystal structure of tachylectin 5A provides evidence for the common origin of the innate immunity and the blood coagulation systems. Proc Natl Acad Sci USA 2001; 98: 13519-13524.
8. Spraggon G, Everse SJ, Doolittle RF. Crystal structures of fragment D from human fibrinogen and its crosslinked counterpart from fibrin. Nature 1997; 389: 455-462.
9. Pratt KP, Cote HCF, Chung DW, Stenkamp RE, Davie EW. The primary fibrin polymerization pocket: three-dimensional structure of a 30-kDa C-terminal γ chain fragment complexed with the peptide Gly-Pro-Arg-Pro. Proc Natl Acad Sci USA 1997; 94: 7176-7181.
10. Beisel HG, Kawabata S, Iwanaga S, Huber R, Bode W. Tachylectin-2: crystal structure of a specific GlcNAc/Ga1NAc-binding lectin involved in the innate immunity host defense of the Japanese horseshoe crab Tachypleus tridentatus. EMBO J 1999; 18: 2312-2322.
11. Troy FA. Polysialylation: from bacteria to brains. Glycobiology 1992; 2: 2-23.
12. Reuter G, Gabius HJ. Sialic acid: structure-analysis-metabolism-occurrence-recognition. Biol Chem Hoppe-Seyler 1996; 377: 325-342.
13. Troy FA. The chemistry and biosynthesis of selected bacterial capsular polymers. Annu Rev Microbiol 1979; 33: 519-560.
14. Weis WI. Drickamer K. Structural basis of the lectin-carbohydrate recognition. Annu Rev Biochem 1996; 65: 441-473.
15. Fujita T. Evolution of the lectin-complement pathway and its role in innate immunity. Nat Rev Immunol 2002; 2: 346-353.