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C-type lectin-like carbohydrate recognition of the hemolytic lectin CEL-III containing ricin-type -trefoil folds.

Hatakeyama T, Unno H, Kouzuma Y, Uchida T, Eto S, Hidemura H, Kato N, Yonekura M, Kusunoki M
J Biol Chem 282 37826-35 (2007)
Cited: 22 times
EuropePMC logo PMID: 17977832

Abstract

CEL-III is a Ca(2+)-dependent hemolytic lectin, isolated from the marine invertebrate Cucumaria echinata. The three-dimensional structure of CEL-III/GalNAc and CEL-III/methyl alpha-galactoside complexes was solved by x-ray crystallographic analysis. In these complexes, five carbohydrate molecules were found to be bound to two carbohydrate-binding domains (domains 1 and 2) located in the N-terminal 2/3 portion of the polypeptide and that contained beta-trefoil folds similar to ricin B-chain. The 3-OH and 4-OH of bound carbohydrate molecules were coordinated with Ca(2+) located at the subdomains 1alpha, 1gamma, 2alpha, 2beta, and 2gamma, simultaneously forming hydrogen bond networks with nearby amino acid side chains, which is similar to carbohydrate binding in C-type lectins. The binding of carbohydrates was further stabilized by aromatic amino acid residues, such as tyrosine and tryptophan, through a stacking interaction with the hydrophobic face of carbohydrates. The importance of amino acid residues in the carbohydrate-binding sites was confirmed by the mutational analyses. The orientation of bound GalNAc and methyl alpha-galactoside was similar to the galactose moiety of lactose bound to the carbohydrate-binding site of the ricin B-chain, although the ricin B-chain does not require Ca(2+) ions for carbohydrate binding. The binding of the carbohydrates induced local structural changes in carbohydrate-binding sites in subdomains 2alpha and 2beta. Binding of GalNAc also induced a slight change in the main chain structure of domain 3, which could be related to the conformational change upon binding of specific carbohydrates to induce oligomerization of the protein.

Reviews - 2z48 mentioned but not cited (1)

  1. Functional Diversity of Novel Lectins with Unique Structural Features in Marine Animals. Hatakeyama T, Unno H. Cells 12 1814 (2023)

Articles - 2z48 mentioned but not cited (3)

  1. Hemolytic lectin CEL-III heptamerizes via a large structural transition from α-helices to a β-barrel during the transmembrane pore formation process. Unno H, Goda S, Hatakeyama T. J Biol Chem 289 12805-12812 (2014)
  2. Crystallization and preliminary crystallographic study of oligomers of the haemolytic lectin CEL-III from the sea cucumber Cucumaria echinata. Unno H, Hisamatsu K, Nagao T, Tateya Y, Matsumoto N, Goda S, Hatakeyama T. Acta Crystallogr Sect F Struct Biol Cryst Commun 69 416-420 (2013)
  3. Novel carbohydrate-recognition mode of the invertebrate C-type lectin SPL-1 from Saxidomus purpuratus revealed by the GlcNAc-complex crystal in the presence of Ca2. Unno H, Higuchi S, Goda S, Hatakeyama T. Acta Crystallogr F Struct Biol Commun 76 271-277 (2020)


Reviews citing this publication (1)

  1. Sugar recognition and protein-protein interaction of mammalian lectins conferring diverse functions. Nagae M, Yamaguchi Y. Curr Opin Struct Biol 34 108-115 (2015)

Articles citing this publication (17)

  1. Structural basis of the preferential binding for globo-series glycosphingolipids displayed by Pseudomonas aeruginosa lectin I. Blanchard B, Nurisso A, Hollville E, Tétaud C, Wiels J, Pokorná M, Wimmerová M, Varrot A, Imberty A. J Mol Biol 383 837-853 (2008)
  2. Identification of a unique ganglioside binding loop within botulinum neurotoxins C and D-SA . Karalewitz AP, Kroken AR, Fu Z, Baldwin MR, Kim JJ, Barbieri JT. Biochemistry 49 8117-8126 (2010)
  3. An insight into the sialotranscriptome of the West Nile mosquito vector, Culex tarsalis. Calvo E, Sanchez-Vargas I, Favreau AJ, Barbian KD, Pham VM, Olson KE, Ribeiro JM. BMC Genomics 11 51 (2010)
  4. Structure and mode of action of a mosquitocidal holotoxin. Treiber N, Reinert DJ, Carpusca I, Aktories K, Schulz GE. J Mol Biol 381 150-159 (2008)
  5. What Is IL-1 for? The Functions of Interleukin-1 Across Evolution. Boraschi D. Front Immunol 13 872155 (2022)
  6. Molecular diversity of the two sugar-binding sites of the β-trefoil lectin HA33/C (HA1) from Clostridium botulinum type C neurotoxin. Nakamura T, Tonozuka T, Ito S, Takeda Y, Sato R, Matsuo I, Ito Y, Oguma K, Nishikawa A. Arch Biochem Biophys 512 69-77 (2011)
  7. Galactose recognition by a tetrameric C-type lectin, CEL-IV, containing the EPN carbohydrate recognition motif. Hatakeyama T, Kamiya T, Kusunoki M, Nakamura-Tsuruta S, Hirabayashi J, Goda S, Unno H. J Biol Chem 286 10305-10315 (2011)
  8. The carbohydrate-binding promiscuity of Euonymus europaeus lectin is predicted to involve a single binding site. Agostino M, Velkov T, Dingjan T, Williams SJ, Yuriev E, Ramsland PA. Glycobiology 25 101-114 (2015)
  9. Isolation and identification of mannose-binding proteins and estimation of their abundance in sera from hepatocellular carcinoma patients. Yang G, Chu W, Zhang H, Sun X, Cai T, Dang L, Wang Q, Yu H, Zhong Y, Chen Z, Yang F, Li Z. Proteomics 13 878-892 (2013)
  10. Identification of the Ricin-B-Lectin LdRBLk in the Colorado Potato Beetle and an Analysis of Its Expression in Response to Fungal Infections. Rotskaya UN, Kryukov VY, Kosman E, Tyurin M, Glupov VV. J Fungi (Basel) 7 364 (2021)
  11. Identification of the amino acid residues involved in the hemolytic activity of the Cucumaria echinata lectin CEL-III. Hisamatsu K, Nagao T, Unno H, Goda S, Hatakeyama T. Biochim Biophys Acta 1830 4211-4217 (2013)
  12. In silico prediction of molecular mechanisms of toxicity mediated by the leptospiral PF07598 gene family-encoded virulence-modifying proteins. Chaurasia R, Vinetz JM. Front Mol Biosci 9 1092197 (2022)
  13. A lytic mechanism based on soluble phospholypases A2 (sPLA2) and β-galactoside specific lectins is exerted by Ciona intestinalis (ascidian) unilocular refractile hemocytes against K562 cell line and mammalian erythrocytes. Arizza V, Parrinello D, Cammarata M, Vazzana M, Vizzini A, Giaramita FT, Parrinello N. Fish Shellfish Immunol 30 1014-1023 (2011)
  14. Effects of Ca2+ on refolding of the recombinant hemolytic lectin CEL-III. Hisamatsu K, Unno H, Goda S, Hatakeyama T. Biosci Biotechnol Biochem 73 1203-1205 (2009)
  15. Effects of amino acid mutations in the pore-forming domain of the hemolytic lectin CEL-III. Nagao T, Masaki R, Unno H, Goda S, Hatakeyama T. Biosci Biotechnol Biochem 80 1966-1969 (2016)
  16. Molecular cloning, functional expression, and characterization of isolectin genes of hemolytic lectin CEL-III from the marine invertebrate Cucumaria echinata. Shimizu Y, Yamazaki H, Yoshida S, Yonekura M, Kouzuma Y. Biosci Biotechnol Biochem 76 276-282 (2012)
  17. Structural and biochemical analysis of family 92 carbohydrate-binding modules uncovers multivalent binding to β-glucans. Hao MS, Mazurkewich S, Li H, Kvammen A, Saha S, Koskela S, Inman AR, Nakajima M, Tanaka N, Nakai H, Brändén G, Bulone V, Larsbrink J, McKee LS. Nat Commun 15 3429 (2024)


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