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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)
Related entries: 3ah1, 3ah2, 3ah4, 3aj5

Cited: 17 times
EuropePMC logo PMID: 21640703

Abstract

A critical role in internalizing the Clostridium botulinum neurotoxin into gastrointestinal cells is played by nontoxic components complexed with the toxin. One of the components, a β-trefoil lectin has been known as HA33 or HA1. The HA33 from C. botulinum type A (HA33/A) has been predicted to have a single sugar-binding site, while type C HA33 (HA33/C) has two sites. Here we constructed HA33/C mutants and evaluated the binding capacities of the individual sites through mucin-assay and isothermal titration calorimetry. The mutant W176A (site I knockout) had a K(d) value of 31.5mM for galactose (Gal) and 61.3mM for N-acetylgalactosamine (GalNAc), while the K(d) value for N-acetylneuraminic acid (Neu5Ac) was too high to be determined. In contrast, the double mutant N278A/Q279A (site II knockout) had a K(d) value of 11.8mM for Neu5Ac. We also determined the crystal structures of wild-type and the F179I mutant in complex with GalNAc at site II. The results suggest that site I of HA33/C is quite unique in that it mainly recognizes Neu5Ac, and site II seems less important for the lectin specificity. The architectures and the properties of the sugar-binding sites of HA33/C and HA33/A were shown to be drastically different.

Articles - 3aj6 mentioned but not cited (1)

  1. Molecular assembly of botulinum neurotoxin progenitor complexes. Benefield DA, Dessain SK, Shine N, Ohi MD, Lacy DB. Proc Natl Acad Sci U S A 110 5630-5635 (2013)


Reviews citing this publication (6)

  1. Botulinum Neurotoxins: Biology, Pharmacology, and Toxicology. Pirazzini M, Rossetto O, Eleopra R, Montecucco C. Pharmacol Rev 69 200-235 (2017)
  2. Assembly and function of the botulinum neurotoxin progenitor complex. Gu S, Jin R. Curr Top Microbiol Immunol 364 21-44 (2013)
  3. Tables of Toxicity of Botulinum and Tetanus Neurotoxins. Rossetto O, Montecucco C. Toxins (Basel) 11 E686 (2019)
  4. Architecture of the botulinum neurotoxin complex: a molecular machine for protection and delivery. Lam KH, Jin R. Curr Opin Struct Biol 31 89-95 (2015)
  5. Structure and function of carbohydrate-binding module families 13 and 42 of glycoside hydrolases, comprising a β-trefoil fold. Fujimoto Z. Biosci Biotechnol Biochem 77 1363-1371 (2013)
  6. Botulinum neurotoxins: new questions arising from structural biology. Kammerer RA, Benoit RM. Trends Biochem Sci 39 517-526 (2014)

Articles citing this publication (10)

  1. Structure of a bimodular botulinum neurotoxin complex provides insights into its oral toxicity. Lee K, Gu S, Jin L, Le TT, Cheng LW, Strotmeier J, Kruel AM, Yao G, Perry K, Rummel A, Jin R. PLoS Pathog 9 e1003690 (2013)
  2. Crystal structure of Clostridium botulinum whole hemagglutinin reveals a huge triskelion-shaped molecular complex. Amatsu S, Sugawara Y, Matsumura T, Kitadokoro K, Fujinaga Y. J Biol Chem 288 35617-35625 (2013)
  3. High-resolution crystal structure of HA33 of botulinum neurotoxin type B progenitor toxin complex. Lee K, Lam KH, Kruel AM, Perry K, Rummel A, Jin R. Biochem Biophys Res Commun 446 568-573 (2014)
  4. Evolutionary relationships and expression analysis of EUL domain proteins in rice (Oryza sativa). De Schutter K, Tsaneva M, Kulkarni SR, Rougé P, Vandepoele K, Van Damme EJM. Rice (N Y) 10 26 (2017)
  5. Immunoprecipitation of native botulinum neurotoxin complexes from Clostridium botulinum subtype A strains. Lin G, Tepp WH, Bradshaw M, Fredrick CM, Johnson EA. Appl Environ Microbiol 81 481-491 (2015)
  6. Botulinum Neurotoxin Diversity from a Gene-Centered View. Benoit RM. Toxins (Basel) 10 E310 (2018)
  7. 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)
  8. Hemagglutinin gene shuffling among Clostridium botulinum serotypes C and D yields distinct sugar recognition of the botulinum toxin complex. Miyata K, Suzuki T, Hayashi S, Miyashita S, Ohyama T, Niwa K, Watanabe T, Sagane Y. Pathog Dis 73 ftv054 (2015)
  9. Structural studies on a non-toxic homologue of type II RIPs from bitter gourd: Molecular basis of non-toxicity, conformational selection and glycan structure. Chandran T, Sharma A, Vijayan M. J Biosci 40 929-941 (2015)
  10. Glycan detecting tools developed from the Clostridium botulinum whole hemagglutinin complex. Tulin EKC, Nakazawa C, Nakamura T, Saito S, Ohzono N, Hiemori K, Nakakita SI, Tateno H, Tonozuka T, Nishikawa A. Sci Rep 11 21973 (2021)


Related citations provided by authors (1)

  1. Sugar-binding sites of the HA1 subcomponent of Clostridium botulinum type C progenitor toxin.. Nakamura T, Tonozuka T, Ide A, Yuzawa T, Oguma K, Nishikawa A J Mol Biol 376 854-67 (2008)

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