Characterization of the α-helix region in domain 3 of the haemolytic lectin CEL-III: Implications for self-oligomerization and haemolytic processes

Journal of Biochemistry

Volumn 143, Issue 1, 2008, Pages 79-86

  Hisamatsu, Keigo ^a   Tsuda, Nobuaki ^a   Goda, Shuichiro ^a   Hatakeyama, Tomomitsu ^a  

^a NAGASAKI UNIVERSITY   (Japan)

Author keywords

Antibacterial peptide; Ca2+ dependent lectin; Haemolysin; Oligomerization; Small angle X ray scattering

Indexed keywords

GLUTATHIONE TRANSFERASE; LECTIN; SYNTHETIC PEPTIDE; VALINE;

ALPHA HELIX; AMINO ACID SEQUENCE; ANTIBACTERIAL ACTIVITY; ARTICLE; BACILLUS SUBTILIS; BACTERIAL MEMBRANE; CELL MEMBRANE PERMEABILITY; GENE MUTATION; HEMOLYSIS; NONHUMAN; OLIGOMERIZATION; PEPTIDE SYNTHESIS; PROTEIN DOMAIN; STAPHYLOCOCCUS AUREUS;

AMINO ACID SEQUENCE; ANTI-BACTERIAL AGENTS; HEMOLYTIC AGENTS; LECTINS; MOLECULAR SEQUENCE DATA; MUTATION; PEPTIDES; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT FUSION PROTEINS; SCATTERING, SMALL ANGLE; X-RAY DIFFRACTION;

BACILLUS SUBTILIS; BACTERIA (MICROORGANISMS); LOTUS; STAPHYLOCOCCUS AUREUS;

EID: 38849152190     PISSN: 0021924X     EISSN: 17562651     Source Type: Journal    
DOI: 10.1093/jb/mvm195     Document Type: Article

References (22)

1. 2+-dependent lectins from the marine invertebrate, Cucumaria echinata. J. Biochem. 116, 209-214
2. Oda, T., Tsuru, M., Hatakeyama, T., Nagatomo, H., Muramatsu, T., and Yamasaki, N. (1997) Temperature-and pH-dependent cytotoxic effect of the hemolytic lectin CEL-III from the marine invertebrate Cucumaria echinata on various cell lines. J. Biochem. 121, 560-567
3. Hatakeyama, T., Furukawa, M., Nagatomo, H., Yamasaki, N., and Mori, T. (1996) Oligomerization of the hemolytic lectin CEL-III from the marine invertebrate Cucumaria echinata induced by the binding of carbohydrate ligands. J. Biol. Chem. 271, 16915-16920
4. Hatakeyama, T., Nagatomo, H., and Yamasaki, N. (1995) Interaction of the hemolytic lectin CEL-III from the marine invertebrate Cucumaria echinata with the erythrocyte membrane. J. Biol. Chem. 270, 3560-3564
5. Uchida, T., Yamasaki, T., Eto, S., Sugawara, H., Kurisu, G., Nakagawa, A., Kusunoki, M., and Hatakeyama, T. (2004) Crystal structure of the hemolytic lectin CEL-III isolated from the marine invertebrate Cucumaria echinata: implications of domain structure for its membrane pore-formation mechanism. J. Biol. Chem. 279, 37133-37141
6. Rutenber, E. (1991) Structure of ricin B-chain at 2.5 Å resolution. Proteins 10, 260-269
7. Kouzuma, Y., Suzuki, Y., Nakano, M., Matsuyama, K., Tojo, S., Kimura, M., Yamasaki, T., Aoyagi, H., and Hatakeyama, T. (2003) Characterization of functional domains of the hemolytic lectin CEL-III from the marine invertebrate Cucumaria echinata. J. Biochem. 134, 395-402
8. Hatakeyama, T., Suenaga, T., Eto, S., Niidome, T., and Aoyagi, H. (2004) Antibacterial activity of peptides derived from the C-terminal region of a hemolytic lectin, CEL-III, from the marine invertebrate Cucumaria echinata. J. Biochem. 135, 65-70
9. Nakano, M., Tabata, S., Sugihara, K., Kouzuma, Y., Kimura, M., and Yamasaki, N. (1999) Primary structure of hemolytic lectin CEL-III from marine invertebrate Cucumaria echinata and its cDNA: structural similarity to the B-chain from plant lectin, ricin. Biochim. Biophys. Acta 1435, 167-176
10. Leppla, S. (2006) Bacillus anthracis toxins, in The Comprehensive Sourcebook of Bacterial Protein Toxins, (Alouf, J. and Popof, M., eds.) 3rd edn., pp. 323-347, Academic Press, New York
11. Fields, G.B. (1990) Solid phase peptide synthesis utilizing 9-fluorenylmethoxycarbonyl amino acids. Int. J. Pept. Protein Res. 35, 161-214
12. Yoshida, K., Mukai, Y., Niidome, T., Takashi, C., Tokunaga, Y., Hatakeyama, T., and Aoyagi, H. (2001) Interaction of pleurocidin and its analogs with phospholipid membrane and their antibacterial activity. J. Pept. Res. 57, 119-126
13. Pellegrini, A., Dettling, C., Thomas, U., and Hunziker, P. (2001) Isolation and characterization of four bactericidal domains in the bovine β-lactoglobulin. Biochem. Biophys. Acta 1526, 131-140
14. Hiragi, Y., Seki, Y., Ichimura, K., and Soda, K. (2002) Direct detection of the protein quaternary structure and denatured entity by small-angle scattering: guanidine hydrochloride denaturation of chaperonin protein GroEL. J. Appl. Cryst. 35, 1-7
15. Guinier, A. (1955) Small-Angle Scattering of X-Rays. Chapman & Hall, New York
16. Lim, K., Ho, J.X., Keeling, K., Gilliland, G.L., Ji, X., Ruker, F., and Carter, D.C. (1994) Three-dimensional structure of Schistosoma japonicum glutathione S-transferase fused with a six-amino acid conserved neutralizing epitope of gp41 from HIV. Protein Sci. 3, 2233-2244
17. Ohmori, N., Niidome, T., Hatakeyama, T., Mihara, H., and Aoyagi, H. (1998) Interaction of α-helical peptides with phospholipid membrane: effects of chain length and hydrophobicity of peptides. J. Peptide Res. 51, 103-109
18. Tossi, A., Sandri, L., and Giangaspero, A. (2000) Amphipathic, α-helical antimicrobial peptides. Biopolymers 55, 4-30
19. Saberwal, G. (1994) Cell-lytic and antibacterial peptides that act by perturbing the barrier function of membranes: facets of their conformational features, structure-function correlations and membrane-perturbing abilities. Biochim. Biophys. Acta 1197, 109-131
20. Fujisawa, T., Kuwahara, H., Hiromasa, Y., Niidome, T., Aoyagi, H., and Hatakeyama, T. (1997) Small-angle X-ray scattering study on CEL-III, a hemolytic lectin from Holothuroidea Cucumaria echinata, and its oligomer induced by the binding of specific carbohydrate. FEBS Lett. 414, 79-83
21. Song, L., Hobaugh, M.R., Shustak, C., Cheley, S., Bayley, H., and Gouaux, J.E. (1996) Structure of staphylococcal α-hemolysin, a heptameric transmembrane pore. Science 274, 1859-1866
22. Kajiwara, K. (1996) Structure analysis by small-angle X-ray scattering, in Applications of Synchrotron Radiation to Material Analysis (Saisho, H. and Goshi, Y., eds.) Elsevier Science, Amsterdam