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


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Title: Characterization of the α-helix region in domain 3 of the haemolytic lectin CEL-III: implications for self-oligomerization and haemolytic processes.
Authors: Hisamatsu, Keigo / Tsuda, Nobuaki / Goda, Shuichiro / Hatakeyama, Tomomitsu
Issue Date: Jan-2008
Publisher: The Japanese Biochemical Society / 日本生化学会
Citation: Journal of biochemistry, 143(1), pp.79-86; 2008
Abstract: CEL-III is a haemolytic lectin, which has two beta-trefoil domains (domains 1 and 2) and a beta-sheet-rich domain (domain 3). In domain 3 (residues 284-432), there is a hydrophobic region containing two alpha-helices (H8 and H9, residues 317-357) and a loop between them, in which alternate hydrophobic residues, especially Val residues, are present. To elucidate the role of the alpha-helix region in the haemolytic process, peptides corresponding to different parts of this region were synthesized and characterized. The peptides containing the sequence that corresponded to the loop and second alpha-helix (H9) showed the strongest antibacterial activity for Staphylococcus aureus and Bacillus subtilis through a marked permeabilization of the bacterial cell membrane. The recombinant glutathione S-transferase (GST)-fusion proteins containing domain 3 or the alpha-helix region peptide formed self-oligomers, whereas mutations in the alternate Val residues in the alpha-helix region lead to decreased oligomerization ability of the fusion proteins. These results suggest that the alpha-helix region, particularly its alternate Val residues are important for oligomerization of CEL-III in target cell membranes, which is also required for a subsequent haemolytic action.
Keywords: Antibacterial peptide / Ca2+-dependent lectin / Haemolysin / Oligomerization / Small-angle X-ray scattering
URI: http://hdl.handle.net/10069/23015
ISSN: 0021924X
DOI: 10.1093/jb/mvm195
PubMed ID: 17965430
Rights: © 2007 The Japanese Biochemical Society.
Type: Journal Article
Text Version: author
Appears in Collections:Articles in academic journal

Citable URI : http://hdl.handle.net/10069/23015

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