A novel β-defensin structure: A potential strategy of big defensin for overcoming resistance by gram-positive bacteria

Takahide Kouno, Naoki Fujitani, Mineyuki Mizuguchi, Tsukasa Osaki, Shin Ichiro Nishimura, Shun-Ichiro Kawabata, Tomoyasu Aizawa, Makoto Demura, Katsutoshi Nitta, Keiichi Kawano

研究成果: Contribution to journalArticle査読

30 被引用数 (Scopus)

抄録

Big defensin is a 79-residue peptide derived from hemocytes of the Japanese horseshoe crab. It has antimicrobial activities against Gram-positive and -negative bacteria. The amino acid sequence of big defensin can be divided into an N-terminal hydrophobic half and a C-terminal cationic half. Interestingly, the trypsin cleaves big defensin into two fragments, the N-terminal and C-terminal fragments, which are responsible for antimicrobial activity against Gram-positive and -negative bacteria, respectively. To explore the antimicrobial mechanism of big defensin, we determined the solution structure of mature big defensin and performed a titration experiment with DPC micelles. Big defensin has a novel defensin structure; the C-terminal domain adopts a β-defensin structure, and the N-terminal domain forms a unique globular conformation. It is noteworthy that the hydrophobic N-terminal domain undergoes a conformational change in micelle solution, while the C-terminal domain remains unchanged. Here, we propose that the N-terminal domain achieves its antimicrobial activity in a novel fashion and explain that big defensin has developed a sttategy different from those of other β-defensins to suppress the growth of Gram-positive bacteria.

本文言語英語
ページ(範囲)10611-10619
ページ数9
ジャーナルBiochemistry
47
40
DOI
出版ステータス出版済み - 10 7 2008

All Science Journal Classification (ASJC) codes

  • 生化学

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