Maximins S, a novel group of antimicrobial peptides from toad Bombina maxima

	Maximins S, a novel group of antimicrobial peptides from toad Bombina maxima
	Wang T 1,2; Zhang J 1,2; Shen JH 1,3; Jin Y 1; Lee WH 1; Zhang Y*1; zhangy@mail.kiz.ac.cn
	2005
发表期刊	BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
ISSN	0006-291X
卷号	327 期号:3 页码:945-951
合作性质	其它
摘要	Amphibian skin secretions are rich in antimicrobial peptides acting as important components of innate defense system against invading microorganisms. A novel type of peptide, designated as maximin S, was deduced by random sequencing of 793 clones from a constructed Bombina maxima skin cDNA library. The putative primary structures of maximin S peptides can be grouped into five species, in which maximin S1 has 14 amino acid residues and the rest of maximin S peptides (S2-S5) all have 18 amino acid residues. Unlike most of the amphibian antimicrobial peptides so far identified, the newly characterized four maximin S precursors are composed of maximin S1 and different combinations of tandem repeated maximin S2-S5 linked by internal peptides. Except maximin S1, the predicted secondary structures of maximin S2-S5 show a similar amphipathic alpha-helical structure. MALDI-TOF mass spectrometry analysis of partially isolated skin secretions of the toad indicates that most of the deduced maximin S peptides are expressed. Two deduced maximin S peptides (S1, S4) were synthesized and their antimicrobial activities were tested. Maximin S4 only had an antibiotic activity against mycoplasma and had no antibacterial or antifungal activity toward tested strains. Maximin S1 had no activity under the same conditions.
关键词	Amphibian Antimicrobial Peptide Antimycoplasma Bombina Maxima Cdna Sequence Maximin s Peptide
资助者	This work was supported by the grants of ‘‘Western Light’’ projects from The Chinese Academy of Sciences to Y. Zhang and W.H. Lee; and grants from National Natural Science Foundation (30170195, 30470380), and Yunnan Science and Technology Commission (2001C0061M, 2001C0062M, and 2003C0066M). ; This work was supported by the grants of ‘‘Western Light’’ projects from The Chinese Academy of Sciences to Y. Zhang and W.H. Lee; and grants from National Natural Science Foundation (30170195, 30470380), and Yunnan Science and Technology Commission (2001C0061M, 2001C0062M, and 2003C0066M). ; This work was supported by the grants of ‘‘Western Light’’ projects from The Chinese Academy of Sciences to Y. Zhang and W.H. Lee; and grants from National Natural Science Foundation (30170195, 30470380), and Yunnan Science and Technology Commission (2001C0061M, 2001C0062M, and 2003C0066M). ; This work was supported by the grants of ‘‘Western Light’’ projects from The Chinese Academy of Sciences to Y. Zhang and W.H. Lee; and grants from National Natural Science Foundation (30170195, 30470380), and Yunnan Science and Technology Commission (2001C0061M, 2001C0062M, and 2003C0066M).
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收录类别	SCI
语种	英语
资助者	This work was supported by the grants of ‘‘Western Light’’ projects from The Chinese Academy of Sciences to Y. Zhang and W.H. Lee; and grants from National Natural Science Foundation (30170195, 30470380), and Yunnan Science and Technology Commission (2001C0061M, 2001C0062M, and 2003C0066M). ; This work was supported by the grants of ‘‘Western Light’’ projects from The Chinese Academy of Sciences to Y. Zhang and W.H. Lee; and grants from National Natural Science Foundation (30170195, 30470380), and Yunnan Science and Technology Commission (2001C0061M, 2001C0062M, and 2003C0066M). ; This work was supported by the grants of ‘‘Western Light’’ projects from The Chinese Academy of Sciences to Y. Zhang and W.H. Lee; and grants from National Natural Science Foundation (30170195, 30470380), and Yunnan Science and Technology Commission (2001C0061M, 2001C0062M, and 2003C0066M). ; This work was supported by the grants of ‘‘Western Light’’ projects from The Chinese Academy of Sciences to Y. Zhang and W.H. Lee; and grants from National Natural Science Foundation (30170195, 30470380), and Yunnan Science and Technology Commission (2001C0061M, 2001C0062M, and 2003C0066M).
文献类型	期刊论文
条目标识符	http://ir.kiz.ac.cn/handle/152453/2683
专题	科研部门_生物毒素与人类疾病（张云）
通讯作者	zhangy@mail.kiz.ac.cn
作者单位	1.Department of Animal Toxinology, Kunming Institute of Zoology, The Chinese Academy of Sciences, Kunming, Yunnan 650223, China 2.Graduate School of The Chinese Academy of Sciences, Beijing 100039, China 3.The First Affiliated Hospital of Kunming Medical College, Kunming, Yunnan 650032, China
推荐引用方式 GB/T 7714	Wang T,Zhang J,Shen JH,et al. Maximins S, a novel group of antimicrobial peptides from toad Bombina maxima[J]. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS,2005,327(3):945-951.
APA	Wang T.,Zhang J.,Shen JH.,Jin Y.,Lee WH.,...&zhangy@mail.kiz.ac.cn.(2005).Maximins S, a novel group of antimicrobial peptides from toad Bombina maxima.BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS,327(3),945-951.
MLA	Wang T,et al."Maximins S, a novel group of antimicrobial peptides from toad Bombina maxima".BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS 327.3(2005):945-951.

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