Mechanism study on a new antimicrobial peptide Sphistin derived from the N-terminus of crab histone H2A identified in haemolymphs of Scylla paramamosain
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- 作者：Bei Chena ; 1 ; Dan-Qing Fana ; 1 ; Ke-Xin Zhua ; Zhong-Guo Shana ; Fang-Yi Chena ; Lin Houa ; Ling Caia ; Ke-Jian Wanga ; b ; c ; wkjian@xmu.edu.cn" class="auth_mail" title="E-mail the corresponding author
- 关键词：Scylla paramamosain ; Histone ; Sphistin ; Antimicrobial activity ; Antimicrobial mechanism ; Cytotoxicity
- 刊名：Fish & Shellfish Immunology
- 出版年：2015
- 出版时间：December 2015
- 年：2015
- 卷：47
- 期：2
- 页码：833-846
- 全文大小：4664 K
文摘
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A new histone-derived AMP Sphistin identified from haemolymphs of mud crab.
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Sphistin exhibited strong antimicrobial activities against bacteria and yeast.
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Sphistin caused adsorption and permeabilization of bacterial cell membrane.
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Sphistin binded to LPS and LTA in a concentration dependent manner.
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Sphistin did not display toxicity towards either mammal or crab normal cells.