Functional structure and antimicrobial activity of persulcatusin, an antimicrobial peptide from the hard tick Ixodes persulcatus

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• 作者：Naruhide Miyoshi ; Takeshi Saito ; Tadahiro Ohmura ; Kengo Kuroda…
• 关键词：Tick ; Antimicrobial peptide ; Persulcatusin ; S ; S bond ; Methicillin ; resistant Staphylococcus aureus
• 刊名：Parasites & Vectors
• 出版年：2016
• 出版时间：December 2016
• 年：2016
• 卷：9
• 期：1
• 全文大小：2,739 KB
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• 作者单位：Naruhide Miyoshi (1)
  Takeshi Saito (2)
  Tadahiro Ohmura (2)
  Kengo Kuroda (1)
  Kazumasa Suita (1)
  Kohei Ihara (1)
  Emiko Isogai (1)
  
  1. Department of Animal Microbiology, Graduate School of Agricultural Science, Tohoku University, 1-1 Tsutsumidori Amamiya-machi, Aoba-ku, Sendai, Miyagi, 981-8555, Japan
  2. Dassault Systemes Biovia K.K, Shinagawa-ku, Tokyo, Japan
  
• 刊物主题：Parasitology; Infectious Diseases; Tropical Medicine; Entomology;
• 出版者：BioMed Central
• ISSN：1756-3305

文摘

Background Antimicrobial peptides (AMPs) are considered promising candidates for the development of novel anti-infective agents. In arthropods such as ticks, AMPs form the first line of defense against pathogens in the innate immune response. Persulcatusin (IP) was found in the Ixodes persulcatus midgut, and its amino acid sequence was reported. However, the complete structure of IP has not been identified. We evaluated the relation between structural features and antimicrobial activity of IP, and its potential as a new anti-methicillin-resistant Staphylococcus aureus (MRSA) agent.