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A novel defensin-like peptide from salivary glands of the hard tick, Haemaphysalis longicornis

  1. Xiangyun Lu1,2,†,
  2. Qiaolin Che1,†,
  3. Yi Lv1,
  4. Meijuan Wang1,
  5. Zekuan Lu3,
  6. Feifei Feng3,
  7. Jingze Liu3,*,
  8. Haining Yu3,4,*

Article first published online: 21 DEC 2009

DOI: 10.1002/pro.317

Issue

Protein Science

Protein Science

Volume 19, Issue 3, pages 392–397, March 2010

Additional Information

How to Cite

Lu, X., Che, Q., Lv, Y., Wang, M., Lu, Z., Feng, F., Liu, J. and Yu, H. (2010), A novel defensin-like peptide from salivary glands of the hard tick, Haemaphysalis longicornis. Protein Science, 19: 392–397. doi: 10.1002/pro.317

Author Information

  1. 1

    Key Laboratory of Microbiological Engineering of Agricultural Environment, Life Sciences College of Nanjing Agricultural University, Ministry of Agriculture, Nanjing, Jiangsu, 210095 China

  2. 2

    Department of Life Science & Technology, Changshu Institute of Technology, Changshu, Jiangsu, 215500 China

  3. 3

    College of Life Sciences, Hebei Normal University, Shijiazhuang, Hebei, 050016 China

  4. 4

    Department of Bioscience and Biotechnology, Dalian University of Technology, Dalian, Liaoning, 116023 China

  1. †

    The first two authors share the same contribution to this paper

*College of Life Sciences, Hebei Normal University, Shijiazhuang, Hebei, 050016 China

Publication History

  1. Issue published online: 22 FEB 2010
  2. Article first published online: 21 DEC 2009
  3. Accepted manuscript online: 21 DEC 2009 12:00AM EST
  4. Manuscript Accepted: 8 DEC 2009
  5. Manuscript Revised: 6 DEC 2009
  6. Manuscript Received: 16 SEP 2009

Funded by

  • National Natural Science Foundation of China. Grant Number: 30670259
  • Natural Science Foundation of Hebei province. Grant Number: C2007000266

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Keywords:

  • tick;
  • antimicrobial peptide;
  • defensin;
  • salivary gland;
  • Haemaphysalis longicornis

Abstract

A novel defensin-like antimicrobial peptide named longicornsin was isolated from the salivary glands of the hard tick, Haemaphysalis longicornis, using a 10-kDa cut-off Centriprep filter and reversed-phase high-performance liquid chromatography (RP-HPLC). Its amino acid sequence was determined as DFGCGQGMIFMCQRRCMRLYPGSTGFCRGFRCMCDTHIPLRPPFMVG by Edman degradation. The cDNA encoding longicornsin was cloned by cDNA library screening. The predicted protein from the cDNA sequence was composed of 78 amino acids including a mature longicornsin. It showed similarity with defensin-like peptides from other ticks by BLAST search. Different from most other tick defensin-like peptides, longicornsin had a C-terminal extension. Purified longicornsin exerted potent antimicrobial activities against bacteria and fungi. Interestingly, it even showed strong antimicrobial ability against drug-resistant microorganisms and Helicobacter pylori. The results of this study indicated that longicornsin is a potential candidate for novel antimicrobial drug design.

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