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Toxins 2016, 8(8), 229; doi:10.3390/toxins8080229

Purification and Characterization of a Novel Kazal-Type Trypsin Inhibitor from the Leech of Hirudinaria manillensis

1
Department of Endocrine and breast Surgery, The First Affiliated Hospital of Chongqing Medical University, Chongqing 400016, China
2
Key Laboratory of Animal Models and Human Disease Mechanisms of Chinese Academy of Sciences & Yunnan Province, Kunming Institute of Zoology, Kunming 650223, China
3
Life Sciences College, Nanjing Agricultural University, Nanjing 210095, China
4
Sino-Africa Joint Research Center, Chinese Academy of Sciences, Kunming Institute of Zoology, Kunming 650223, Yunnan, China
5
Institute of Primate Research, P.O Box 24481, Nairobi, Kenya
These authors contributed equally to this work.
*
Authors to whom correspondence should be addressed.
Academic Editor: Andreimar M. Soares
Received: 14 April 2016 / Revised: 11 July 2016 / Accepted: 18 July 2016 / Published: 23 July 2016
(This article belongs to the Section Animal Venoms)
View Full-Text   |   Download PDF [2178 KB, uploaded 23 July 2016]   |  

Abstract

Kazal-type serine proteinase inhibitors are found in a large number of living organisms and play crucial roles in various biological and physiological processes. Although some Kazal-type serine protease inhibitors have been identified in leeches, none has been reported from Hirudinaria manillensis, which is a medically important leech. In this study, a novel Kazal-type trypsin inhibitor was isolated from leech H. manillensis, purified and named as bdellin-HM based on the sequence similarity with bdellin-KL and bdellin B-3. Structural analysis revealed that bdellin-HM was a 17,432.8 Da protein and comprised of 149 amino acid residues with six cysteines forming three intra-molecular disulfide bonds. Bdellin-HM showed similarity with the Kazal-type domain and may belong to the group of “non-classical” Kazal inhibitors according to its CysI-CysII disulfide bridge position. Bdellin-HM had no inhibitory effect on elastase, chymotrypsin, kallikrein, Factor (F) XIIa, FXIa, FXa, thrombin and plasmin, but it showed a potent ability to inhibit trypsin with an inhibition constant (Ki) of (8.12 ± 0.18) × 10−9 M. These results suggest that bdellin-HM from the leech of H. manillensis plays a potent and specific inhibitory role towards trypsin. View Full-Text
Keywords: Hirudinaria manillensis; Kazal-type trypsin inhibitor; bdellin; protease inhibitor Hirudinaria manillensis; Kazal-type trypsin inhibitor; bdellin; protease inhibitor
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MDPI and ACS Style

Lai, Y.; Li, B.; Liu, W.; Wang, G.; Du, C.; Ombati, R.; Lai, R.; Long, C.; Li, H. Purification and Characterization of a Novel Kazal-Type Trypsin Inhibitor from the Leech of Hirudinaria manillensis. Toxins 2016, 8, 229.

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