Serine protease inhibitors of parasitic helminths

Molehin, Adebayo J., Gobert, Geoffrey N. and McManus, Donald P. (2012) Serine protease inhibitors of parasitic helminths. Parasitology, 139 6: 681-695. doi:10.1017/S0031182011002435

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Author Molehin, Adebayo J.
Gobert, Geoffrey N.
McManus, Donald P.
Title Serine protease inhibitors of parasitic helminths
Journal name Parasitology   Check publisher's open access policy
ISSN 0031-1820
1469-8161
Publication date 2012-05
Sub-type Critical review of research, literature review, critical commentary
DOI 10.1017/S0031182011002435
Open Access Status
Volume 139
Issue 6
Start page 681
End page 695
Total pages 15
Place of publication Cambridge, United Kingdom
Publisher Cambridge University Press
Collection year 2013
Language eng
Formatted abstract
Serine protease inhibitors (serpins) are a superfamily of structurally conserved proteins that inhibit serine proteases and play key physiological roles in numerous biological systems such as blood coagulation, complement activation and inflammation. A number of serpins have now been identified in parasitic helminths with putative involvement in immune regulation and in parasite survival through interference with the host immune response. This review describes the serpins and smapins (small serine protease inhibitors) that have been identified in Ascaris spp., Brugia malayi, Ancylostoma caninum Onchocerca volvulus, Haemonchus contortus, Trichinella spiralis, Trichostrongylus vitrinus, Anisakis simplex, Trichuris suis, Schistosoma spp., Clonorchis sinensis, Paragonimus westermani and Echinococcus spp. and discusses their possible biological functions, including roles in host-parasite interplay and their evolutionary relationships.
Keyword Serine protease inhibitors
Serpins
Small serine protease inhibitors
Smapins biochemical characterization
Parasitic helminths
Leech Theromyzon-Tessulatum
Acid-Sequence Determination
Nematode Brugia-Malayi
Proteinase-Inhibitors
Anisakis-Simplex
Ascaris-Suum
Echinococcus-Granulosus
Schistosoma-Mansoni
Biological-Activity
Trypsin-Inhibitor
Q-Index Code CX
Q-Index Status Confirmed Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Critical review of research, literature review, critical commentary
Collections: Non HERDC
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Citation counts: TR Web of Science Citation Count  Cited 21 times in Thomson Reuters Web of Science Article | Citations
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