A pore-forming haemolysin from the hookworm, Ancylostoma caninum

Don, Tegan A., Jones, Malcolm K., Smyth, Danielle, O'Donoghue, Peter, Hotez, Peter and Loukas, Alex (2004) A pore-forming haemolysin from the hookworm, Ancylostoma caninum. International Journal For Parasitology, 34 9: 1029-1035. doi:10.1016/j.ijpara.2004.04.013

Author Don, Tegan A.
Jones, Malcolm K.
Smyth, Danielle
O'Donoghue, Peter
Hotez, Peter
Loukas, Alex
Title A pore-forming haemolysin from the hookworm, Ancylostoma caninum
Journal name International Journal For Parasitology   Check publisher's open access policy
ISSN 0020-7519
Publication date 2004
Sub-type Article (original research)
DOI 10.1016/j.ijpara.2004.04.013
Volume 34
Issue 9
Start page 1029
End page 1035
Total pages 7
Place of publication Oxford
Publisher Elsevier
Collection year 2004
Language eng
Subject C1
320405 Medical Parasitology
730101 Infectious diseases
270308 Microbial Systematics, Taxonomy and Phylogeny
Abstract Hookworms feed on blood, but the mechanism by which they lyse ingested erythrocytes is unknown. Here we show that Ancylostoma caninum, the common dog hookworm, expresses a detergent soluble, haemolytic factor. Activity was identified in both adult and larval stages, was heat-stable and unaffected by the addition of protease inhibitors, metal ions, chelators and reducing agents. Trypsin ablated lysis indicating that the haemolysin is a protein. A closely migrating doublet of hookworm proteins with apparent molecular weights of 60-65 kDa bound to the erythrocyte membrane after lysis of cells using both unlabeled and biotinylated detergent-solubilised hookworm extracts. In addition, separation of detergent-soluble parasite extracts using strong cation-exchange chromatography, resulted in purification of 60-65 kDa proteins with trypsin-sensitive haemolytic activity. Erythrocytes lysed with particulate, buffer-insoluble worm extracts were observed using scanning electron microscopy and appeared as red cell ghosts with approximately 100 nm diameter pores formed in the cell membranes. Red blood cell ghosts remained visible indicating that lysis was likely caused by pore formation and followed by osmotic disruption of the cell. (C) 2004 Australian Society for Parasitology Inc. Published by Elsevier Ltd. All rights reserved.
Keyword Parasitology
Ancylostoma Caninum
Human Hemoglobin
Q-Index Code C1

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Created: Wed, 15 Aug 2007, 03:57:00 EST