scholarly journals Molecular and pharmacological characterization of an acetylcholine-gated chloride channel (ACC-2) from the parasitic nematode Haemonchus contortus

2018 ◽  
Vol 8 (3) ◽  
pp. 518-525 ◽  
Author(s):  
Sarah A. Habibi ◽  
Micah Callanan ◽  
Sean G. Forrester
Keyword(s):  
Chloride Channel ◽  
Haemonchus Contortus ◽  
Parasitic Nematode ◽  
Pharmacological Characterization

scholarly journals Characterization of a secreted cystatin of the parasitic nematode Haemonchus contortus and its immune-modulatory effect on goat monocytes

2017 ◽  
Vol 10 (1) ◽  
Author(s):  
Yujian Wang ◽  
Lingyan Wu ◽  
Xinchao Liu ◽  
Shuai Wang ◽  
Muhammad Ehsan ◽  
...  
Keyword(s):  
Haemonchus Contortus ◽  
Parasitic Nematode

Molecular characterization of a family of metalloendopeptidases from the intestinal brush border of Haemonchus contortus

Parasitology ◽  
2006 ◽  
Vol 133 (3) ◽  
pp. 357-368 ◽  
Author(s):  
G. F. J. NEWLANDS ◽  
P. J. SKUCE ◽  
A. J. NISBET ◽  
D. L. REDMOND ◽  
S. K. SMITH ◽  
...  
Keyword(s):  
Haemonchus Contortus ◽  
Proteomic Analysis ◽  
Parasitic Nematode ◽  
Integral Membrane Protein ◽  
Cleavage Sites ◽  
Molecular Architecture ◽  
Intestinal Brush Border ◽  
Typical Type ◽  
Ph Range

Substantial protection against the economically important parasitic nematode Haemonchus contortus has been achieved by immunizing sheep with a glycoprotein fraction isolated from the intestinal membranes of the worm (H-gal-GP). Previous studies showed that one of the major components of H-gal-GP is a family of at least 4 zinc metalloendopeptidases, designated MEPs 1–4. This paper describes aspects of the molecular architecture of this protease family, including the proteomic analysis of the MEP fraction of the H-gal-GP complex. These enzymes belong to the M13 zinc metalloendopeptidase family (EC 3.4.24.11), also known as neutral endopeptidases or neprilysins. The sequences of MEPs 1 and 3 suggested a typical Type II integral membrane protein structure, whilst MEPs 2 and 4 had putative cleavable signal peptides, typical of secreted proteins. Proteomic analysis of H-gal-GP indicated that the extracellular domain of all 4 MEPs had been cleaved close to the transmembrane region/signal peptide with additional cleavage sites mid-way along the polypeptide. MEP3 was present as a homo-dimer in H-gal-GP, whereas MEP1 or MEP2 formed hetero-dimers with MEP4. It was found that expression of MEP3 was confined to developing 4th-stage larvae and to adult worms, the stages of Haemonchus which feed on blood. MEP-like activity was detected in the H-gal-GP complex over a broad pH range (5–9). Since all 4 MEPs must share a similar microenvironment in the complex, this suggests that each might have a different substrate specificity.

scholarly journals Investigating the function and possible biological role of an acetylcholine-gated chloride channel subunit (ACC-1) from the parasitic nematode Haemonchus contortus

2018 ◽  
Vol 8 (3) ◽  
pp. 526-533 ◽  
Author(s):  
Micah K. Callanan ◽  
Sarah A. Habibi ◽  
Wen Jing Law ◽  
Kristen Nazareth ◽  
Richard L. Komuniecki ◽  
...  
Keyword(s):  
Chloride Channel ◽  
Haemonchus Contortus ◽  
Parasitic Nematode ◽  
Biological Role

scholarly journals An Ivermectin-Sensitive Glutamate-Gated Chloride Channel from the Parasitic Nematode Haemonchus contortus

2009 ◽  
Vol 75 (6) ◽  
pp. 1347-1355 ◽  
Author(s):  
Samantha McCavera ◽  
Adrian T. Rogers ◽  
Darran M. Yates ◽  
Debra J. Woods ◽  
Adrian J. Wolstenholme
Keyword(s):  
Chloride Channel ◽  
Haemonchus Contortus ◽  
Parasitic Nematode
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