Early immunodiagnosis of fasciolosis in ruminants using recombinant Fasciola hepatica cathepsin L-like protease

2001 ◽  
Vol 31 (7) ◽  
pp. 728-737 ◽  
Author(s):  
Jan B.W.J Cornelissen ◽  
Cor P.H Gaasenbeek ◽  
Fred H.M Borgsteede ◽  
Wicher G Holland ◽  
Michiel M Harmsen ◽  
...  
Pathogens ◽  
2021 ◽  
Vol 10 (6) ◽  
pp. 725
Author(s):  
David Becerro-Recio ◽  
Javier González-Miguel ◽  
Alberto Ucero ◽  
Javier Sotillo ◽  
Álvaro Martínez-Moreno ◽  
...  

Excretory/secretory products released by helminth parasites have been widely studied for their diagnostic utility, immunomodulatory properties, as well as for their use as vaccines. Due to their location at the host/parasite interface, the characterization of parasite secretions is important to unravel the molecular interactions governing the relationships between helminth parasites and their hosts. In this study, the excretory/secretory products from adult worms of the trematode Fasciola hepatica (FhES) were employed in a combination of two-dimensional electrophoresis, immunoblot and mass spectrometry, to analyze the immune response elicited in sheep during the course of an experimental infection. Ten different immunogenic proteins from FhES recognized by serum samples from infected sheep at 4, 8, and/or 12 weeks post-infection were identified. Among these, different isoforms of cathepsin L and B, peroxiredoxin, calmodulin, or glutathione S-transferase were recognized from the beginning to the end of the experimental infection, suggesting their potential role as immunomodulatory antigens. Furthermore, four FhES proteins (C2H2-type domain-containing protein, ferritin, superoxide dismutase, and globin-3) were identified for the first time as non-immunogenic proteins. These results may help to further understand host/parasite relationships in fasciolosis, and to identify potential diagnostic molecules and drug target candidates of F. hepatica.


2000 ◽  
Vol 277 (1) ◽  
pp. 79-82 ◽  
Author(s):  
Susan J. Hawthorne ◽  
Maurice Pagano ◽  
David W. Halton ◽  
Brian Walker

1994 ◽  
Vol 223 (1) ◽  
pp. 91-98 ◽  
Author(s):  
Andrew J. DOWD ◽  
Angela M. SMITH ◽  
Sharon McGONIGLE ◽  
John P. DALTON

2004 ◽  
Vol 34 (6) ◽  
pp. 675-682 ◽  
Author(s):  
Michiel M. Harmsen ◽  
Jan B.W.J. Cornelissen ◽  
Herma E.C.M. Buijs ◽  
Wim J.A. Boersma ◽  
Suzan H.M. Jeurissen ◽  
...  

Animals ◽  
2021 ◽  
Vol 11 (12) ◽  
pp. 3495
Author(s):  
Tara Barbour ◽  
Krystyna Cwiklinski ◽  
Richard Lalor ◽  
John Pius Dalton ◽  
Carolina De Marco Verissimo

Fasciolosis caused by Fasciola hepatica is a major global disease of livestock and an important neglected helminthiasis of humans. Infection arises when encysted metacercariae are ingested by the mammalian host. Within the intestine, the parasite excysts as a newly excysted juvenile (NEJ) that penetrates the intestinal wall and migrates to the liver. NEJ excystment and tissue penetration are facilitated by the secretion of cysteine peptidases, namely, cathepsin B1 (FhCB1), cathepsin B2 (FhCB2), cathepsin B3 (FhCB3) and cathepsin L3 (FhCL3). While our knowledge of these peptidases is growing, we have yet to understand why multiple enzymes are required for parasite invasion. Here, we produced functional recombinant forms of these four peptidases and compared their physio-biochemical characteristics. Our studies show great variation of their pH optima for activity, substrate specificity and inhibitory profile. Carboxy-dipeptidase activity was exhibited exclusively by FhCB1. Our studies suggest that, combined, these peptidases create a powerful hydrolytic cocktail capable of digesting the various host tissues, cells and macromolecules. Although we found several inhibitors of these enzymes, they did not show potent inhibition of metacercarial excystment or NEJ viability in vitro. However, this does not exclude these peptidases as targets for future drug or vaccine development.


1993 ◽  
Vol 23 (8) ◽  
pp. 977-983 ◽  
Author(s):  
Angela M. Smith ◽  
Andrew J. Dowd ◽  
Mary Heffernan ◽  
Colin D. Robertson ◽  
John P. Dalton

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