Comparison of cysteine peptidase activities in<i>Trichobilharzia regenti</i>and<i>Schistosoma mansoni</i>cercariae

Kašný, Martin; Mikeš, Libor; Dalton, John P.; Mountford, Adrian P.; Horák, Petr

doi:10.1017/s0031182007002910

Cited by 33 publications

(18 citation statements)

References 43 publications

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“…However, in another study, the reaction of antibodies raised against elastase of S. mansoni was observed neither with the penetration glands of T. szidati nor with the cercarial secretions on Western blots (180). In contrast, high activities of cysteine peptidases were noticed in induced cercarial secretions and homogenates for T. szidati and T. regenti (180,185). In addition, the presence of cercarial elastase in the latter species was not confirmed by screening of a cDNA library (186).…”

Section: Vertebrate Host Finding and Penetrationmentioning

confidence: 89%

Avian Schistosomes and Outbreaks of Cercarial Dermatitis

et al. 2015

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SUMMARY Cercarial dermatitis (swimmer's itch) is a condition caused by infective larvae (cercariae) of a species-rich group of mammalian and avian schistosomes. Over the last decade, it has been reported in areas that previously had few or no cases of dermatitis and is thus considered an emerging disease. It is obvious that avian schistosomes are responsible for the majority of reported dermatitis outbreaks around the world, and thus they are the primary focus of this review. Although they infect humans, they do not mature and usually die in the skin. Experimental infections of avian schistosomes in mice show that in previously exposed hosts, there is a strong skin immune reaction that kills the schistosome. However, penetration of larvae into naive mice can result in temporary migration from the skin. This is of particular interest because the worms are able to migrate to different organs, for example, the lungs in the case of visceral schistosomes and the central nervous system in the case of nasal schistosomes. The risk of such migration and accompanying disorders needs to be clarified for humans and animals of interest (e.g., dogs). Herein we compiled the most comprehensive review of the diversity, immunology, and epidemiology of avian schistosomes causing cercarial dermatitis.

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Section: Vertebrate Host Finding and Penetrationmentioning

confidence: 89%

Avian Schistosomes and Outbreaks of Cercarial Dermatitis

et al. 2015

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“…Interference of cathepsin L expression, however, had the greater impact on invasion possibly because the infective juvenile-specific cathepsin Ls are specifically adapted to this function. Cysteine proteases have also been implicated in the invasion process by the skin-penetrating parasites Schistosoma mansoni (37) and Trichobilharzia regenti (38) pointing to a common mechanism of host invasion among these trematodes.…”

Section: Discussionmentioning

confidence: 99%

Proteomics and Phylogenetic Analysis of the Cathepsin L Protease Family of the Helminth Pathogen Fasciola hepatica

Robinson

Tort

Lowther

et al. 2008

Molecular & Cellular Proteomics

120

131

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Cathepsin L proteases secreted by the helminth pathogen Fasciola hepatica have functions in parasite virulence including tissue invasion and suppression of host immune responses. Using proteomics methods alongside phylogenetic studies we characterized the profile of cathepsin L proteases secreted by adult F. hepatica and hence identified those involved in host-pathogen interaction. Phylogenetic analyses showed that the Fasciola cathepsin L gene family expanded by a series of gene duplications followed by divergence that gave rise to three clades associated with mature adult worms (Clades 1, 2, and 5) and two clades specific to infective juvenile stages (Clades 3 and 4). Consistent with these observations our proteomics studies identified representatives from Clades 1, 2, and 5 but not from Clades 3 and 4 in adult F. hepatica secretory products. Clades 1 and 2 account for 67.39 and 27.63% of total secreted cathepsin Ls, respectively, suggesting that their expansion was positively driven and that these proteases are most critical for parasite survival and adaptation. Sequence comparison studies revealed that the expansion of cathepsin Ls by gene duplication was followed by residue changes in the S2 pocket of the active site. Our biochemical studies showed that these changes result in alterations in substrate binding and suggested that the divergence of the cathepsin L family produced a repertoire of enzymes with overlapping and complementary substrate specificities that could cleave host macromolecules more efficiently. Although the cathepsin Ls are produced as zymogens containing a prosegment and mature domain, all secreted enzymes identified by MS were processed to mature active enzymes. The prosegment region was highly conserved between the clades except at the boundary of prosegment and mature enzyme. Despite the lack of conservation at this section, sites for exogenous cleavage by asparaginyl endopeptidases and a Leu-Ser2His motif for autocatalytic cleavage by cathepsin Ls were preserved.

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“…Cathepsin B and cathepsin L activities are readily detected by enzymatic assays in S. mansoni cercarial extracts and may facilitate skin penetration (Dalton et al, 1997; Kasný et al, 2007, 2009; Dvorák et al, 2008). 8–10 day old cultured larvae of S. mansoni also exhibited a dramatic increase in expression of these hemoglobin-degrading peptidases (Zerda et al, 1988; Dalton et al, 1995; Dalton and Brindley, 1996) and RNAi-mediated knockdown experiments showed that at least for SmCB1 the parasites cannot feed in vitro on hemoglobin and do not survive in vivo without this enzyme (Correnti et al, 2005).…”

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confidence: 99%

Induction of protective immune responses against schistosomiasis using functionally active cysteine peptidases

Ridi

Tallima

Dalton³

et al. 2014

Front. Genet.

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Each year schistosomiasis afflicts up to 600 million people in 74 tropical and sub-tropical countries, predominantly in the developing world. Yet we depend on a single drug, praziquantel, for its treatment and control. There is no vaccine available but one is urgently needed especially since praziquantel-resistant parasites are likely to emerge at some time in the future. The disease is caused by several worm species of the genus Schistosoma. These express several classes of papain-like cysteine peptidases, cathepsins B and L, in various tissues but particularly in their gastrodermis where they employ them as digestive enzymes. We have shown that sub-cutaneous injection of recombinant and functionally active Schistosoma mansoni cathepsin B1 (SmCB1), or a cathepsin L from a related parasite Fasciola hepatica (FhCL1), elicits highly significant protection (up to 73%) against an experimental challenge worm infection in murine models of schistosomiasis. The immune modulating properties of this subcutaneous injection can boost protection levels (up to 83%) when combined with other S. mansoni vaccine candidates, glyceraldehyde 3-phosphate dehydrogenase (SG3PDH) and peroxiredoxin (PRX-MAP). Here, we discuss these data in the context of the parasite’s biology and development, and provide putative mechanism by which the native-like cysteine peptidase induce protective immune responses.

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Comparison of cysteine peptidase activities inTrichobilharzia regentiandSchistosoma mansonicercariae

Cited by 33 publications

References 43 publications

Avian Schistosomes and Outbreaks of Cercarial Dermatitis

Avian Schistosomes and Outbreaks of Cercarial Dermatitis

Proteomics and Phylogenetic Analysis of the Cathepsin L Protease Family of the Helminth Pathogen Fasciola hepatica

Induction of protective immune responses against schistosomiasis using functionally active cysteine peptidases

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