Paramyosin is the Schistosoma mansoni (Trematoda) homologue of antigen B from Taenia solium (Cestoda)

Laclette, Juan Pedro; Landa, Abraham; Arcos, Lourdes; Willms, Kaethe; Davis, Alvin E.; Shoemaker, Charles B.

doi:10.1016/0166-6851(91)90015-x

Cited by 70 publications

(60 citation statements)

References 21 publications

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“…The sera from neurocysticercotic patients are also strongly reactive against the carboxyl-end region, with poor recognition of the central and amino regions (Vázquez-Talavera et al, submitted). These results are intriguing, con- sidering that the secondary structure of paramyosins is highly homogeneous: about 95% of the complete amino acid sequences of these proteins maintains the 7/28 repeat pattern characteristic of ␣-helical coiled-coil proteins (10,12). TPmy contains small sequences (15 residues at the amino end and 31 residues at the carboxyl end) that break the helical secondary structure, suggesting that the nonhelical regions have small influence on the asymmetry of the antibody recognition (12).…”

Section: Discussionmentioning

confidence: 86%

“…It is also an antigen during infections by several flatworms that are important parasites of humans and of domestic animals such as Schistosoma mansoni (10), Schistosoma japonicum (4), Taenia solium (10,12), and Echinococcus granulosus (18). The paramyosin of T. solium (TPmy) is present in the musculature but has also been found associated with the tegument of the parasite (7).…”

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confidence: 99%

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Characterization and Protective Potential of the Immune Response toTaenia soliumParamyosin in a Murine Model of Cysticercosis

et al. 2001

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Paramyosin has been proposed as a vaccine candidate in schistosomiasis and filariasis. However, limited information is available about its protective potential against cysticercosis and the immune response it induces. Immunization of mice with recombinant full-length paramyosin of Taenia solium (TPmy) results in about a 52% reduction in parasite burden after a subsequent challenge by intraperitoneal inoculation of Taenia crassiceps cysticerci. Immunization assays using recombinant fragments of TPmy, corresponding approximately to thirds on the amino, central, or carboxyl regions, suggest that protective epitopes are located mostly in the amino-end third. Proliferation assays using T cells obtained from mice immunized with the full-length recombinant TPmy also showed a preferential response to the amino-terminal fragment. In contrast, antibodies in the sera from these mice predominantly recognize epitopes located in the carboxyl-terminal fragment, being the immunoglobulin G1 subclass, the predominant antibody isotype. Characterization of the cellular immune response induced against the protective amino-terminal fragment reveals production of gamma interferon and interleukin-2, but not interleukin-4, suggesting a Th1-like profile.Paramyosin (Pmy) is a filamentous, ␣-helical, coiled-coil protein of about 100 kDa, present in some muscles of invertebrates. It is also an antigen during infections by several flatworms that are important parasites of humans and of domestic animals such as Schistosoma mansoni (10), Schistosoma japonicum (4), Taenia solium (10, 12), and Echinococcus granulosus (18). The paramyosin of T. solium (TPmy) is present in the musculature but has also been found associated with the tegument of the parasite (7). The collagen-binding and complement-inhibitory properties of TPmy have been described previously (8, 9, 11). TPmy is synthesized by the tegumentary cytons and apparently released through the cyst tegument (8). Furthermore, TPmy can be collected in the culture medium in which T. solium cysts are maintained (8), suggesting that a similar release to the host tissues might occur in vivo and that TPmy may modulate the host response through diminution of the inflammatory mediators at the host-parasite interface (8,11).Paramyosins have been proposed as vaccine candidates in a number of helminthiases including schistosomiasis (3, 20) and filariasis (14,19). Despite their protective abilities against schistosomiasis and filariasis, limited information is available on their potential as vaccines against cysticercosis. Here we report that immunization of mice with recombinant fragments of TPmy induces significant levels of protection in the murine model of cysticercosis by Taenia crassiceps. The profile of cytokine production suggests that the protective amino-terminal fragment of TPmy induces a Th1-like immune response. MATERIALS AND METHODSAnimal model. Mice used in all experiments were 4-to 6-week-old female BALB/c AnN strain mice. The ORF strain of T. crassiceps was maintained by consecutive passa...

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Section: Discussionmentioning

confidence: 86%

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confidence: 99%

Characterization and Protective Potential of the Immune Response toTaenia soliumParamyosin in a Murine Model of Cysticercosis

et al. 2001

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“…suggesting the presence of distinct, internal Fc-binding proteins that are unrelated to Pmy. Antigen B is secreted by a range of cestodes, and it shares high sequence identity with Pmy from schistosomes (23). Antigen B is secreted from the tegumental membrane of Taenia solium metacestodes (24), and a homologous protein from Taenia crassiceps binds to murine Fc␥ (17).…”

Section: S Mansoni and S Japonicum Pmy Binds To Fcmentioning

confidence: 99%

Receptor for Fc on the Surfaces of Schistosomes

et al. 2001

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Schistosoma mansoni masks its surface with adsorbed host proteins including erythrocyte antigens, immunoglobulins, major histocompatibility complex class I, and ␤ 2 -microglobulin (␤ 2 m), presumably as a means of avoiding host immune responses. How this is accomplished has not been explained. To identify surface receptors for host proteins, we biotinylated the tegument of live S. mansoni adults and mechanically transformed schistosomula and then removed the parasite surface with detergent. Incubation of biotinylated schistosome surface extracts with human immunoglobulin G (IgG) Fc-Sepharose resulted in purification of a 97-kDa protein that was subsequently identified as paramyosin (Pmy), using antiserum specific for recombinant Pmy. Fc also bound recombinant S. mansoni Pmy and native S. japonicum Pmy. Antiserum to Pmy decreased the binding of Pmy to Fc-Sepharose, and no proteins bound after removal of Pmy from extracts. Fluoresceinated human Fc bound to the surface, vestigial penetration glands, and nascent oral cavity of mechanically transformed schistosomula, and rabbit anti-Pmy Fab fragments ablated the binding of Fc to the schistosome surface. Pmy coprecipitated with host IgG from parasite surface extracts, indicating that complexes formed on the parasite surface as well as in vitro. Binding of Pmy to Fc was not inhibited by soluble protein A, suggesting that Pmy does not bind to the region between the CH2 and CH3 domains used by many other Fc-binding proteins. ␤ 2 m did not bind to the schistosome Fc receptor (Pmy), a finding that contradicts reports from earlier workers but did bind to a heteromultimer of labeled schistosomula surface proteins. This is the first report of the molecular identity of a schistosome Fc receptor; moreover it demonstrates an additional aspect of the unusual and multifunctional properties of Pmy from schistosomes and other parasitic flatworms.Schistosomes establish chronic infections in their hosts despite the presence of specific cellular and humoral immune responses. One of the most striking immunoevasive mechanisms displayed by these parasites is the acquisition of host products onto the tegument of the schistosome to mask its foreign status. Host molecules adsorbed onto the surface include immunoglobulins (20,40,44), major histocompatibility complex products (3, 36), ␤ 2 -microglobulin (␤ 2 m) (40), complement components (35, 38), ␣ 2 -macroglobulin (7, 19), C3 decay-accelerating factor (14), and glycolipids in the form of A, B, H, and Lewis blood group antigens (12).More than 20 years ago, Schistosoma mansoni schistosomula were shown to selectively bind the Fc but not the Fab fragment of immunoglobulin G (IgG) (40). This was demonstrated by the adhesion of rosetted sheep erythrocytes to transformed schistosomula of S. mansoni in vitro and inhibition of adhesion by free Fc fragments. IgG from rat, mouse, and rabbit also inhibited rosette formation. Whereas most of the host molecules listed above are adsorbed by schistosomula, receptors for Fc and complement C3 have also been ...

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“…One of the more studied antigens was antigen B, described by Flisser et al in 1980 as the antigen more frequently recognized by sera from NCC-infected patients, 31 producing a strong antibody response. [32][33][34] Use of antigen B in an antibody detecting ELISA in serum 35 as well as in CSF, did not demonstrate much advantage over other antigen sources. 36, 37 Grogl et al…”

Section: -24mentioning

confidence: 99%

Immunological and molecular diagnosis of cysticercosis

Rodríguez¹,

Wilkins

Dorny

2012

Pathogens and Global Health

134

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Cysticercosis, the infection with the larval stage of Taenia solium, is a cause of neurological symptoms including seizures, affecting the quality of life of patients and their families. Diagnosis focuses on brain imaging and serological tests are mostly used as confirmatory tools. Most cases, however, occur in poor endemic areas, where both kinds of diagnostic tools are poorly available. Development of point of care diagnostic tests is one of the most important priorities for cysticercosis researches today. The ideal point of care test would require detection of viable cysticercosis and hopefully identify cases with severe or progressive forms of neurocysticercosis, leading to referral of the patient for specialized medical attention. This manuscript describes the evolution of the serological diagnosis of cysticercosis over time, and the characteristics of the most common currently available tools, their advantages and disadvantages, and their potential use in future diagnostic tests.

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Paramyosin is the Schistosoma mansoni (Trematoda) homologue of antigen B from Taenia solium (Cestoda)

Cited by 70 publications

References 21 publications

Characterization and Protective Potential of the Immune Response toTaenia soliumParamyosin in a Murine Model of Cysticercosis

Characterization and Protective Potential of the Immune Response toTaenia soliumParamyosin in a Murine Model of Cysticercosis

Receptor for Fc on the Surfaces of Schistosomes

Immunological and molecular diagnosis of cysticercosis

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