Receptor for IgG(Fc) and human β2-microglobulin on S. mansoni schistosomula

Torpier, Gérard; Càpron, André; Ouaissi, M. A.

doi:10.1038/278447a0

Cited by 104 publications

(57 citation statements)

References 9 publications

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“…Many authors (16,17,28,30) have suggested that host protein antigen uptake by parasites offers a means of escape from host immune responses by disguising parasitical antigenic determinants. We believe that this is the case for the Fc receptor present on the parasites examined in this paper.…”

Section: Discussionmentioning

confidence: 99%

Receptor for immunoglobulin Fc on pathogenic but not on nonpathogenic protozoa of the Trypanosomatidae.

Miranda-Santos¹,

Campos-Neto²

1981

The Journal of Experimental Medicine

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The mechanisms parasites have developed to escape immune surveillance are currently under investigation in many laboratories, because their elucidation may provide new approaches to the prevention of the diseases the parasites cause. For a detailed description and experimental evidence of these various mechanisms, see the recent review by Bloom (1).One possible means of evasion is the uptake of host antigen by the parasite (2). This phenomenon has been amply studied and documented in schistosomiasis. The acquisition of mouse antigens (3-5), human A, B, and H blood group antigens (6, 7), glycolipids from erythrocytes (8), serum factors (9-11) and, more recently, mouse histocompatibility antigens (12) have been demonstrated in this parasite and offer an effective mechanism for antigenic mimicry of the host and subsequent escape from the immune response.This same parasite has been used to study the possibility of immunological blockade (13). Host immunoglobulin has been shown to occur on the surface of Schistosoma mansoni (14,15), and it has also been determined that this immunoglobulin is heterospecific, excluding the possibility of a specific parasite-antigen host-antibody interaction (15). These studies also suggest that the host immunoglobulin adsorbed by the parasite is oriented so as to have a Fab region of the molecule available, possibly representing a specific binding of the immunoglobulin through a receptor for Fc present on the membrane of S. mansoni, Indeed, receptors for IgG Fc, human fl2-microglobulin (16), and Clq (17) on this parasite have recently been reported.

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Section: Discussionmentioning

confidence: 99%

Receptor for immunoglobulin Fc on pathogenic but not on nonpathogenic protozoa of the Trypanosomatidae.

Miranda-Santos¹,

Campos-Neto²

1981

The Journal of Experimental Medicine

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“…Torpier and colleagues showed the presence of Fc receptors on the surface of mechanically transformed schistosomula using an erythrocyte-antierythrocyte complex (40). Probing of fixed schistosomula with Fc-FITC also showed binding to the parasite surface, but the strongest fluorescence was localized to internal structures (presumed to be the vestigial penetration glands and the nascent oral cavity) (Fig.…”

Section: S Mansoni and S Japonicum Pmy Binds To Fcmentioning

confidence: 99%

“…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.…”

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confidence: 99%

“…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.…”

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confidence: 99%

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confidence: 99%

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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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Hypothesis: rheumatoid factors are antiidiotypes related to bacterial or viral fc receptors

Williams

1988

Arthritis & Rheumatism

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Receptor for IgG(Fc) and human β2-microglobulin on S. mansoni schistosomula

Cited by 104 publications

References 9 publications

Receptor for immunoglobulin Fc on pathogenic but not on nonpathogenic protozoa of the Trypanosomatidae.

Receptor for immunoglobulin Fc on pathogenic but not on nonpathogenic protozoa of the Trypanosomatidae.

Receptor for Fc on the Surfaces of Schistosomes

Hypothesis: rheumatoid factors are antiidiotypes related to bacterial or viral fc receptors

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