Role of human decay-accelerating factor in the evasion of Schistosoma mansoni from the complement-mediated killing in vitro.

Horta, Maria Fátima; Ramalho-Pinto, F. J.; Fatima, Masroor

doi:10.1084/jem.174.6.1399

Cited by 47 publications

(17 citation statements)

References 46 publications

(40 reference statements)

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“…Previous studies have investigated the interaction between schistosomes and complement and have described several mechanisms that schistosomes have developed to evade complement-mediated lysis (12)(13)(14)(15)(16)(17)(18). Consistent with these studies, we found that infected C3-deficient mice had a similar adult worm burden to that of infected wild-type (WT) mice, supporting the finding that C3 is not involved in controlling worm development or establishment (Table I).…”

Section: The Absence Of C3 Does Not Alter Schistosome Burden or Liversupporting

confidence: 80%

“…C3 and its derivatives have also been shown to be important in Ab responses when the Ag dose is limiting (6, 7), clearance of Ag-Ab complexes (8), inhibition of IL-12 production by macrophages (9), and germinal center formation (10,11). Although previous studies have shown that schistosomes have developed several mechanisms to evade complement-mediated lysis by the host (12)(13)(14)(15)(16)(17)(18), the possible contribution of C3 to response development during schistosome infection has not been investigated.…”

mentioning

confidence: 99%

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Lack of C3 Affects Th2 Response Development and the Sequelae of Chemotherapy in Schistosomiasis

Flamme

MacDonald

Huxtable

et al. 2003

The Journal of Immunology

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The role of the third component of complement (C3) during schistosome infection was investigated using mice deficient in C3. While no effect was observed 8 wk after infection on worm development or liver pathology, Ag-specific Th2-associated cytokine production (IL-13, IL-5, IL-6, and IL-10) was significantly reduced, and IFN-γ production was enhanced in the absence of C3. IgG1 and IgE, but not IgG2a or IgM, Ab responses were also significantly impaired in infected C3−/− mice, suggesting that C3 may play a role in IL-4-mediated Th2 response enhancement during schistosome infection. Furthermore, C3-deficient mice could not effectively clear adult worms after praziquantel (PZQ) treatment and suffered increased morbidity due to the overproduction of proinflammatory mediators following drug administration. However, the ischemic liver damage that normally accompanies PZQ administration in infected wild-type mice was substantially reduced in treated C3-deficient mice, probably due to the absence of dead or dying worms in the livers of these animals. Together these results indicate that C3 enhances Th2 responses during schistosome infection, potentiates PZQ-mediated parasite clearance, and reduces chemotherapy-induced proinflammatory mediator production.

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Section: The Absence Of C3 Does Not Alter Schistosome Burden or Liversupporting

confidence: 80%

mentioning

confidence: 99%

Lack of C3 Affects Th2 Response Development and the Sequelae of Chemotherapy in Schistosomiasis

Flamme

MacDonald

Huxtable

et al. 2003

The Journal of Immunology

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“…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).…”

mentioning

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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“…This concept of molecular mimicry was introduced by Yoshino and Bayne (1983) when they found haemolymph-like antigens on the surface tegument of sporocysts. Similar mimicry has been suggested in schistosomula by Guillou et al (2007) and Horta and Ramalho-Pinto (1991) by demonstrating that decay-accelerating factor from human erythrocytes could be transferred to S. mansoni and protect it against complement-mediated haemolysis. We observed that the secondary sporocysts were recognised at a lower rate than the primary sporocysts in the in vitro experiments.…”

Section: Discussionmentioning

confidence: 73%

Interaction between primary and secondary sporocysts of Schistosoma mansoni and the internal defence system of Biomphalaria resistant and susceptible to the parasite

Mattos

Martins-Souza

Kusel

et al. 2011

Mem. Inst. Oswaldo Cruz

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Role of human decay-accelerating factor in the evasion of Schistosoma mansoni from the complement-mediated killing in vitro.

Cited by 47 publications

References 46 publications

Lack of C3 Affects Th2 Response Development and the Sequelae of Chemotherapy in Schistosomiasis

Lack of C3 Affects Th2 Response Development and the Sequelae of Chemotherapy in Schistosomiasis

Receptor for Fc on the Surfaces of Schistosomes

Interaction between primary and secondary sporocysts of Schistosoma mansoni and the internal defence system of Biomphalaria resistant and susceptible to the parasite

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