Comparative Antigen Analysis of Different Life Stages of &lt;i&gt;Schistosoma mansoni&lt;/i&gt; by Crossed Immunoelectrophoresis

Akhiani, Ali A.; Nilsson, Lars; Ouchterlony, Örjan

doi:10.1159/000235440

Cited by 5 publications

(6 citation statements)

References 15 publications

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“…SmMDH is an important enzyme involved in anaerobic carbohydrate metabolism through catalysing reduction of oxaloacetate to malate, the main pathway of energy production for the Schistosoma parasite [ 101 ]. The enzyme is expressed in schistosome adult worms, cercariae and eggs stages [ 102 ].…”

Section: Discussionmentioning

confidence: 99%

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Treatment of Schistosoma mansoni with miltefosine in vitro enhances serological recognition of defined worm surface antigens

et al. 2017

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BackgroundMiltefosine, an anti-cancer drug that has been successfully repositioned for treatment of Leishmania infections, has recently also shown promising effects against Schistosoma spp targeting all life cycle stages of the parasite. The current study examined the effect of treating Schistosoma mansoni adult worms with miltefosine on exposure of worm surface antigens in vitro.Methodology/Principal findingsIn an indirect immunofluorescence assay, rabbit anti-S.mansoni adult worm homogenate and anti-S. mansoni infection antisera gave strong immunofluorescence of the S. mansoni adult worm surface after treatment with miltefosine, the latter antiserum having previously been shown to synergistically enhance the schistosomicidal activity of praziquantel. Rabbit antibodies that recognised surface antigens exposed on miltefosine-treated worms were recovered by elution off the worm surface in low pH buffer and were used in a western immunoblotting assay to identify antigenic targets in a homogenate extract of adult worms (SmWH). Four proteins reacting with the antibodies in immunoblots were purified and proteomic analysis (MS/MS) combined with specific immunoblotting indicated they were the S. mansoni proteins: fructose-1,6 bisphosphate aldolase (SmFBPA), Sm22.6, alkaline phosphatase and malate dehydrogenase. These antibodies were also found to bind to the surface of 3-hour schistosomula and induce immune agglutination of the parasites, suggesting they may have a role in immune protection.Conclusion/SignificanceThis study reveals a novel mode of action of miltefosine as an anti-schistosome agent. The immune-dependent hypothesis we investigated has previously been lent credence with praziquantel (PZQ), whereby treatment unmasks parasite surface antigens not normally exposed to the host during infection. Antigens involved in this molecular mechanism could have potential as intervention targets and antibodies against these antigens may act to increase the drug’s anti-parasite efficacy and be involved in the development of resistance to re-infection.

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Section: Discussionmentioning

confidence: 99%

“…The latter non-agglutinating antibodies showed reactivities against Sm22.6 and SmAP but not against the SmFBPA pr33 in western blots. The low levels of expression of the first two proteins on 3-hour schistosomula could be an explanation [ 102 , 109 ].…”

Section: Discussionmentioning

confidence: 99%

Treatment of Schistosoma mansoni with miltefosine in vitro enhances serological recognition of defined worm surface antigens

et al. 2017

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“…Parasites and antigen preparations. Schistosoma mansoni (Puerto Rican strain) adult worms, eggs and cercariae were collected as described elsewhere [16]. For intranasal immunization, a soluble extract of adult worms (SWAP) was prepared as described previously [12].…”

Section: Methodsmentioning

confidence: 99%

Interaction of Cholera Toxin with Three Life‐cycle Stages of Schistosoma mansoni: Adult Worm, Egg and Cercaria

Akhiani

Deelder

Månsson³

et al. 2006

Scand J Immunol

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We have previously reported that there is an immunological cross‐reactivity between Schistosoma mansoni and cholera toxin (CT). In this study, using an immunofluorescence technique with anti‐CT antibody, we provide further evidence for this cross‐reactivity by demonstrating an antigen, localized in the tegument of S. mansoni adult worms which is cross‐reactive with a CT antigen. Anti‐CT antibodies also reacted with structures in S. mansoni cercariae and eggs. Additionally, CT itself was found to bind strongly to the gut of the adult worm, gut cells of cercaria and the egg shell. The binding of CT to the parasite was blocked when parasite sections were incubated with CT which had been incubated with the ganglioside GM1. Lipid extraction and isolation of gangliosides demonstrated the presence of GM1 in adult worms. For further analysis of CT‐binding structures, the possible interaction of CT with two major schistosome gut antigens, circulating cathodic antigen (CCA) and circulating anodic antigen (CAA), was studied. We found that CT blocked the binding of anti‐CCA antibody to the gut of adult worms and that anti‐CCA blocked the binding of CT to the worm gut. These findings indicate that CT binds to CCA present in the gut of the parasite and thus has, in addition to GM1, a second binding specificity.

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“…Schistosoma mansoni (Puerto Rican strain) adult worms and cercariae were collected as described elsewhere (Akhiani et al 1991).…”

Section: Parasites and Antigen Preparationsmentioning

confidence: 99%

Immunological cross reactivity between Schistosoma mansoni and cholera toxin

Akhiani

Nilsson

Ouchterlony

1997

Parasite Immunology

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Intranasal administration of schistosome antigens in combination with appropriate adjuvant may be an effective route for immunization against schistosomes, since the lungs represent an important site of elimination of schistosomulae. Our previous studies have shown that in mice intranasal administration of cholera toxin (CT) before infection with Schistosoma mansoni results in an enhancement of the worm burden in comparison to nontreated infected animals. In the present study, it was shown that mice treated intranasally with CT displayed high numbers of schistosome-reactive IgM-secreting cells in the spleen as well as high levels of schistosome-reactive serum IgM antibodies, whereas no significant immunological response against two other antigens, ovalbumin (OVA) or keyhole limpet haemocyanin (KLH) was noted. Sera from mice treated intranasally with CT recognized a 22 kDA antigen on SWAP blots. This band was not demonstrable after absorption of the sera with SWAP. These findings indicate a possible cross reactivity between cholera toxin and schistosome antigens. Further analysis by Western blot revealed that a 22 kDa antigen was detected on CT blots by sera from mice and humans infected with S. mansoni. This band was not demonstrable after absorption of the mouse or the human sera with CT. The 22 kDa cross reactive antigen was heat-stable. The antibodies against the 22 kDa antigen were only found within the IgM class but not within other Ig isotypes. Our findings also indicate that the 22 kDa antigen detected by anti-S. mansoni antibodies represents the A1 fragment of the cholera toxin.

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Comparative Antigen Analysis of Different Life Stages of <i>Schistosoma mansoni</i> by Crossed Immunoelectrophoresis

Cited by 5 publications

References 15 publications

Treatment of Schistosoma mansoni with miltefosine in vitro enhances serological recognition of defined worm surface antigens

Treatment of Schistosoma mansoni with miltefosine in vitro enhances serological recognition of defined worm surface antigens

Interaction of Cholera Toxin with Three Life‐cycle Stages of Schistosoma mansoni: Adult Worm, Egg and Cercaria

Immunological cross reactivity between Schistosoma mansoni and cholera toxin

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