Complex formation of human alpha‐1–antitrypsin with components in <i>Schistosoma mansoni</i> cercariae

Modha, J.; Doenhoff, Michael J.

doi:10.1111/j.1365-3024.1994.tb00372.x

Cited by 7 publications

(3 citation statements)

References 30 publications

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“…Our finding is consistent with a previous report by Darani et al (1997) who showed the native elastase to be poorly immunogenic when injected into mice. Reasons for the apparently poor immunogenicity of the native enzyme may be a consequence of the enzyme's ability to degrade host immunoglobulins and complement (Auriault et al 1981; Marikovsky et al 1988; Darani et al 1997; Pleass et al 2000) or its interaction with serine protease inhibitors in the host (Mast et al 1991; Modha and Doenhoff, 1994 a , b ). The latter was found to result in rapid clearance of the enzyme from the circulation preventing its normal processing by the antigen-presenting cells (Mast et al .…”

Section: Discussionmentioning

confidence: 99%

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Schistosoma mansonicercarial elastase (SmCE): differences in immunogenic properties of native and recombinant forms

et al. 2017

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The Schistosoma mansoni cercarial elastase (SmCE) has previously been shown to be poorly immunogenic in mice. However, a minority of mice were able to produce antibodies against SmCE after multiple immunizations with crude preparations containing the enzyme. These mice were partially protected against challenge infections of S. mansoni. In the present study, we show that in contrast to the poor immunogenicity of the enzymatically active native form of SmCE derived from a crude preparation (cercarial transformation fluid), immunization of CBA/Ca mice with two enzymatically inactive forms, namely purified native SmCE or a recombinant SmCE fused to recombinant Schistosoma japonicum glutathione S-transferase (rSmCE-SjGST), after adsorption onto aluminum hydroxide adjuvant, induced specific anti-SmCE immunoglobulin G (IgG) in all mice within 2 weeks of the second immunization. The IgG antibody response to rSmCESjGST was mainly of the IgG1 subclass. These results suggest that inactive forms of the antigen could be used to obtain the optimum immunogenic effects as a vaccine candidate against schistosomiasis. Mice immunized with the rSmCESjGST on alum had smaller mean worm burdens and lower tissue egg counts when compared with adjuvant aloneand recombinant SjGST-injected controls. The native SmCE was antigenically cross-reactive with homologous enzymes of Schistosoma haematobium and Schistosoma margrebowiei.

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Section: Discussionmentioning

confidence: 99%

“…The latter was found to result in rapid clearance of the enzyme from the circulation preventing its normal processing by the antigen-presenting cells (Mast et al . 1991; Modha and Doenhoff, 1994 a , b ).…”

Section: Discussionmentioning

confidence: 99%

Schistosoma mansonicercarial elastase (SmCE): differences in immunogenic properties of native and recombinant forms

et al. 2017

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“…It has been shown that levels of IgE, IL-8 and A1AT rise dramatically after infection with helminth parasites 56 . Indeed A1AT is known to bind directly to schistosomes 57 , is upregulated in the livers of infected animals 58 , and infections with schistosomes aggravate liver disease 59 . Thus A1AT may protect IgE from the damaging effects of serine proteases derived from migrating parasites.…”

Section: Discussionmentioning

confidence: 99%

IgE-tailpiece associates with α-1-antitrypsin (A1AT) to protect IgE from proteolysis without compromising its ability to interact with FcεRI

Quinn

Dunne

Moore

et al. 2016

Sci Rep

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Several splice variants of IgE exist in human plasma, including a variant called IgE-tailpiece (IgE-tp) that differs from classical IgE by the replacement of two carboxy-terminal amino acids with eight novel residues that include an ultimate cysteine. To date, the role of the secreted IgE-tp isoform in human immunity is unknown. We show that levels of IgE-tp are raised in helminth-infected donors, and that both the classical form of IgE (IgE-c) and IgE-tp interact with polymers of the serine protease inhibitor alpha-1-antitrypsin (A1AT). The association of IgE-tp with A1AT polymers in plasma protects the antibody from serine protease-mediated degradation, without affecting the functional interaction of IgE-tp with important receptors, including FcεR1. That polymers of A1AT protect IgE from degradation by helminth proteases may explain why these common and normally non-disease causing polymorphic variants of A1AT have been retained by natural selection. The observation that IgE can be complexed with polymeric forms of A1AT may therefore have important consequences for our understanding of the pathophysiology of pulmonary diseases that arise either as a consequence of A1AT-deficiency or through IgE-mediated type 1 hypersensitivity responses.

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Cloning and characterization of two genes encoding Schistosoma mansoni elastase

Pierrot¹,

Càpron²,

Khalife³

1995

Molecular and Biochemical Parasitology

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Complex formation of human alpha‐1–antitrypsin with components in Schistosoma mansoni cercariae

Cited by 7 publications

References 30 publications

Schistosoma mansonicercarial elastase (SmCE): differences in immunogenic properties of native and recombinant forms

Schistosoma mansonicercarial elastase (SmCE): differences in immunogenic properties of native and recombinant forms

IgE-tailpiece associates with α-1-antitrypsin (A1AT) to protect IgE from proteolysis without compromising its ability to interact with FcεRI

Cloning and characterization of two genes encoding Schistosoma mansoni elastase

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