Molecular Characterization of a 20.8-kDaSchistosoma mansoni Antigen

Hoffmann, Karl F.; Strand, Mette

doi:10.1074/jbc.272.23.14509

Cited by 42 publications

(25 citation statements)

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“…In fact, expression of Sm21.7 appeared to be relatively constant throughout those life stages present in the host, whereas expressions of Sm22.6 and Sm20.8 were mostly concentrated in the adult worm. Earlier expression studies, although not entirely consistent, do support our findings that transcription and translation of Sm22.6 and Sm20.8 are high in adult worms and absent in eggs [11, 13, 16, 33]. Furthermore, the ubiquitous nature of Sm21.7 is supported by previous Northern blotting experiments on Sm21.7 [12] which showed that mRNA was equally abundant in snail-stage sporocysts, schistosomula and adult worms.…”

Section: Discussionsupporting

confidence: 76%

“…M29837), Sm21.7 (M67507), Sm20.8 (U872430) and SmDLC1 (U55992) were cloned into pGEX-1λT expression vector (Pharmacia) as described previously [8, 13, 25]. The antigens were expressed as GST fusion proteins, cleaved and purified by preparative electrophoresis as described previously [10].…”

Section: Methodsmentioning

confidence: 99%

“…Members are characterized by the presence of EF-hand motifs (Pfam accession No. PF00036) at the N-terminal end and by a region similar to dynein light chain (DLC) at the C-terminal end [10,11,12,13,14,15,16,17,18]. Localization within the parasite has been studied for Sm22.6, Sj22.6, Sm20.8 and Fasciola gigantica calcium-binding protein 1.…”

Section: Introductionmentioning

confidence: 99%

“…It is a member of a gene family that includes orthologues Sj22.6 in S. japonicum and Sh22.6 in S. haematobium, which are also human IgE antigens [9, 10]. The familyincludes other characterized schistosomeproteins Sm21.7, Sm20.8 Sj20.8 and Sj21.7 [11,12,13,14,15,16] and similar molecules in other trematodes [17, 18]. Members are characterized by the presence of EF-hand motifs (Pfam accession No.…”

Section: Introductionmentioning

confidence: 99%

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Factors Affecting Human IgE and IgG Responses to Allergen-Like <i>Schistosoma mansoni </i>Antigens: Molecular Structure and Patterns of in vivo Exposure

Fitzsimmons

McBeath

Joseph

et al. 2006

Int Arch Allergy Immunol

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Background: The human IgE response is associated with allergy and with host defence against parasitic worms. A response to Sm22.6, the dominant IgE antigen in adult Schistosoma mansoni worms, correlates with resistance to re-infection after treatment. Sm22.6 is one of a family of EF-hand containing parasite proteins with sequence similarity to dynein light chain (DLC) and with major non-parasite allergens. Here we compare human IgE and IgG responses to other family members, Sm20.8 and Sm21.7, as well as to SmDLC1, relating these to antigen structure and expression in parasite life stages. Methods: Recombinant antigens were used in ELISA to measure antibody isotype responses in 177 cases from an endemic area, before and 7 weeks after treatment. Parasite antigen expression was assessed by RT-PCR and Western blotting. Results: Levels of antibodies to Sm22.6 and Sm20.8 (but not to Sm21.7 or SmDLC1) showed posttreatment increases in all but young children. Many produced IgE to Sm22.6 and Sm20.8 (2 EF-hands), few to Sm21.7 (1 EF-hand) or SmDLC1 (no EF-hands). Sm21.7 was expressed in cercariae, adults and eggs, Sm22.6 and Sm20.8 were concentrated in the adult. Conclusions: These studies suggest that IgE antigens Sm22.6 and Sm20.8 are only released to boost antibodies when adult worms die, whilst Sm21.7 and SmDLC1 are released constantly from eggs dying in host tissue. IgE responses to these allergen-like molecules may be influenced by patterns of exposure and the number of EF-hand motifs.

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Section: Discussionsupporting

confidence: 76%

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Factors Affecting Human IgE and IgG Responses to Allergen-Like <i>Schistosoma mansoni </i>Antigens: Molecular Structure and Patterns of in vivo Exposure

Fitzsimmons

McBeath

Joseph

et al. 2006

Int Arch Allergy Immunol

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“…The deduced amino acid sequence showed significant identity to several schistosome tegumental antigens which contain an EF–hand motif (aa 56–68), including Sm21.7 [24], Sm20.8 [25]and Sm16 [26]. Similar to earlier reports [12, 22], Sj22.6 also exhibited similarity to calmodulins, myosin regulatory light chains and other calcium–binding proteins.…”

Section: Resultssupporting

confidence: 67%

Identification of the Schistosoma japonicum 22.6–kDa Antigen as a Major Target of the Human IgE Response: Similarity of IgE–Binding Epitopes to Allergen Peptides

Santiago

Hafalla²,

Kurtis

et al. 1998

Int Arch Allergy Immunol

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Human resistance to reinfection with Schistosoma mansoni and Schistosoma haematobium correlates with elevated IgE titers against worm antigens (soluble worm antigen preparation, SWAP). In S. mansoni infection, low levels of reinfection following chemotherapy are associated with the recognition of a cloned tegumental protein Sm22.6. Because of potential species–specific differences in resistance to schistosomes, we attempted to identify Schistosoma japonicum antigens recognized by human IgE. Following a survey of 176 infected individuals in Leyte, Philippines, we show that IgE antibodies from the majority of older, high–IgE/SWAP responders recognize antigens in the 22 (Sj22)–, 45–, 78– and 97–kDa range in SWAP. Limited IgE cross–reactivity between Sj22 and Sm22 was observed following a comparison of Filipino IgE responses to these antigens. The antigen was cloned from an adult S. japonicum λ–ZAP cDNA library (Mindoro strain) by immunoscreening with pooled high–titer IgE antisera and a rabbit anti–Sj22 polyclonal antibody. The deduced amino acid sequence of the identified cDNA clone, MJ–1, showed significant homology to Sm22.6 (74%) and Sj22.6 (99%). Although the molecular sequence of Sj22.6 has already been reported, this is the first demonstration of its recognition by human IgE, thereby strengthening its potential as a vaccine candidate. Using an overlapping peptide approach, four IgE–binding epitopes were identified in Sj22.6, two of which exhibited similarities to known IgE–binding epitopes from codfish (Gad c 1) and β–lactoglobulin–related allergens. These findings suggest that allergy and protective immunity to helminth infection may be linked by the structural similarities of epitopes recognized by human IgE.

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Dynein and dynein-related genes

Milisav

1998

Cell Motil. Cytoskeleton

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Molecular Characterization of a 20.8-kDaSchistosoma mansoni Antigen

Abstract: Survival of

Cited by 42 publications

References 31 publications

Factors Affecting Human IgE and IgG Responses to Allergen-Like <i>Schistosoma mansoni </i>Antigens: Molecular Structure and Patterns of in vivo Exposure

Factors Affecting Human IgE and IgG Responses to Allergen-Like <i>Schistosoma mansoni </i>Antigens: Molecular Structure and Patterns of in vivo Exposure

Identification of the Schistosoma japonicum 22.6–kDa Antigen as a Major Target of the Human IgE Response: Similarity of IgE–Binding Epitopes to Allergen Peptides

Dynein and dynein-related genes

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