Identification and partial characterization of a parasite antigen in sera from humans infected with Wuchereria bancrofti.
Identifieur interne : 006391 ( PubMed/Curation ); précédent : 006390; suivant : 006392Identification and partial characterization of a parasite antigen in sera from humans infected with Wuchereria bancrofti.
Auteurs : G J Weil ; F. LiftisSource :
- Journal of immunology (Baltimore, Md. : 1950) [ 0022-1767 ] ; 1987.
Descripteurs français
- KwdFr :
- MESH :
English descriptors
- KwdEn :
- MESH :
- chemical , analysis : Antigens, Helminth.
- chemical , immunology : Antibodies, Monoclonal.
- immunology : Elephantiasis, Filarial, Wuchereria, Wuchereria bancrofti.
- Humans, Immunoenzyme Techniques, Immunosorbent Techniques, Molecular Weight.
Abstract
The purpose of this study was to identify and characterize soluble parasite antigens present in sera from humans infected with the filarial nematode Wuchereria bancrofti. Affinity chromatography and immunoblot methods were used to demonstrate a 200,000 m.w. circulating parasite antigen in sera from infected humans which corresponded to an antigen released by adult W. bancrofti during in vitro culture. Two monoclonal antibodies were produced to this antigen by immunizing mice with antigens from Dirofilaria immitis, a filarial parasite that is closely related to W. bancrofti, and screening cell fusion supernatants by enzyme immunoassay and counterimmunoelectrophoresis inhibition. The antibodies bound to a single repeated epitope (not phosphorylcholine) that was resistant to heat, acid, and protease treatments but sensitive to periodate oxidation. Immunoperoxidase studies showed that the epitope was concentrated in the cuticle and reproductive organs in D. immitis, and it was released in relatively large amounts by adult female D. immitis in vitro. The epitope is also present in antigens of other species of filarial and nonfilarial nematodes, but on the basis of preliminary studies, its presence in human serum appears to be specific for W. bancrofti infection.
PubMed: 3553330
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Antibodies, Monoclonal (immunology)</term>
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<term>Elephantiasis, Filarial (immunology)</term>
<term>Humans</term>
<term>Immunoenzyme Techniques</term>
<term>Immunosorbent Techniques</term>
<term>Molecular Weight</term>
<term>Wuchereria (immunology)</term>
<term>Wuchereria bancrofti (immunology)</term>
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<keywords scheme="KwdFr" xml:lang="fr"><term>Anticorps monoclonaux (immunologie)</term>
<term>Antigènes d'helminthe (analyse)</term>
<term>Filariose lymphatique (immunologie)</term>
<term>Humains</term>
<term>Masse moléculaire</term>
<term>Techniques d'immunoadsorption</term>
<term>Techniques immunoenzymatiques</term>
<term>Wuchereria (immunologie)</term>
<term>Wuchereria bancrofti (immunologie)</term>
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<keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Antigens, Helminth</term>
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<keywords scheme="MESH" type="chemical" qualifier="immunology" xml:lang="en"><term>Antibodies, Monoclonal</term>
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<keywords scheme="MESH" qualifier="analyse" xml:lang="fr"><term>Antigènes d'helminthe</term>
</keywords>
<keywords scheme="MESH" qualifier="immunologie" xml:lang="fr"><term>Anticorps monoclonaux</term>
<term>Filariose lymphatique</term>
<term>Wuchereria</term>
<term>Wuchereria bancrofti</term>
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<keywords scheme="MESH" qualifier="immunology" xml:lang="en"><term>Elephantiasis, Filarial</term>
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<front><div type="abstract" xml:lang="en">The purpose of this study was to identify and characterize soluble parasite antigens present in sera from humans infected with the filarial nematode Wuchereria bancrofti. Affinity chromatography and immunoblot methods were used to demonstrate a 200,000 m.w. circulating parasite antigen in sera from infected humans which corresponded to an antigen released by adult W. bancrofti during in vitro culture. Two monoclonal antibodies were produced to this antigen by immunizing mice with antigens from Dirofilaria immitis, a filarial parasite that is closely related to W. bancrofti, and screening cell fusion supernatants by enzyme immunoassay and counterimmunoelectrophoresis inhibition. The antibodies bound to a single repeated epitope (not phosphorylcholine) that was resistant to heat, acid, and protease treatments but sensitive to periodate oxidation. Immunoperoxidase studies showed that the epitope was concentrated in the cuticle and reproductive organs in D. immitis, and it was released in relatively large amounts by adult female D. immitis in vitro. The epitope is also present in antigens of other species of filarial and nonfilarial nematodes, but on the basis of preliminary studies, its presence in human serum appears to be specific for W. bancrofti infection.</div>
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<Title>Journal of immunology (Baltimore, Md. : 1950)</Title>
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<Abstract><AbstractText>The purpose of this study was to identify and characterize soluble parasite antigens present in sera from humans infected with the filarial nematode Wuchereria bancrofti. Affinity chromatography and immunoblot methods were used to demonstrate a 200,000 m.w. circulating parasite antigen in sera from infected humans which corresponded to an antigen released by adult W. bancrofti during in vitro culture. Two monoclonal antibodies were produced to this antigen by immunizing mice with antigens from Dirofilaria immitis, a filarial parasite that is closely related to W. bancrofti, and screening cell fusion supernatants by enzyme immunoassay and counterimmunoelectrophoresis inhibition. The antibodies bound to a single repeated epitope (not phosphorylcholine) that was resistant to heat, acid, and protease treatments but sensitive to periodate oxidation. Immunoperoxidase studies showed that the epitope was concentrated in the cuticle and reproductive organs in D. immitis, and it was released in relatively large amounts by adult female D. immitis in vitro. The epitope is also present in antigens of other species of filarial and nonfilarial nematodes, but on the basis of preliminary studies, its presence in human serum appears to be specific for W. bancrofti infection.</AbstractText>
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