Characterization of a muscle-associated antigen from Wuchereria bancrofti.
Identifieur interne : 00D156 ( Main/Exploration ); précédent : 00D155; suivant : 00D157Characterization of a muscle-associated antigen from Wuchereria bancrofti.
Auteurs : N. Raghavan [États-Unis] ; C V Maina ; P C Fitzgerald ; R S Tuan ; B E Slatko ; E A Ottesen ; T B NutmanSource :
- Experimental parasitology [ 0014-4894 ] ; 1992.
Descripteurs français
- KwdFr :
- Animaux, Antigènes d'helminthe (), Données de séquences moléculaires, Femelle, Filariose lymphatique (immunologie), Filarioses (immunologie), Humains, Hybridation in situ, Immunotransfert, Myosines (), Myosines (analyse), Myosines (immunologie), Poumon éosinophile (immunologie), Protéines d'helminthes (), Protéines d'helminthes (analyse), Protéines d'helminthes (immunologie), Protéines de fusion recombinantes (), Protéines de fusion recombinantes (analyse), Similitude de séquences d'acides aminés, Séquence d'acides aminés, Test ELISA, Wuchereria bancrofti (immunologie), Épitopes.
- MESH :
- analyse : Myosines, Protéines d'helminthes, Protéines de fusion recombinantes.
- immunologie : Filariose lymphatique, Filarioses, Myosines, Poumon éosinophile, Protéines d'helminthes, Wuchereria bancrofti.
- Animaux, Antigènes d'helminthe, Données de séquences moléculaires, Femelle, Humains, Hybridation in situ, Immunotransfert, Myosines, Protéines d'helminthes, Protéines de fusion recombinantes, Similitude de séquences d'acides aminés, Séquence d'acides aminés, Test ELISA, Épitopes.
English descriptors
- KwdEn :
- Amino Acid Sequence, Animals, Antigens, Helminth (chemistry), Elephantiasis, Filarial (immunology), Enzyme-Linked Immunosorbent Assay, Epitopes, Female, Filariasis (immunology), Helminth Proteins (analysis), Helminth Proteins (chemistry), Helminth Proteins (immunology), Humans, Immunoblotting, In Situ Hybridization, Molecular Sequence Data, Myosins (analysis), Myosins (chemistry), Myosins (immunology), Pulmonary Eosinophilia (immunology), Recombinant Fusion Proteins (analysis), Recombinant Fusion Proteins (chemistry), Sequence Homology, Amino Acid, Wuchereria bancrofti (immunology).
- MESH :
- chemical , analysis : Helminth Proteins, Myosins, Recombinant Fusion Proteins.
- chemical , chemistry : Antigens, Helminth, Helminth Proteins, Myosins, Recombinant Fusion Proteins.
- immunology : Elephantiasis, Filarial, Filariasis, Helminth Proteins, Myosins, Pulmonary Eosinophilia, Wuchereria bancrofti.
- Amino Acid Sequence, Animals, Enzyme-Linked Immunosorbent Assay, Epitopes, Female, Humans, Immunoblotting, In Situ Hybridization, Molecular Sequence Data, Sequence Homology, Amino Acid.
Abstract
A recombinant clone, WbN1, isolated from a genomic expression library of Wuchereria bancrofti and showing restricted specificity at the DNA level (Southern and PCR analyses) for Wuchereria bancrofti and Brugia malayi has been previously described. Sequence analysis of WbN1 indicated that it had notable similarity to myosin. Further characterization using in situ hybridization has localized the mRNA in the muscle of the adult parasite and in the microfilariae. Rabbit polyclonal antiserum, raised against the recombinant WbN1 fused to the maltose-binding protein, recognized a 200-kDa polypeptide in immunoblots containing B. malayi antigen extracts. The same antibody also recognized myosin extracted from Brugia pahangi, Onchocerca volvulus, and Caenorhabditis elegans. Localization using the rabbit antiserum revealed the presence of the antigen in the adult muscle tissue and in the microfilariae; the same antibody inhibited the binding of a monoclonal antibody 28.2 (directed toward MHC B of C. elegans myosin) to the recombinant WbN1 antigen and also to purified C. elegans myosin. Based on homology data, structural location, competitive ELISA, and immunoblot we conclude that WbN1 is related to myosin or a similar myofibrillar protein.
PubMed: 1283597
Affiliations:
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Raghavan</name><affiliation wicri:level="2"><nlm:affiliation>Laboratory of Parasitic Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892.</nlm:affiliation><country xml:lang="fr">États-Unis</country><placeName><region type="state">Maryland</region></placeName><wicri:cityArea>Laboratory of Parasitic Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda</wicri:cityArea></affiliation></author><author><name sortKey="Maina, C V" sort="Maina, C V" uniqKey="Maina C" first="C V" last="Maina">C V Maina</name></author><author><name sortKey="Fitzgerald, P C" sort="Fitzgerald, P C" uniqKey="Fitzgerald P" first="P C" last="Fitzgerald">P C Fitzgerald</name></author><author><name sortKey="Tuan, R S" sort="Tuan, R S" uniqKey="Tuan R" first="R S" last="Tuan">R S Tuan</name></author><author><name sortKey="Slatko, B E" sort="Slatko, B E" uniqKey="Slatko B" first="B E" last="Slatko">B E Slatko</name></author><author><name sortKey="Ottesen, E A" sort="Ottesen, E A" uniqKey="Ottesen E" first="E A" last="Ottesen">E A Ottesen</name></author><author><name sortKey="Nutman, T B" sort="Nutman, T B" uniqKey="Nutman T" first="T B" last="Nutman">T B Nutman</name></author></analytic><series><title level="j">Experimental parasitology</title><idno type="ISSN">0014-4894</idno><imprint><date when="1992" type="published">1992</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Antigens, Helminth (chemistry)</term><term>Elephantiasis, Filarial (immunology)</term><term>Enzyme-Linked Immunosorbent Assay</term><term>Epitopes</term><term>Female</term><term>Filariasis (immunology)</term><term>Helminth Proteins (analysis)</term><term>Helminth Proteins (chemistry)</term><term>Helminth Proteins (immunology)</term><term>Humans</term><term>Immunoblotting</term><term>In Situ Hybridization</term><term>Molecular Sequence Data</term><term>Myosins (analysis)</term><term>Myosins (chemistry)</term><term>Myosins (immunology)</term><term>Pulmonary Eosinophilia (immunology)</term><term>Recombinant Fusion Proteins (analysis)</term><term>Recombinant Fusion Proteins (chemistry)</term><term>Sequence Homology, Amino Acid</term><term>Wuchereria bancrofti (immunology)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term><term>Antigènes d'helminthe ()</term><term>Données de séquences moléculaires</term><term>Femelle</term><term>Filariose lymphatique (immunologie)</term><term>Filarioses (immunologie)</term><term>Humains</term><term>Hybridation in situ</term><term>Immunotransfert</term><term>Myosines ()</term><term>Myosines (analyse)</term><term>Myosines (immunologie)</term><term>Poumon éosinophile (immunologie)</term><term>Protéines d'helminthes ()</term><term>Protéines d'helminthes (analyse)</term><term>Protéines d'helminthes (immunologie)</term><term>Protéines de fusion recombinantes ()</term><term>Protéines de fusion recombinantes (analyse)</term><term>Similitude de séquences d'acides aminés</term><term>Séquence d'acides aminés</term><term>Test ELISA</term><term>Wuchereria bancrofti (immunologie)</term><term>Épitopes</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Helminth Proteins</term><term>Myosins</term><term>Recombinant Fusion Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Antigens, Helminth</term><term>Helminth Proteins</term><term>Myosins</term><term>Recombinant Fusion Proteins</term></keywords><keywords scheme="MESH" qualifier="analyse" xml:lang="fr"><term>Myosines</term><term>Protéines d'helminthes</term><term>Protéines de fusion recombinantes</term></keywords><keywords scheme="MESH" qualifier="immunologie" xml:lang="fr"><term>Filariose lymphatique</term><term>Filarioses</term><term>Myosines</term><term>Poumon éosinophile</term><term>Protéines d'helminthes</term><term>Wuchereria bancrofti</term></keywords><keywords scheme="MESH" qualifier="immunology" xml:lang="en"><term>Elephantiasis, Filarial</term><term>Filariasis</term><term>Helminth Proteins</term><term>Myosins</term><term>Pulmonary Eosinophilia</term><term>Wuchereria bancrofti</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Enzyme-Linked Immunosorbent Assay</term><term>Epitopes</term><term>Female</term><term>Humans</term><term>Immunoblotting</term><term>In Situ Hybridization</term><term>Molecular Sequence Data</term><term>Sequence Homology, Amino Acid</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Antigènes d'helminthe</term><term>Données de séquences moléculaires</term><term>Femelle</term><term>Humains</term><term>Hybridation in situ</term><term>Immunotransfert</term><term>Myosines</term><term>Protéines d'helminthes</term><term>Protéines de fusion recombinantes</term><term>Similitude de séquences d'acides aminés</term><term>Séquence d'acides aminés</term><term>Test ELISA</term><term>Épitopes</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">A recombinant clone, WbN1, isolated from a genomic expression library of Wuchereria bancrofti and showing restricted specificity at the DNA level (Southern and PCR analyses) for Wuchereria bancrofti and Brugia malayi has been previously described. Sequence analysis of WbN1 indicated that it had notable similarity to myosin. Further characterization using in situ hybridization has localized the mRNA in the muscle of the adult parasite and in the microfilariae. Rabbit polyclonal antiserum, raised against the recombinant WbN1 fused to the maltose-binding protein, recognized a 200-kDa polypeptide in immunoblots containing B. malayi antigen extracts. The same antibody also recognized myosin extracted from Brugia pahangi, Onchocerca volvulus, and Caenorhabditis elegans. Localization using the rabbit antiserum revealed the presence of the antigen in the adult muscle tissue and in the microfilariae; the same antibody inhibited the binding of a monoclonal antibody 28.2 (directed toward MHC B of C. elegans myosin) to the recombinant WbN1 antigen and also to purified C. elegans myosin. Based on homology data, structural location, competitive ELISA, and immunoblot we conclude that WbN1 is related to myosin or a similar myofibrillar protein.</div></front></TEI><affiliations><list><country><li>États-Unis</li></country><region><li>Maryland</li></region></list><tree><noCountry><name sortKey="Fitzgerald, P C" sort="Fitzgerald, P C" uniqKey="Fitzgerald P" first="P C" last="Fitzgerald">P C Fitzgerald</name><name sortKey="Maina, C V" sort="Maina, C V" uniqKey="Maina C" first="C V" last="Maina">C V Maina</name><name sortKey="Nutman, T B" sort="Nutman, T B" uniqKey="Nutman T" first="T B" last="Nutman">T B Nutman</name><name sortKey="Ottesen, E A" sort="Ottesen, E A" uniqKey="Ottesen E" first="E A" last="Ottesen">E A Ottesen</name><name sortKey="Slatko, B E" sort="Slatko, B E" uniqKey="Slatko B" first="B E" last="Slatko">B E Slatko</name><name sortKey="Tuan, R S" sort="Tuan, R S" uniqKey="Tuan R" first="R S" last="Tuan">R S Tuan</name></noCountry><country name="États-Unis"><region name="Maryland"><name sortKey="Raghavan, N" sort="Raghavan, N" uniqKey="Raghavan N" first="N" last="Raghavan">N. Raghavan</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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