A major allergen of lymphatic filarial nematodes is a parasite homolog of the gamma-glutamyl transpeptidase.
Identifieur interne : 00B898 ( Ncbi/Checkpoint ); précédent : 00B897; suivant : 00B899A major allergen of lymphatic filarial nematodes is a parasite homolog of the gamma-glutamyl transpeptidase.
Auteurs : E. Lobos ; R. Zahn ; N. Weiss ; T. B. NutmanSource :
- Molecular Medicine [ 1076-1551 ] ; 1996.
Descripteurs français
- KwdFr :
- Amorces ADN (), Analyse de séquence, Animaux, Antigènes d'helminthe (), Antigènes d'helminthe (immunologie), Autoanticorps (immunologie), Brugia malayi (immunologie), Clonage moléculaire, Données de séquences moléculaires, Filariose lymphatique (parasitologie), Humains, Immunoglobuline E (immunologie), Immunoglobuline E (métabolisme), Protéines membranaires (), Similitude de séquences, Séquence d'acides aminés, Séquence nucléotidique, Technique de Northern, Technique de Western, gamma-Glutamyltransferase (), gamma-Glutamyltransferase (métabolisme), Éosinophilie (parasitologie), Éosinophilie (physiopathologie).
- MESH :
- immunologie : Antigènes d'helminthe, Autoanticorps, Brugia malayi, Immunoglobuline E.
- métabolisme : Immunoglobuline E, gamma-Glutamyltransferase.
- parasitologie : Filariose lymphatique, Éosinophilie.
- physiopathologie : Éosinophilie.
- Amorces ADN, Analyse de séquence, Animaux, Antigènes d'helminthe, Clonage moléculaire, Données de séquences moléculaires, Humains, Protéines membranaires, Similitude de séquences, Séquence d'acides aminés, Séquence nucléotidique, Technique de Northern, Technique de Western, gamma-Glutamyltransferase.
English descriptors
- KwdEn :
- Amino Acid Sequence, Animals, Antigens, Helminth (chemistry), Antigens, Helminth (immunology), Autoantibodies (immunology), Base Sequence, Blotting, Northern, Blotting, Western, Brugia malayi (immunology), Cloning, Molecular, DNA Primers (chemistry), Elephantiasis, Filarial (parasitology), Eosinophilia (parasitology), Eosinophilia (physiopathology), Humans, Immunoglobulin E (immunology), Immunoglobulin E (metabolism), Membrane Proteins (chemistry), Molecular Sequence Data, Sequence Analysis, Sequence Homology, gamma-Glutamyltransferase (chemistry), gamma-Glutamyltransferase (metabolism).
- MESH :
- chemical , chemistry : Antigens, Helminth, DNA Primers, Membrane Proteins, gamma-Glutamyltransferase.
- chemical , immunology : Antigens, Helminth, Autoantibodies, Immunoglobulin E.
- immunology : Brugia malayi.
- chemical , metabolism : Immunoglobulin E, gamma-Glutamyltransferase.
- parasitology : Elephantiasis, Filarial, Eosinophilia.
- physiopathology : Eosinophilia.
- Amino Acid Sequence, Animals, Base Sequence, Blotting, Northern, Blotting, Western, Cloning, Molecular, Humans, Molecular Sequence Data, Sequence Analysis, Sequence Homology.
Abstract
BACKGROUND: Bm2325, a major IgE-inducing antigen of the filarial parasite Brugia malayi has been implicated in the pathology of tropical pulmonary eosinophilia (TPE), a pulmonary syndrome thought to result from hypersensitivity to microfilariae. MATERIALS AND METHODS: Affinity-purified IgE to Bm2325 from patients with TPE was used to identify a complementary DNA (cDNA) from a B. malayi expression library. Sequence analysis of the cDNA revealed a hitherto unknown parasite protein. Immunoblotting of the recombinant filarial protein using sera of patients with TPE determined its IgE-binding capacity. Reactivity to human lung epithelial cell proteins was analyzed using murine anti-Bm2325 antibodies and serum from patients with TPE. RESULTS: The predicted protein is a homolog of the entire precursor of the gamma-glutamyl transpeptidase (gamma-GT), a key enzyme in the synthesis and degradation of glutathione. The filarial precursor encodes both the heavy (H) and the light (L) chain subunits and shares structural similarities with the mammalian enzymes. The Bm2325 allergen was identified as the homolog of the enzyme light chain subunit. Murine antibodies against the recombinant parasite gamma-GT cross-reacted with the human enzyme present in human airway epithelial cells, and human gamma-GT is a target of antibodies present in the serum of patients with TPE. CONCLUSION: Molecular mimicry between the parasite gamma-GT homolog and the host membrane-bound gamma-GT present in lung epithelial cells likely contributes to the pathogenesis observed in tropical pulmonary eosinophilia.
Url:
PubMed: 8972486
PubMed Central: 2230135
Affiliations:
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Lobos</name></author><author><name sortKey="Zahn, R" sort="Zahn, R" uniqKey="Zahn R" first="R." last="Zahn">R. Zahn</name></author><author><name sortKey="Weiss, N" sort="Weiss, N" uniqKey="Weiss N" first="N." last="Weiss">N. Weiss</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">Molecular Medicine</title><idno type="ISSN">1076-1551</idno><idno type="eISSN">1528-3658</idno><imprint><date when="1996">1996</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>Antigens, Helminth (immunology)</term><term>Autoantibodies (immunology)</term><term>Base Sequence</term><term>Blotting, Northern</term><term>Blotting, Western</term><term>Brugia malayi (immunology)</term><term>Cloning, Molecular</term><term>DNA Primers (chemistry)</term><term>Elephantiasis, Filarial (parasitology)</term><term>Eosinophilia (parasitology)</term><term>Eosinophilia (physiopathology)</term><term>Humans</term><term>Immunoglobulin E (immunology)</term><term>Immunoglobulin E (metabolism)</term><term>Membrane Proteins (chemistry)</term><term>Molecular Sequence Data</term><term>Sequence Analysis</term><term>Sequence Homology</term><term>gamma-Glutamyltransferase (chemistry)</term><term>gamma-Glutamyltransferase (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Amorces ADN ()</term><term>Analyse de séquence</term><term>Animaux</term><term>Antigènes d'helminthe ()</term><term>Antigènes d'helminthe (immunologie)</term><term>Autoanticorps (immunologie)</term><term>Brugia malayi (immunologie)</term><term>Clonage moléculaire</term><term>Données de séquences moléculaires</term><term>Filariose lymphatique (parasitologie)</term><term>Humains</term><term>Immunoglobuline E (immunologie)</term><term>Immunoglobuline E (métabolisme)</term><term>Protéines membranaires ()</term><term>Similitude de séquences</term><term>Séquence d'acides aminés</term><term>Séquence nucléotidique</term><term>Technique de Northern</term><term>Technique de Western</term><term>gamma-Glutamyltransferase ()</term><term>gamma-Glutamyltransferase (métabolisme)</term><term>Éosinophilie (parasitologie)</term><term>Éosinophilie (physiopathologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Antigens, Helminth</term><term>DNA Primers</term><term>Membrane Proteins</term><term>gamma-Glutamyltransferase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="immunology" xml:lang="en"><term>Antigens, Helminth</term><term>Autoantibodies</term><term>Immunoglobulin E</term></keywords><keywords scheme="MESH" qualifier="immunologie" xml:lang="fr"><term>Antigènes d'helminthe</term><term>Autoanticorps</term><term>Brugia malayi</term><term>Immunoglobuline E</term></keywords><keywords scheme="MESH" qualifier="immunology" xml:lang="en"><term>Brugia malayi</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Immunoglobulin E</term><term>gamma-Glutamyltransferase</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Immunoglobuline E</term><term>gamma-Glutamyltransferase</term></keywords><keywords scheme="MESH" qualifier="parasitologie" xml:lang="fr"><term>Filariose lymphatique</term><term>Éosinophilie</term></keywords><keywords scheme="MESH" qualifier="parasitology" xml:lang="en"><term>Elephantiasis, Filarial</term><term>Eosinophilia</term></keywords><keywords scheme="MESH" qualifier="physiopathologie" xml:lang="fr"><term>Éosinophilie</term></keywords><keywords scheme="MESH" qualifier="physiopathology" xml:lang="en"><term>Eosinophilia</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Base Sequence</term><term>Blotting, Northern</term><term>Blotting, Western</term><term>Cloning, Molecular</term><term>Humans</term><term>Molecular Sequence Data</term><term>Sequence Analysis</term><term>Sequence Homology</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Amorces ADN</term><term>Analyse de séquence</term><term>Animaux</term><term>Antigènes d'helminthe</term><term>Clonage moléculaire</term><term>Données de séquences moléculaires</term><term>Humains</term><term>Protéines membranaires</term><term>Similitude de séquences</term><term>Séquence d'acides aminés</term><term>Séquence nucléotidique</term><term>Technique de Northern</term><term>Technique de Western</term><term>gamma-Glutamyltransferase</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>BACKGROUND: Bm2325, a major IgE-inducing antigen of the filarial parasite Brugia malayi has been implicated in the pathology of tropical pulmonary eosinophilia (TPE), a pulmonary syndrome thought to result from hypersensitivity to microfilariae. MATERIALS AND METHODS: Affinity-purified IgE to Bm2325 from patients with TPE was used to identify a complementary DNA (cDNA) from a B. malayi expression library. Sequence analysis of the cDNA revealed a hitherto unknown parasite protein. Immunoblotting of the recombinant filarial protein using sera of patients with TPE determined its IgE-binding capacity. Reactivity to human lung epithelial cell proteins was analyzed using murine anti-Bm2325 antibodies and serum from patients with TPE. RESULTS: The predicted protein is a homolog of the entire precursor of the gamma-glutamyl transpeptidase (gamma-GT), a key enzyme in the synthesis and degradation of glutathione. The filarial precursor encodes both the heavy (H) and the light (L) chain subunits and shares structural similarities with the mammalian enzymes. The Bm2325 allergen was identified as the homolog of the enzyme light chain subunit. Murine antibodies against the recombinant parasite gamma-GT cross-reacted with the human enzyme present in human airway epithelial cells, and human gamma-GT is a target of antibodies present in the serum of patients with TPE. CONCLUSION: Molecular mimicry between the parasite gamma-GT homolog and the host membrane-bound gamma-GT present in lung epithelial cells likely contributes to the pathogenesis observed in tropical pulmonary eosinophilia.</p><sec sec-type="scanned-figures"><title>Images</title><fig id="F1"><label>FIG. 4</label><graphic xlink:href="molmed00042-0069-a" xlink:role="719"></graphic></fig><fig id="F2"><label>FIG. 5</label><graphic xlink:href="molmed00042-0069-b" xlink:role="719"></graphic></fig><fig id="F3"><label>FIG. 6</label><graphic xlink:href="molmed00042-0070-a" xlink:role="720"></graphic></fig><fig id="F4"><label>FIG. 7</label><graphic xlink:href="molmed00042-0070-b" xlink:role="720"></graphic></fig></sec></div></front></TEI><affiliations><list></list><tree><noCountry><name sortKey="Lobos, E" sort="Lobos, E" uniqKey="Lobos E" first="E." last="Lobos">E. Lobos</name><name sortKey="Nutman, T B" sort="Nutman, T B" uniqKey="Nutman T" first="T. B." last="Nutman">T. B. Nutman</name><name sortKey="Weiss, N" sort="Weiss, N" uniqKey="Weiss N" first="N." last="Weiss">N. Weiss</name><name sortKey="Zahn, R" sort="Zahn, R" uniqKey="Zahn R" first="R." last="Zahn">R. Zahn</name></noCountry></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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