Qualitative characterization of antibody responses to single and multiple Brugia pahangi infections in jirds.
Identifieur interne : 00D503 ( Main/Exploration ); précédent : 00D502; suivant : 00D504Qualitative characterization of antibody responses to single and multiple Brugia pahangi infections in jirds.
Auteurs : R G Farrar ; T R Klei ; C S Mcvay ; S U ColemanSource :
- The Journal of parasitology [ 0022-3395 ] ; 1991.
Descripteurs français
- KwdFr :
- Animaux, Anticorps antihelminthe (biosynthèse), Anticorps antihelminthe (sang), Antigènes d'helminthe (), Antigènes d'helminthe (analyse), Antigènes d'helminthe (immunologie), Brugia (immunologie), Femelle, Filariose lymphatique (immunologie), Gerbillinae, Masse moléculaire, Modèles animaux de maladie humaine, Mâle, Protéines d'helminthes (), Protéines d'helminthes (analyse), Protéines d'helminthes (immunologie), Technique de Western, Test ELISA, Électrophorèse sur gel de polyacrylamide.
- MESH :
- analyse : Antigènes d'helminthe, Protéines d'helminthes.
- biosynthèse : Anticorps antihelminthe.
- immunologie : Antigènes d'helminthe, Brugia, Filariose lymphatique, Protéines d'helminthes.
- sang : Anticorps antihelminthe.
- Animaux, Antigènes d'helminthe, Femelle, Gerbillinae, Masse moléculaire, Modèles animaux de maladie humaine, Mâle, Protéines d'helminthes, Technique de Western, Test ELISA, Électrophorèse sur gel de polyacrylamide.
English descriptors
- KwdEn :
- Animals, Antibodies, Helminth (biosynthesis), Antibodies, Helminth (blood), Antigens, Helminth (analysis), Antigens, Helminth (chemistry), Antigens, Helminth (immunology), Blotting, Western, Brugia (immunology), Disease Models, Animal, Electrophoresis, Polyacrylamide Gel, Elephantiasis, Filarial (immunology), Enzyme-Linked Immunosorbent Assay, Female, Gerbillinae, Helminth Proteins (analysis), Helminth Proteins (chemistry), Helminth Proteins (immunology), Male, Molecular Weight.
- MESH :
- chemical , analysis : Antigens, Helminth, Helminth Proteins.
- chemical , biosynthesis : Antibodies, Helminth.
- chemical , blood : Antibodies, Helminth.
- chemical , chemistry : Antigens, Helminth, Helminth Proteins.
- chemical , immunology : Antigens, Helminth, Helminth Proteins.
- immunology : Brugia, Elephantiasis, Filarial.
- Animals, Blotting, Western, Disease Models, Animal, Electrophoresis, Polyacrylamide Gel, Enzyme-Linked Immunosorbent Assay, Female, Gerbillinae, Male, Molecular Weight.
Abstract
Antibody responses of jirds, singly and multiply inoculated with Brugia pahangi infective larvae (L3), to soluble somatic extracts of adult parasites were characterized by western blot analysis. Forty-two protein bands ranging in molecular weight from 12 to 160 kDa were recognized by sera from infected jirds. Antibody recognition of individual B. pahangi antigen bands in this assay appears to be independent of antibody enzyme-linked immunosorbent assay (ELISA) titers to crude parasite extract, severity of lymphatic lesions, levels of microfilaremia, numbers of L3 inoculated, or numbers of adult parasites in individual jirds. Antibody recognition of protein bands with molecular weights of 37 kDa, 21 kDa, and 17 kDa, however, did temporally correspond with certain parasitological and pathologic events. Antibody against the 37-kDa protein band first was identified at the onset of patency, reaching a 90% prevalence rate by 90 days postinfection (DPI). The prevalence of this antibody remained high. Antibody recognition of the 21-kDa protein band first occurred at 90 DPI and gradually increased in prevalence during the course of infection temporally similar to the increase in microfilaremia. Recognition of the 17-kDa protein band first occurred at 48 DPI, reached a maximum prevalence of 80% at 90 DPI, and decreased to a minimal prevalence by 160 DPI. Prevalence of antibody responses to the 17-kDa protein band corresponded temporally with the kinetics of the rise and fall of numbers of intralymphatic thrombi. The patterns of antibody response to these 3 bands were similar in both singly and multiply inoculated animals.(ABSTRACT TRUNCATED AT 250 WORDS)
PubMed: 1919919
Affiliations:
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Coleman</name></author></analytic><series><title level="j">The Journal of parasitology</title><idno type="ISSN">0022-3395</idno><imprint><date when="1991" type="published">1991</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Antibodies, Helminth (biosynthesis)</term><term>Antibodies, Helminth (blood)</term><term>Antigens, Helminth (analysis)</term><term>Antigens, Helminth (chemistry)</term><term>Antigens, Helminth (immunology)</term><term>Blotting, Western</term><term>Brugia (immunology)</term><term>Disease Models, Animal</term><term>Electrophoresis, Polyacrylamide Gel</term><term>Elephantiasis, Filarial (immunology)</term><term>Enzyme-Linked Immunosorbent Assay</term><term>Female</term><term>Gerbillinae</term><term>Helminth Proteins (analysis)</term><term>Helminth Proteins (chemistry)</term><term>Helminth Proteins (immunology)</term><term>Male</term><term>Molecular Weight</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term><term>Anticorps antihelminthe (biosynthèse)</term><term>Anticorps antihelminthe (sang)</term><term>Antigènes d'helminthe ()</term><term>Antigènes d'helminthe (analyse)</term><term>Antigènes d'helminthe (immunologie)</term><term>Brugia (immunologie)</term><term>Femelle</term><term>Filariose lymphatique (immunologie)</term><term>Gerbillinae</term><term>Masse moléculaire</term><term>Modèles animaux de maladie humaine</term><term>Mâle</term><term>Protéines d'helminthes ()</term><term>Protéines d'helminthes (analyse)</term><term>Protéines d'helminthes (immunologie)</term><term>Technique de Western</term><term>Test ELISA</term><term>Électrophorèse sur gel de polyacrylamide</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Antigens, Helminth</term><term>Helminth Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Antibodies, Helminth</term></keywords><keywords scheme="MESH" type="chemical" qualifier="blood" xml:lang="en"><term>Antibodies, Helminth</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Antigens, Helminth</term><term>Helminth Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="immunology" xml:lang="en"><term>Antigens, Helminth</term><term>Helminth Proteins</term></keywords><keywords scheme="MESH" qualifier="analyse" xml:lang="fr"><term>Antigènes d'helminthe</term><term>Protéines d'helminthes</term></keywords><keywords scheme="MESH" qualifier="biosynthèse" xml:lang="fr"><term>Anticorps antihelminthe</term></keywords><keywords scheme="MESH" qualifier="immunologie" xml:lang="fr"><term>Antigènes d'helminthe</term><term>Brugia</term><term>Filariose lymphatique</term><term>Protéines d'helminthes</term></keywords><keywords scheme="MESH" qualifier="immunology" 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and multiply inoculated with Brugia pahangi infective larvae (L3), to soluble somatic extracts of adult parasites were characterized by western blot analysis. Forty-two protein bands ranging in molecular weight from 12 to 160 kDa were recognized by sera from infected jirds. Antibody recognition of individual B. pahangi antigen bands in this assay appears to be independent of antibody enzyme-linked immunosorbent assay (ELISA) titers to crude parasite extract, severity of lymphatic lesions, levels of microfilaremia, numbers of L3 inoculated, or numbers of adult parasites in individual jirds. Antibody recognition of protein bands with molecular weights of 37 kDa, 21 kDa, and 17 kDa, however, did temporally correspond with certain parasitological and pathologic events. Antibody against the 37-kDa protein band first was identified at the onset of patency, reaching a 90% prevalence rate by 90 days postinfection (DPI). The prevalence of this antibody remained high. Antibody recognition of the 21-kDa protein band first occurred at 90 DPI and gradually increased in prevalence during the course of infection temporally similar to the increase in microfilaremia. Recognition of the 17-kDa protein band first occurred at 48 DPI, reached a maximum prevalence of 80% at 90 DPI, and decreased to a minimal prevalence by 160 DPI. Prevalence of antibody responses to the 17-kDa protein band corresponded temporally with the kinetics of the rise and fall of numbers of intralymphatic thrombi. The patterns of antibody response to these 3 bands were similar in both singly and multiply inoculated animals.(ABSTRACT TRUNCATED AT 250 WORDS)</div></front></TEI><affiliations><list></list><tree><noCountry><name sortKey="Coleman, S U" sort="Coleman, S U" uniqKey="Coleman S" first="S U" last="Coleman">S U Coleman</name><name sortKey="Farrar, R G" sort="Farrar, R G" uniqKey="Farrar R" first="R G" last="Farrar">R G Farrar</name><name sortKey="Klei, T R" sort="Klei, T R" uniqKey="Klei T" first="T R" last="Klei">T R Klei</name><name sortKey="Mcvay, C S" sort="Mcvay, C S" uniqKey="Mcvay C" first="C S" last="Mcvay">C S Mcvay</name></noCountry></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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