Crucial epitopes of Wuchereria bancrofti abundant larval transcript recognized in natural infection.
Identifieur interne : 005964 ( Main/Exploration ); précédent : 005963; suivant : 005965Crucial epitopes of Wuchereria bancrofti abundant larval transcript recognized in natural infection.
Auteurs : J. Madhumathi [Inde] ; D. Pradiba ; P R Prince ; P J Jeyaprita ; D N Rao ; P. KalirajSource :
- European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology [ 1435-4373 ] ; 2010.
Descripteurs français
- KwdFr :
- Animaux, Anticorps antihelminthe (immunologie), Anticorps antihelminthe (sang), Antigènes d'helminthe (), Antigènes d'helminthe (immunologie), Données de séquences moléculaires, Filariose lymphatique (immunologie), Filariose lymphatique (parasitologie), Humains, Immunoglobuline G (sang), Isotypes des immunoglobulines, Larve (immunologie), Peptides (), Peptides (synthèse chimique), Protéines d'helminthes (), Protéines d'helminthes (immunologie), Souris, Séquence d'acides aminés, Wuchereria bancrofti (croissance et développement), Wuchereria bancrofti (immunologie), Wuchereria bancrofti (pathogénicité), Épitopes (), Épitopes (immunologie).
- MESH :
- croissance et développement : Wuchereria bancrofti.
- immunologie : Anticorps antihelminthe, Antigènes d'helminthe, Filariose lymphatique, Larve, Protéines d'helminthes, Wuchereria bancrofti, Épitopes.
- parasitologie : Filariose lymphatique.
- pathogénicité : Wuchereria bancrofti.
- sang : Anticorps antihelminthe, Immunoglobuline G.
- synthèse chimique : Peptides.
- Animaux, Antigènes d'helminthe, Données de séquences moléculaires, Humains, Isotypes des immunoglobulines, Peptides, Protéines d'helminthes, Souris, Séquence d'acides aminés, Épitopes.
English descriptors
- KwdEn :
- Amino Acid Sequence, Animals, Antibodies, Helminth (blood), Antibodies, Helminth (immunology), Antigens, Helminth (chemistry), Antigens, Helminth (immunology), Elephantiasis, Filarial (immunology), Elephantiasis, Filarial (parasitology), Epitopes (chemistry), Epitopes (immunology), Helminth Proteins (chemistry), Helminth Proteins (immunology), Humans, Immunoglobulin G (blood), Immunoglobulin Isotypes, Larva (immunology), Mice, Molecular Sequence Data, Peptides (chemical synthesis), Peptides (chemistry), Wuchereria bancrofti (growth & development), Wuchereria bancrofti (immunology), Wuchereria bancrofti (pathogenicity).
- MESH :
- chemical , blood : Antibodies, Helminth, Immunoglobulin G.
- chemical , chemical synthesis : Peptides.
- chemical , chemistry : Antigens, Helminth, Epitopes, Helminth Proteins, Peptides.
- chemical , immunology : Antibodies, Helminth, Antigens, Helminth, Epitopes, Helminth Proteins.
- growth & development : Wuchereria bancrofti.
- immunology : Elephantiasis, Filarial, Larva, Wuchereria bancrofti.
- parasitology : Elephantiasis, Filarial.
- pathogenicity : Wuchereria bancrofti.
- Amino Acid Sequence, Animals, Humans, Immunoglobulin Isotypes, Mice, Molecular Sequence Data.
Abstract
Lymphatic filariasis is a tropical disease, with over 40 million people seriously incapacitated due to lymphangitis and elephantiasis. Over 99% of infections are caused by the nematode Wuchereria bancrofti. Expressed sequence tag (EST) analysis of filarial genome identified novel infective larval (L3) stage-specific antigen, abundant larval transcript (ALT-2), which was shown to be highly essential for parasite establishment and survival in the host. The unique structural features and immunological characteristics of ALT-2 indicate the presence of critical motifs that needs to be explored in natural human infection for understanding and management of the disease. In order to dissect the epitopes of ALT protein recognized in humans, eight peptides spanning the entire protein sequence were selected based on in-silico epitope prediction and synthesized. Analysis of the reactivity of W. bancrofti ALT-2 synthetic peptides with clinical sera (n = 40) from endemic areas identified epitopes recognized by putatively immune sera, of which two comprise the highly variable acidic domain (21-60). Interestingly, our study also revealed crucial epitopes recognized by microfilaremic (MF) sera with significantly high IgG4 isotype (p < 0.001), implicated in immunomodulation. The epitope peptides identified were highly specific for MF sera and, thus, have the potential to be exploited as diagnostic markers.
DOI: 10.1007/s10096-010-1026-8
PubMed: 20803227
Affiliations:
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Le document en format XML
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<term>Antibodies, Helminth (immunology)</term>
<term>Antigens, Helminth (chemistry)</term>
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<term>Elephantiasis, Filarial (immunology)</term>
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<term>Epitopes (immunology)</term>
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<term>Wuchereria bancrofti (immunology)</term>
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<term>Antigènes d'helminthe (immunologie)</term>
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<term>Filariose lymphatique (parasitologie)</term>
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<term>Peptides (synthèse chimique)</term>
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<term>Séquence d'acides aminés</term>
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<term>Molecular Sequence Data</term>
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<term>Isotypes des immunoglobulines</term>
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<front><div type="abstract" xml:lang="en">Lymphatic filariasis is a tropical disease, with over 40 million people seriously incapacitated due to lymphangitis and elephantiasis. Over 99% of infections are caused by the nematode Wuchereria bancrofti. Expressed sequence tag (EST) analysis of filarial genome identified novel infective larval (L3) stage-specific antigen, abundant larval transcript (ALT-2), which was shown to be highly essential for parasite establishment and survival in the host. The unique structural features and immunological characteristics of ALT-2 indicate the presence of critical motifs that needs to be explored in natural human infection for understanding and management of the disease. In order to dissect the epitopes of ALT protein recognized in humans, eight peptides spanning the entire protein sequence were selected based on in-silico epitope prediction and synthesized. Analysis of the reactivity of W. bancrofti ALT-2 synthetic peptides with clinical sera (n = 40) from endemic areas identified epitopes recognized by putatively immune sera, of which two comprise the highly variable acidic domain (21-60). Interestingly, our study also revealed crucial epitopes recognized by microfilaremic (MF) sera with significantly high IgG4 isotype (p < 0.001), implicated in immunomodulation. The epitope peptides identified were highly specific for MF sera and, thus, have the potential to be exploited as diagnostic markers.</div>
</front>
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