Horizon / Plein textes La base de ressources documentaires de l'IRD

IRD

Publications des scientifiques de l'IRD

Dambrun Magalie, Dechavanne Célia, Emmanuel Alexandra, Aussenac Florentin, Leduc M., Giangrande C., Vinh J., Dugoujon J. M., Lefranc M. P., Guillonneau F., Migot Nabias Florence. (2017). Human immunoglobulin heavy gamma chain polymorphisms : molecular confirmation of proteomic assessment. Molecular and Cellular Proteomics, 16 (5), 824-839. ISSN 1535-9476

Accès réservé (Intranet IRD) Document en accès réservé (Intranet IRD)

Lien direct chez l'éditeur doi:10.1074/mcp.M116.064733

Titre
Human immunoglobulin heavy gamma chain polymorphisms : molecular confirmation of proteomic assessment
Année de publication2017
Type de documentArticle référencé dans le Web of Science WOS:000400759600010
AuteursDambrun Magalie, Dechavanne Célia, Emmanuel Alexandra, Aussenac Florentin, Leduc M., Giangrande C., Vinh J., Dugoujon J. M., Lefranc M. P., Guillonneau F., Migot Nabias Florence.
SourceMolecular and Cellular Proteomics, 2017, 16 (5), p. 824-839. ISSN 1535-9476
RésuméImmunoglobulin G (IgG) proteins are known for the huge diversity of the variable domains of their heavy and light chains, aimed at protecting each individual against foreign antigens. The IgG also harbor specific polymorphism concentrated in the CH2 and CH3-CHS constant regions located on the Fc fragment of their heavy chains. But this individual particularity relies only on a few amino acids among which some could make accurate sequence determination a challenge for mass spectrometry-based techniques. The purpose of the study was to bring a molecular validation of proteomic results by the sequencing of encoding DNA fragments. It was performed using ten individual samples (DNA and sera) selected on the basis of their Gm (gamma marker) allotype polymorphism in order to cover the main immunoglobulin heavy gamma (IGHG) gene diversity. Gm allotypes, reflecting part of this diversity, were determined by a serological method. On its side, the IGH locus comprises four functional IGHG genes totalizing 34 alleles and encoding the four IgG subclasses. The genomic study focused on the nucleotide polymorphism of the CH2 and CH3-CHS exons and of the intron. Despite strong sequence identity, four pairs of specific gene amplification primers could be designed. Additional primers were identified to perform the subsequent sequencing. The nucleotide sequences obtained were first assigned to a specific IGHG gene, and then IGHG alleles were deduced using a home-made decision tree reading of the nucleotide sequences. IGHG amino acid (AA) alleles were determined by mass spectrometry. Identical results were found at 95% between alleles identified by proteomics and those deduced from genomics. These results validate the proteomic approach which could be used for diagnostic purposes, namely for a mother-and-child differential IGHG detection in a context of suspicion of congenital infection.
Plan de classementSciences fondamentales / Techniques d'analyse et de recherche [020]
LocalisationFonds IRD
Identifiant IRDPAR00016039
Lien permanenthttp://www.documentation.ird.fr/hor/PAR00016039

Export des données

Disponibilité des documents

Télechargment fichier PDF téléchargeable

Lien sur le Web lien chez l'éditeur

Accès réservé en accès réservé

HAL en libre accès sur HAL


Accès aux documents originaux :

Accès direct

Bureau du chercheur

Site de la documentation

Espace intranet IST (accès réservé)

Suivi des publications IRD (accès réservé)

Mentions légales

Services Horizon

Poser une question

Consulter l'aide en ligne

Déposer une publication (accès réservé)

S'abonner au flux RSS

Voir les tableaux chronologiques et thématiques

Centres de documentation

Bondy

Montpellier (centre IRD)

Montpellier (MSE)

Nouméa

Papeete

Niamey

Ouagadougou

Tunis

La Paz

Quito