@article{fdi:010071134,
  title = {{H}uman immunoglobulin heavy gamma chain polymorphisms : molecular confirmation of proteomic assessment},
  author = {{D}ambrun, {M}agalie and {D}echavanne, {C}{\'e}lia and {E}mmanuel, {A}lexandra and {A}ussenac, {F}lorentin and {L}educ, {M}. and {G}iangrande, {C}. and {V}inh, {J}. and {D}ugoujon, {J}. {M}. and {L}efranc, {M}. {P}. and {G}uillonneau, {F}. and {M}igot {N}abias, {F}lorence},
  editor = {},
  language = {{ENG}},
  abstract = {{I}mmunoglobulin {G} ({I}g{G}) 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. {T}he {I}g{G} also harbor specific polymorphism concentrated in the {CH}2 and {CH}3-{CHS} constant regions located on the {F}c fragment of their heavy chains. {B}ut 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. {T}he purpose of the study was to bring a molecular validation of proteomic results by the sequencing of encoding {DNA} fragments. {I}t was performed using ten individual samples ({DNA} and sera) selected on the basis of their {G}m (gamma marker) allotype polymorphism in order to cover the main immunoglobulin heavy gamma ({IGHG}) gene diversity. {G}m allotypes, reflecting part of this diversity, were determined by a serological method. {O}n its side, the {IGH} locus comprises four functional {IGHG} genes totalizing 34 alleles and encoding the four {I}g{G} subclasses. {T}he genomic study focused on the nucleotide polymorphism of the {CH}2 and {CH}3-{CHS} exons and of the intron. {D}espite strong sequence identity, four pairs of specific gene amplification primers could be designed. {A}dditional primers were identified to perform the subsequent sequencing. {T}he 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. {I}dentical results were found at 95% between alleles identified by proteomics and those deduced from genomics. {T}hese 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.},
  keywords = {},
  booktitle = {},
  journal = {{M}olecular and {C}ellular {P}roteomics},
  volume = {16},
  numero = {5},
  pages = {824--839},
  ISSN = {1535-9476},
  year = {2017},
  DOI = {10.1074/mcp.{M}116.064733},
  URL = {https://www.documentation.ird.fr/hor/fdi:010071134},
}