Cargando…

Evaluation of a novel antibody to define histone 3.3 G34R mutant brain tumours

Missense somatic mutations affecting histone H3.1 and H3.3 proteins are now accepted as the hallmark of paediatric diffuse intrinsic pontine gliomas (DIPG), non-brain stem paediatric high grade gliomas (pHGG) as well as a subset of adult glioblastoma multiforme (GBM). Different mutations give rise t...

Descripción completa

Detalles Bibliográficos
Autores principales: Haque, Farhana, Varlet, Pascale, Puntonet, Julien, Storer, Lisa, Bountali, Aikaterini, Rahman, Ruman, Grill, Jacques, Carcaboso, Angel M, Jones, Chris, Layfield, Robert, Grundy, Richard G
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5461722/
https://www.ncbi.nlm.nih.gov/pubmed/28587626
http://dx.doi.org/10.1186/s40478-017-0449-1
_version_ 1783242393959530496
author Haque, Farhana
Varlet, Pascale
Puntonet, Julien
Storer, Lisa
Bountali, Aikaterini
Rahman, Ruman
Grill, Jacques
Carcaboso, Angel M
Jones, Chris
Layfield, Robert
Grundy, Richard G
author_facet Haque, Farhana
Varlet, Pascale
Puntonet, Julien
Storer, Lisa
Bountali, Aikaterini
Rahman, Ruman
Grill, Jacques
Carcaboso, Angel M
Jones, Chris
Layfield, Robert
Grundy, Richard G
author_sort Haque, Farhana
collection PubMed
description Missense somatic mutations affecting histone H3.1 and H3.3 proteins are now accepted as the hallmark of paediatric diffuse intrinsic pontine gliomas (DIPG), non-brain stem paediatric high grade gliomas (pHGG) as well as a subset of adult glioblastoma multiforme (GBM). Different mutations give rise to one of three amino acid substitutions at two critical positions within the histone tails, K27M, G34R/V. Several studies have highlighted gene expression and epigenetic changes associated with histone H3 mutations; however their precise roles in tumourigenesis remain incompletely understood. Determining how such amino acid substitutions in a protein affect its properties can be challenging because of difficulties in detecting and tracking mutant proteins within cells and tissues. Here we describe a strategy for the generation of antibodies to discriminate G34R and G34V mutant histone H3 proteins from their wild-type counterparts. Antibodies were validated by western blotting and immunocytochemistry, using recombinant H3.3 proteins and paediatric GBM cell lines. The H3-G34R antibody demonstrated a high degree of selectivity towards its target sequence. Accordingly, immunostaining on a cohort of 22 formalin-fixed paraffin embedded tumours with a previously known H3.3 G34R mutation status, detected successfully the corresponding mutant protein in 11/11 G34R cases. Since there was a high concordance between genotype and immunohistochemical analysis of G34R mutant tumour samples, we analysed a series of tissue microarrays (TMAs) to assess the specificity of the antibody in a range of paediatric brain tumours, and noted immunoreactivity in 2/634 cases. Importantly, we describe the generation and validation of highly specific antibodies for G34 mutations. Overall our work adds to an extremely valuable portfolio of antibodies, not only for histopathologic detection of tumour-associated mutant histone sequences, but also facilitating the study of spatial/anatomical aspects of tumour formation and the identification of downstream targets and pathways in malignant glioma progression.
format Online
Article
Text
id pubmed-5461722
institution National Center for Biotechnology Information
language English
publishDate 2017
publisher BioMed Central
record_format MEDLINE/PubMed
spelling pubmed-54617222017-06-07 Evaluation of a novel antibody to define histone 3.3 G34R mutant brain tumours Haque, Farhana Varlet, Pascale Puntonet, Julien Storer, Lisa Bountali, Aikaterini Rahman, Ruman Grill, Jacques Carcaboso, Angel M Jones, Chris Layfield, Robert Grundy, Richard G Acta Neuropathol Commun Research Missense somatic mutations affecting histone H3.1 and H3.3 proteins are now accepted as the hallmark of paediatric diffuse intrinsic pontine gliomas (DIPG), non-brain stem paediatric high grade gliomas (pHGG) as well as a subset of adult glioblastoma multiforme (GBM). Different mutations give rise to one of three amino acid substitutions at two critical positions within the histone tails, K27M, G34R/V. Several studies have highlighted gene expression and epigenetic changes associated with histone H3 mutations; however their precise roles in tumourigenesis remain incompletely understood. Determining how such amino acid substitutions in a protein affect its properties can be challenging because of difficulties in detecting and tracking mutant proteins within cells and tissues. Here we describe a strategy for the generation of antibodies to discriminate G34R and G34V mutant histone H3 proteins from their wild-type counterparts. Antibodies were validated by western blotting and immunocytochemistry, using recombinant H3.3 proteins and paediatric GBM cell lines. The H3-G34R antibody demonstrated a high degree of selectivity towards its target sequence. Accordingly, immunostaining on a cohort of 22 formalin-fixed paraffin embedded tumours with a previously known H3.3 G34R mutation status, detected successfully the corresponding mutant protein in 11/11 G34R cases. Since there was a high concordance between genotype and immunohistochemical analysis of G34R mutant tumour samples, we analysed a series of tissue microarrays (TMAs) to assess the specificity of the antibody in a range of paediatric brain tumours, and noted immunoreactivity in 2/634 cases. Importantly, we describe the generation and validation of highly specific antibodies for G34 mutations. Overall our work adds to an extremely valuable portfolio of antibodies, not only for histopathologic detection of tumour-associated mutant histone sequences, but also facilitating the study of spatial/anatomical aspects of tumour formation and the identification of downstream targets and pathways in malignant glioma progression. BioMed Central 2017-06-06 /pmc/articles/PMC5461722/ /pubmed/28587626 http://dx.doi.org/10.1186/s40478-017-0449-1 Text en © The Author(s). 2017 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.
spellingShingle Research
Haque, Farhana
Varlet, Pascale
Puntonet, Julien
Storer, Lisa
Bountali, Aikaterini
Rahman, Ruman
Grill, Jacques
Carcaboso, Angel M
Jones, Chris
Layfield, Robert
Grundy, Richard G
Evaluation of a novel antibody to define histone 3.3 G34R mutant brain tumours
title Evaluation of a novel antibody to define histone 3.3 G34R mutant brain tumours
title_full Evaluation of a novel antibody to define histone 3.3 G34R mutant brain tumours
title_fullStr Evaluation of a novel antibody to define histone 3.3 G34R mutant brain tumours
title_full_unstemmed Evaluation of a novel antibody to define histone 3.3 G34R mutant brain tumours
title_short Evaluation of a novel antibody to define histone 3.3 G34R mutant brain tumours
title_sort evaluation of a novel antibody to define histone 3.3 g34r mutant brain tumours
topic Research
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5461722/
https://www.ncbi.nlm.nih.gov/pubmed/28587626
http://dx.doi.org/10.1186/s40478-017-0449-1
work_keys_str_mv AT haquefarhana evaluationofanovelantibodytodefinehistone33g34rmutantbraintumours
AT varletpascale evaluationofanovelantibodytodefinehistone33g34rmutantbraintumours
AT puntonetjulien evaluationofanovelantibodytodefinehistone33g34rmutantbraintumours
AT storerlisa evaluationofanovelantibodytodefinehistone33g34rmutantbraintumours
AT bountaliaikaterini evaluationofanovelantibodytodefinehistone33g34rmutantbraintumours
AT rahmanruman evaluationofanovelantibodytodefinehistone33g34rmutantbraintumours
AT grilljacques evaluationofanovelantibodytodefinehistone33g34rmutantbraintumours
AT carcabosoangelm evaluationofanovelantibodytodefinehistone33g34rmutantbraintumours
AT joneschris evaluationofanovelantibodytodefinehistone33g34rmutantbraintumours
AT layfieldrobert evaluationofanovelantibodytodefinehistone33g34rmutantbraintumours
AT grundyrichardg evaluationofanovelantibodytodefinehistone33g34rmutantbraintumours