The complexity of screening PMS2 in DNA isolated from formalin-fixed paraffin-embedded material.


Journal

European journal of human genetics : EJHG
ISSN: 1476-5438
Titre abrégé: Eur J Hum Genet
Pays: England
ID NLM: 9302235

Informations de publication

Date de publication:
03 2020
Historique:
received: 25 09 2018
accepted: 27 09 2019
revised: 19 09 2019
pubmed: 17 10 2019
medline: 1 5 2021
entrez: 17 10 2019
Statut: ppublish

Résumé

Germline variants in the DNA mismatch repair (MMR) gene PMS2 cause 1-14% of all Lynch Syndrome cancers. Correct variant analysis of PMS2 is complex due to the presence of multiple pseudogenes and the occurrence of gene conversion. The analysis complexity increases in highly fragmented DNA from formalin-fixed paraffin-embedded (FFPE) tissue. Here we describe a reliable approach to detect true PMS2 variants in fragmented DNA. A custom NGS panel designed for FFPE tissue was used targeting four MMR genes, POLE and POLD1. Amplicon design for PMS2 was based on the position of paralogous sequence variants (PSVs) that distinguish PMS2 from its pseudogenes. PMS2 variants in exons 1-11 can be correctly curated based on this information. For exons 12-15 this is less reliable as these undergo gene conversion. Using this method, we screened PMS2 variants in 125 MMR-deficient tumors. Of the 125 tumors tested, six were unexplained MMR-deficient tumors with solitary PMS2 protein expression loss. In these six tumors two unclassified variants (class 3) and five variants likely affecting function (class 4/5) were detected in PMS2. One microsatellite unstable tumor with positive staining for all MMR proteins was found to carry a frameshift PMS2 variant (class 5). No class 4 or class 5 PMS2 variants were detected in tumors with other patterns of MMR protein expression loss.

Identifiants

pubmed: 31616036
doi: 10.1038/s41431-019-0527-x
pii: 10.1038/s41431-019-0527-x
pmc: PMC7028990
doi:

Substances chimiques

Poly-ADP-Ribose Binding Proteins 0
Formaldehyde 1HG84L3525
DNA 9007-49-2
POLD1 protein, human EC 2.7.7.-
DNA Polymerase II EC 2.7.7.7
DNA Polymerase III EC 2.7.7.7
POLE protein, human EC 2.7.7.7
PMS2 protein, human EC 3.6.1.-
Mismatch Repair Endonuclease PMS2 EC 3.6.1.3

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

333-338

Subventions

Organisme : KWF Kankerbestrijding (Dutch Cancer Society)
ID : UL2012-5542
Pays : International
Organisme : KWF Kankerbestrijding (Dutch Cancer Society)
ID : UL2012-5542
Pays : International
Organisme : KWF Kankerbestrijding (Dutch Cancer Society)
ID : UL2012-5542
Pays : International

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Auteurs

Anne M L Jansen (AML)

Department of Pathology, Leiden University Medical Center, Leiden, The Netherlands.
Department of Human Genetics, Leiden University Medical Center, Leiden, The Netherlands.

Carli M J Tops (CMJ)

Department of Clinical Genetics, Leiden University Medical Center, Leiden, The Netherlands.

Dina Ruano (D)

Department of Pathology, Leiden University Medical Center, Leiden, The Netherlands.

Ronald van Eijk (R)

Department of Pathology, Leiden University Medical Center, Leiden, The Netherlands.

Juul T Wijnen (JT)

Department of Clinical Genetics, Leiden University Medical Center, Leiden, The Netherlands.

Sanne Ten Broeke (S)

Department of Clinical Genetics, Leiden University Medical Center, Leiden, The Netherlands.

Maartje Nielsen (M)

Department of Clinical Genetics, Leiden University Medical Center, Leiden, The Netherlands.

Frederik J Hes (FJ)

Department of Clinical Genetics, Leiden University Medical Center, Leiden, The Netherlands.

Tom van Wezel (T)

Department of Pathology, Leiden University Medical Center, Leiden, The Netherlands.

Hans Morreau (H)

Department of Pathology, Leiden University Medical Center, Leiden, The Netherlands. j.morreau@lumc.nl.

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