Hb Wilde and Hb Patagonia: two novel elongated beta-globin variants causing dominant beta-thalassemia

We describe here the molecular and hematological characteristics of novel frameshift mutations in exon 2 of the HBB gene (in heterozygous state) found in two Argentinean pediatric patients with dominant b-thalassemia-like features. In Hb Wilde, HBB:c.270_273delTGAG(p.Glu90Cysfs*67), we detected the...

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Detalhes bibliográficos
Autores: Scheps, Karen, Hasenahuer, Marcia Anahí, Parisi, Gustavo Daniel, Fornasari, Maria Silvina, Pennesi, Sandra P., Erramouspe, Beatriz, Basack, Felisa N., Veber, Ernesto S., Aversa, Luis, Elena, Graciela, Varela, Viviana
Formato: artículo
Estado:Versión publicada
Fecha de publicación:2014
País:Argentina
Recursos:Consejo Nacional de Investigaciones Científicas y Técnicas
Repositorio:CONICET Digital (CONICET)
Idioma:inglés
OAI Identifier:oai:ri.conicet.gov.ar:11336/105265
Acesso em linha:http://hdl.handle.net/11336/105265
Access Level:acceso abierto
Palavra-chave:elongated beta-globin
protein structure
dominant beta-thalassemia
frameshift mutations
https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
https://purl.org/becyt/ford/3.3
https://purl.org/becyt/ford/3
https://purl.org/becyt/ford/1.2
Descrição
Resumo:We describe here the molecular and hematological characteristics of novel frameshift mutations in exon 2 of the HBB gene (in heterozygous state) found in two Argentinean pediatric patients with dominant b-thalassemia-like features. In Hb Wilde, HBB:c.270_273delTGAG(p.Glu90Cysfs*67), we detected the deletion of the third base of the codon 89 (T) and the codon 90 (GAG), whereas in Hb Patagonia, HBB: c.296_297dupGT(p.Asp99Trpfs*59), the frameshift mutation was due to a duplication of a ‘GT’ dinucleotide after the second base of codon 98 (GTG). The Hb Patagonia and Hb Wilde mutations would result in elongated b-globin chains with modified C-terminal sequences and a total of 155 and 157 amino acids residues, respectively. Based on bioinformatics and structural analysis, as well as protein modeling, we predict that the elongated b-globins would affect the formation of the ab dimers and their stability, which would further support the mechanism for the observed clinical features in both patients.