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Identification of the hASCT2-binding domain of the Env ERVWE1/syncytin-1 fusogenic glycoprotein

The cellular HERV-W envelope/syncytin-1 protein, encoded by the envelope gene of the ERVWE1 proviral locus is a fusogenic glycoprotein probably involved in the formation of the placental syncytiotrophoblast layer. Syncytin-1-induced in vitro cell-cell fusion is dependent on the interaction with hASC...

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Detalhes bibliográficos
Main Authors: Cheynet, Valérie, Oriol, Guy, Mallet, François
Formato: Artigo
Idioma:English
Publicado em: BioMed Central 2006
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Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC1524976/
https://ncbi.nlm.nih.gov/pubmed/16820059
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1186/1742-4690-3-41
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Resumo:The cellular HERV-W envelope/syncytin-1 protein, encoded by the envelope gene of the ERVWE1 proviral locus is a fusogenic glycoprotein probably involved in the formation of the placental syncytiotrophoblast layer. Syncytin-1-induced in vitro cell-cell fusion is dependent on the interaction with hASCT2. As no receptor binding domain has been clearly defined in the SU of neither the HERV-W Env nor the retroviruses of the same interference group, we designed an in vitro binding assay to evaluate the interaction of the HERV-W envelope with the hASCT2 receptor. Using truncated HERV-W SU subunits, a region consisting of the N-terminal 124 amino acids of the mature SU glycoprotein was determined as the minimal receptor-binding domain. This domain contains several sub-domains which are poorly conserved among retroviruses of this interference group but a region of 18 residus containing the SDGGGX(2)DX(2)R conserved motif was proved to be essential for syncytin-1-hASCT2 interaction.