Structure and function study of paramyxovirus fusion protein heptad repeat peptides

Paramyxovirus might adopt a molecular mechanism of membrane fusion similar to that of other class I viruses in which the heptad repeat (HR) regions of fusion protein (F) HR1 and HR2 form a six-helix bundle structure inducing membrane fusion. In this study, we examined the structure and function of H...

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Detalles Bibliográficos
Autores principales: Wang, Xiao-Jia, Bai, Ya-Duo, Zhang, Guo-Zhong, Zhao, Ji-Xun, Wang, Ming, Gao, George F.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Published by Elsevier Inc. 2005
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7094221/
https://www.ncbi.nlm.nih.gov/pubmed/15797244
http://dx.doi.org/10.1016/j.abb.2005.02.004
Descripción
Sumario:Paramyxovirus might adopt a molecular mechanism of membrane fusion similar to that of other class I viruses in which the heptad repeat (HR) regions of fusion protein (F) HR1 and HR2 form a six-helix bundle structure inducing membrane fusion. In this study, we examined the structure and function of HR1 and HR2 from the avian paramyxovirus-2 (APMV-2) F protein. The study showed that APMV-2 HR1 and HR2 formed a stable six-helix bundle. Only a soluble APMV-2 HR2 peptide showed potent and specific virus-cell fusion inhibition activity. Cross-inhibiting activity with APMV-1 (Newcastle disease virus, NDV) was not found. A possible mechanism of membrane fusion inhibition by the paramyxovirus HR2 peptide is discussed.

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