Five Residues in the Apical Loop of the Respiratory Syncytial Virus Fusion Protein F₂ Subunit Are Critical for Its Fusion Activity.

ABSTRACT: The respiratory syncytial virus (RSV) fusion (F) protein is a trimeric, membrane-anchored glycoprotein capable of mediating both virus-target cell membrane fusion to initiate infection and cell-cell fusion, even in the absence of the attachment glycoprotein. The F protein is initially expressed in a precursor form, whose functional capabilities are activated by proteolysis at two sites between the F₁ and F₂ subunits. This cleavage results in expression of the metastable and high-energy prefusion conformation. To mediate fusion, the F protein is triggered by an unknown stimulus, causing the F₁ subunit to refold dramatically while F₂ changes minimally. Hypothesizing that the most likely site for interaction with a target cell component would be the

SUBMITTER: Hicks SN 

PROVIDER: S-EPMC6052300 | biostudies-literature | 2018 Aug

REPOSITORIES: biostudies-literature