Scripps VIVO scripps research logo

  • Index
  • Log in
  • Home
  • People
  • Organizations
  • Research
  • Events
Search form

Identification of a region in the stalk domain of the nipah virus receptor binding protein that is critical for fusion activation

Academic Article
uri icon
  • Overview
  • Identity
  • Additional Document Info
  • View All
scroll to property group menus

Overview

authors

  • Talekar, A.
  • DeVito, I.
  • Salah, Z.
  • Palmer, S. G.
  • Chattopadhyay, A.
  • Rose, J. K.
  • Xu, R.
  • Wilson, Ian
  • Moscona, A.
  • Porotto, M.

publication date

  • October 2013

journal

  • Journal of Virology  Journal

abstract

  • Paramyxoviruses, including the emerging lethal human Nipah virus (NiV) and the avian Newcastle disease virus (NDV), enter host cells through fusion of the viral and target cell membranes. For paramyxoviruses, membrane fusion is the result of the concerted action of two viral envelope glycoproteins: a receptor binding protein and a fusion protein (F). The NiV receptor binding protein (G) attaches to ephrin B2 or B3 on host cells, whereas the corresponding hemagglutinin-neuraminidase (HN) attachment protein of NDV interacts with sialic acid moieties on target cells through two regions of its globular domain. Receptor-bound G or HN via its stalk domain triggers F to undergo the conformational changes that render it competent to mediate fusion of the viral and cellular membranes. We show that chimeric proteins containing the NDV HN receptor binding regions and the NiV G stalk domain require a specific sequence at the connection between the head and the stalk to activate NiV F for fusion. Our findings are consistent with a general mechanism of paramyxovirus fusion activation in which the stalk domain of the receptor binding protein is responsible for F activation and a specific connecting region between the receptor binding globular head and the fusion-activating stalk domain is required for transmitting the fusion signal.

subject areas

  • Cell Line
  • DNA Mutational Analysis
  • Humans
  • Newcastle disease virus
  • Nipah Virus
  • Protein Interaction Mapping
  • Recombinant Proteins
  • Viral Envelope Proteins
  • Virus Internalization
scroll to property group menus

Identity

PubMed Central ID

  • PMC3807285

International Standard Serial Number (ISSN)

  • 0022-538X

Digital Object Identifier (DOI)

  • 10.1128/jvi.01646-13

PubMed ID

  • 23903846
scroll to property group menus

Additional Document Info

start page

  • 10980

end page

  • 10996

volume

  • 87

issue

  • 20

©2021 The Scripps Research Institute | Terms of Use | Powered by VIVO

  • About
  • Contact Us
  • Support