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Title: Timing is everything: Fine-tuned molecular machines orchestrate paramyxovirus entry

Abstract

The Paramyxoviridae include some of the great and ubiquitous disease-causing viruses of humans and animals. In most paramyxoviruses, two viral membrane glycoproteins, fusion protein (F) and receptor binding protein (HN, H or G) mediate a concerted process of recognition of host cell surface molecules followed by fusion of viral and cellular membranes, resulting in viral nucleocapsid entry into the cytoplasm. The interactions between the F and HN, H or G viral glycoproteins and host molecules are critical in determining host range, virulence and spread of these viruses. Recently, atomic structures, together with biochemical and biophysical studies, have provided major insights into how these two viral glycoproteins successfully interact with host receptors on cellular membranes and initiate the membrane fusion process to gain entry into cells. These studies highlight the conserved core mechanisms of paramyxovirus entry that provide the fundamental basis for rational anti-viral drug design and vaccine development. - Highlights: • New structural and functional insights into paramyxovirus entry mechanisms. • Current data on paramyxovirus glycoproteins suggest a core conserved entry mechanism. • Diverse mechanisms preventing premature fusion activation exist in these viruses. • Precise spacio-temporal interplay between paramyxovirus glycoproteins initiate entry.

Authors:
 [1];  [2];  [1];  [3]
  1. Department of Molecular Biosciences, Northwestern University, Evanston, IL 60208-3500 (United States)
  2. Department of Structural Biology and Program in Immunology, Stanford University School of Medicine, Stanford, CA 94305 (United States)
  3. (United States)
Publication Date:
OSTI Identifier:
22470172
Resource Type:
Journal Article
Journal Name:
Virology
Additional Journal Information:
Journal Volume: 479-480; Other Information: Copyright (c) 2015 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved.; Country of input: International Atomic Energy Agency (IAEA); Journal ID: ISSN 0042-6822
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; ANIMALS; CYTOPLASM; DESIGN; DISEASES; DRUGS; GAIN; GLYCOPROTEINS; MEMBRANES; MOLECULES; RECEPTORS; SURFACES; VACCINES; VIRULENCE; VIRUSES

Citation Formats

Bose, Sayantan, E-mail: sayantan_bose@hms.harvard.edu, Jardetzky, Theodore S., Lamb, Robert A., E-mail: ralamb@northwestern.edu, and Howard Hughes Medical Institute, Northwestern University, Evanston, IL 60208-3500. Timing is everything: Fine-tuned molecular machines orchestrate paramyxovirus entry. United States: N. p., 2015. Web. doi:10.1016/J.VIROL.2015.02.037.
Bose, Sayantan, E-mail: sayantan_bose@hms.harvard.edu, Jardetzky, Theodore S., Lamb, Robert A., E-mail: ralamb@northwestern.edu, & Howard Hughes Medical Institute, Northwestern University, Evanston, IL 60208-3500. Timing is everything: Fine-tuned molecular machines orchestrate paramyxovirus entry. United States. doi:10.1016/J.VIROL.2015.02.037.
Bose, Sayantan, E-mail: sayantan_bose@hms.harvard.edu, Jardetzky, Theodore S., Lamb, Robert A., E-mail: ralamb@northwestern.edu, and Howard Hughes Medical Institute, Northwestern University, Evanston, IL 60208-3500. Fri . "Timing is everything: Fine-tuned molecular machines orchestrate paramyxovirus entry". United States. doi:10.1016/J.VIROL.2015.02.037.
@article{osti_22470172,
title = {Timing is everything: Fine-tuned molecular machines orchestrate paramyxovirus entry},
author = {Bose, Sayantan, E-mail: sayantan_bose@hms.harvard.edu and Jardetzky, Theodore S. and Lamb, Robert A., E-mail: ralamb@northwestern.edu and Howard Hughes Medical Institute, Northwestern University, Evanston, IL 60208-3500},
abstractNote = {The Paramyxoviridae include some of the great and ubiquitous disease-causing viruses of humans and animals. In most paramyxoviruses, two viral membrane glycoproteins, fusion protein (F) and receptor binding protein (HN, H or G) mediate a concerted process of recognition of host cell surface molecules followed by fusion of viral and cellular membranes, resulting in viral nucleocapsid entry into the cytoplasm. The interactions between the F and HN, H or G viral glycoproteins and host molecules are critical in determining host range, virulence and spread of these viruses. Recently, atomic structures, together with biochemical and biophysical studies, have provided major insights into how these two viral glycoproteins successfully interact with host receptors on cellular membranes and initiate the membrane fusion process to gain entry into cells. These studies highlight the conserved core mechanisms of paramyxovirus entry that provide the fundamental basis for rational anti-viral drug design and vaccine development. - Highlights: • New structural and functional insights into paramyxovirus entry mechanisms. • Current data on paramyxovirus glycoproteins suggest a core conserved entry mechanism. • Diverse mechanisms preventing premature fusion activation exist in these viruses. • Precise spacio-temporal interplay between paramyxovirus glycoproteins initiate entry.},
doi = {10.1016/J.VIROL.2015.02.037},
journal = {Virology},
issn = {0042-6822},
number = ,
volume = 479-480,
place = {United States},
year = {2015},
month = {5}
}