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Title: Domain architecture and oligomerization properties of the paramyxovirus PIV 5 hemagglutinin-neuraminidase (HN) protein

Abstract

The mechanism by which the paramyxovirus hemagglutinin-neuraminidase (HN) protein couples receptor binding to activation of virus entry remains to be fully understood, but the HN stalk is thought to play an important role in the process. We have characterized ectodomain constructs of the parainfluenza virus 5 HN to understand better the underlying architecture and oligomerization properties that may influence HN functions. The PIV 5 neuraminidase (NA) domain is monomeric whereas the ectodomain forms a well-defined tetramer. The HN stalk also forms tetramers and higher order oligomers with high {alpha}-helical content. Together, the data indicate that the globular NA domains form weak intersubunit interactions at the end of the HN stalk tetramer, while stabilizing the stalk and overall oligomeric state of the ectodomain. Electron microscopy of the HN ectodomain reveals flexible arrangements of the NA and stalk domains, which may be important for understanding how these two HN domains impact virus entry.

Authors:
 [1];  [2];  [3];  [2]
  1. Department of Structural Biology, Stanford University, Palo Alto, CA 94305-5126 (United States)
  2. Department of Biochemistry, Molecular Biology and Cell Biology, Northwestern University, Evanston, IL 60208-3500 (United States)
  3. Department of Biochemistry, University of Texas Health Science Center at San Antonio, San Antonio, TX 78229-3901 (United States)
Publication Date:
OSTI Identifier:
21141031
Resource Type:
Journal Article
Journal Name:
Virology
Additional Journal Information:
Journal Volume: 378; Journal Issue: 2; Other Information: DOI: 10.1016/j.virol.2008.05.023; PII: S0042-6822(08)00362-0; Copyright (c) 2008 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; ELECTRON MICROSCOPY; MEMBRANES; RECEPTORS; SIALIC ACID; VIRUSES

Citation Formats

Ping, Yuan, Leser, George P, Demeler, Borries, Lamb, Robert A, Howard Hughes Medical Institute, Northwestern University, Evanston, IL 60208-3500, and Jardetzky, Theodore S. Domain architecture and oligomerization properties of the paramyxovirus PIV 5 hemagglutinin-neuraminidase (HN) protein. United States: N. p., 2008. Web. doi:10.1016/j.virol.2008.05.023.
Ping, Yuan, Leser, George P, Demeler, Borries, Lamb, Robert A, Howard Hughes Medical Institute, Northwestern University, Evanston, IL 60208-3500, & Jardetzky, Theodore S. Domain architecture and oligomerization properties of the paramyxovirus PIV 5 hemagglutinin-neuraminidase (HN) protein. United States. https://doi.org/10.1016/j.virol.2008.05.023
Ping, Yuan, Leser, George P, Demeler, Borries, Lamb, Robert A, Howard Hughes Medical Institute, Northwestern University, Evanston, IL 60208-3500, and Jardetzky, Theodore S. Mon . "Domain architecture and oligomerization properties of the paramyxovirus PIV 5 hemagglutinin-neuraminidase (HN) protein". United States. https://doi.org/10.1016/j.virol.2008.05.023.
@article{osti_21141031,
title = {Domain architecture and oligomerization properties of the paramyxovirus PIV 5 hemagglutinin-neuraminidase (HN) protein},
author = {Ping, Yuan and Leser, George P and Demeler, Borries and Lamb, Robert A and Howard Hughes Medical Institute, Northwestern University, Evanston, IL 60208-3500 and Jardetzky, Theodore S.},
abstractNote = {The mechanism by which the paramyxovirus hemagglutinin-neuraminidase (HN) protein couples receptor binding to activation of virus entry remains to be fully understood, but the HN stalk is thought to play an important role in the process. We have characterized ectodomain constructs of the parainfluenza virus 5 HN to understand better the underlying architecture and oligomerization properties that may influence HN functions. The PIV 5 neuraminidase (NA) domain is monomeric whereas the ectodomain forms a well-defined tetramer. The HN stalk also forms tetramers and higher order oligomers with high {alpha}-helical content. Together, the data indicate that the globular NA domains form weak intersubunit interactions at the end of the HN stalk tetramer, while stabilizing the stalk and overall oligomeric state of the ectodomain. Electron microscopy of the HN ectodomain reveals flexible arrangements of the NA and stalk domains, which may be important for understanding how these two HN domains impact virus entry.},
doi = {10.1016/j.virol.2008.05.023},
url = {https://www.osti.gov/biblio/21141031}, journal = {Virology},
issn = {0042-6822},
number = 2,
volume = 378,
place = {United States},
year = {2008},
month = {9}
}