Multiple heparin binding domains of respiratory syncytial virus G mediate binding to mammalian cells

Multiple heparin binding domains of respiratory syncytial virus G mediate binding to mammalian cells Respiratory syncytial virus (RSV) G glycoprotein mediates cell attachment through surface glycosaminoglycans (GAGs). Feldman et al. (10) suggested that specific basic amino acids in residues 184–198 of G defined a critical heparin binding domain (HBD). To further define the G HBD we made a series of truncated G proteins expressed in Escherichia coli . G88 (G residues 143–231), bound to HEp-2 cells in a dose dependent manner and binding was inhibited >99% with heparin. Cell binding of G88 was unaltered by alanine substitution mutagenesis of all basic amino acids in Feldman’s region 184–198. A G88 variant truncated beyond residue 198, G58, and G58 fully alanine substituted in the region 184–198, G58A6, bound to HEp-2 cells about half as well and 100-fold less well than G88, respectively. G88 and all alanine substitution mutants of G88 inhibited RSV plaque formation by 50% (ID 50 ) at concentrations of ∼50 nM; the ID 50 of G58 was ∼425 nM while G58A6 had an ID 50 >1600 nM. These data show that the G HBD includes as much as residues 187–231, that there is redundancy beyond the previously described HBD, and that the cell-binding and virus infectivity-blocking functions of these recombinant G proteins were closely linked and required at least one HBD. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Archives of Virology Springer Journals

Multiple heparin binding domains of respiratory syncytial virus G mediate binding to mammalian cells

Loading next page...
 
/lp/springer_journal/multiple-heparin-binding-domains-of-respiratory-syncytial-virus-g-A4fRRykbon
Publisher
Springer-Verlag
Copyright
Copyright © 2003 by Springer-Verlag/Wien
Subject
LifeSciences
ISSN
0304-8608
eISSN
1432-8798
D.O.I.
10.1007/s00705-003-0139-0
Publisher site
See Article on Publisher Site

Abstract

Respiratory syncytial virus (RSV) G glycoprotein mediates cell attachment through surface glycosaminoglycans (GAGs). Feldman et al. (10) suggested that specific basic amino acids in residues 184–198 of G defined a critical heparin binding domain (HBD). To further define the G HBD we made a series of truncated G proteins expressed in Escherichia coli . G88 (G residues 143–231), bound to HEp-2 cells in a dose dependent manner and binding was inhibited >99% with heparin. Cell binding of G88 was unaltered by alanine substitution mutagenesis of all basic amino acids in Feldman’s region 184–198. A G88 variant truncated beyond residue 198, G58, and G58 fully alanine substituted in the region 184–198, G58A6, bound to HEp-2 cells about half as well and 100-fold less well than G88, respectively. G88 and all alanine substitution mutants of G88 inhibited RSV plaque formation by 50% (ID 50 ) at concentrations of ∼50 nM; the ID 50 of G58 was ∼425 nM while G58A6 had an ID 50 >1600 nM. These data show that the G HBD includes as much as residues 187–231, that there is redundancy beyond the previously described HBD, and that the cell-binding and virus infectivity-blocking functions of these recombinant G proteins were closely linked and required at least one HBD.

Journal

Archives of VirologySpringer Journals

Published: Oct 1, 2003

There are no references for this article.

You’re reading a free preview. Subscribe to read the entire article.


DeepDyve is your
personal research library

It’s your single place to instantly
discover and read the research
that matters to you.

Enjoy affordable access to
over 18 million articles from more than
15,000 peer-reviewed journals.

All for just $49/month

Explore the DeepDyve Library

Search

Query the DeepDyve database, plus search all of PubMed and Google Scholar seamlessly

Organize

Save any article or search result from DeepDyve, PubMed, and Google Scholar... all in one place.

Access

Get unlimited, online access to over 18 million full-text articles from more than 15,000 scientific journals.

Your journals are on DeepDyve

Read from thousands of the leading scholarly journals from SpringerNature, Elsevier, Wiley-Blackwell, Oxford University Press and more.

All the latest content is available, no embargo periods.

See the journals in your area

DeepDyve

Freelancer

DeepDyve

Pro

Price

FREE

$49/month
$360/year

Save searches from
Google Scholar,
PubMed

Create lists to
organize your research

Export lists, citations

Read DeepDyve articles

Abstract access only

Unlimited access to over
18 million full-text articles

Print

20 pages / month

PDF Discount

20% off