Evaluation of recombinant A/Victoria/3/75 (H3N2) influenza neuraminidase mutants as potential broad-spectrum subunit vaccines against influenza A

Evaluation of recombinant A/Victoria/3/75 (H3N2) influenza neuraminidase mutants as potential... Current influenza vaccines require repeated administration for long-term protection. Failure to develop broad-spectrum vaccines may be attributed to the chronic presentation of hypervariable, immunodominant epitopes displayed on the viral surface that keep the immune response somewhat fixed and limited by suppression of broadly neutralizing, low-titered antibodies. To test this hypothesis, we have attempted to dampen the immunogenicity of variable epitopes and potential immunodominant domains of the A/Victoria/3/75 (H3N2) neuraminidase by site-directed mutagenesis. The results suggest that the neuraminidase structure is extremely flexible, since many substitution combinations were tolerated, and constitute proof-of-principle that the antigenicity of this protein can be modulated to a large extent. However, mice immunized with neuraminidase mutants containing multiple amino acid substitutions showed a reduced protection rate against heterologous virus in comparison with the reference groups. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Archives of Virology Springer Journals

Evaluation of recombinant A/Victoria/3/75 (H3N2) influenza neuraminidase mutants as potential broad-spectrum subunit vaccines against influenza A

Loading next page...
 
/lp/springer_journal/evaluation-of-recombinant-a-victoria-3-75-h3n2-influenza-neuraminidase-059SkOpyon
Publisher
Springer-Verlag
Copyright
Copyright © Wien by 1998 Springer-Verlag/
Subject
Legacy
ISSN
0304-8608
eISSN
1432-8798
D.O.I.
10.1007/s007050050437
Publisher site
See Article on Publisher Site

Abstract

Current influenza vaccines require repeated administration for long-term protection. Failure to develop broad-spectrum vaccines may be attributed to the chronic presentation of hypervariable, immunodominant epitopes displayed on the viral surface that keep the immune response somewhat fixed and limited by suppression of broadly neutralizing, low-titered antibodies. To test this hypothesis, we have attempted to dampen the immunogenicity of variable epitopes and potential immunodominant domains of the A/Victoria/3/75 (H3N2) neuraminidase by site-directed mutagenesis. The results suggest that the neuraminidase structure is extremely flexible, since many substitution combinations were tolerated, and constitute proof-of-principle that the antigenicity of this protein can be modulated to a large extent. However, mice immunized with neuraminidase mutants containing multiple amino acid substitutions showed a reduced protection rate against heterologous virus in comparison with the reference groups.

Journal

Archives of VirologySpringer Journals

Published: Oct 1, 1998

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