The amino terminus of the salmonid alphavirus capsid protein determines subcellular localization and inhibits cellular proliferation

The amino terminus of the salmonid alphavirus capsid protein determines subcellular localization... Salmonid alphavirus (SAV) is the most divergent member of the family Togaviridae and constitutes a threat to farming of salmonid fish in Europe. Here, we report cloning, expression and preliminary functional analysis of the capsid protein of SAV, confirming it to be expressed as an approximately 31-kDa protein in infected cells. The protein localizes strictly to the cytoplasm in Chinook salmon embryo cells, and either to the nucleus or cytoplasm in bluegill fry cells. An expression study of full-length and different truncated versions of the SAV capsid fused to the enhanced green fluorescent protein demonstrated that the localization is independent of other viral components in both cell lines, and controlled by the N-terminal 82 aa, which include a conserved, predicted helix and a downstream positively charged region. Thus, the results suggest that the SAV capsid possesses a cell-type-dependent potential for nuclear import and export. Moreover, the SAV capsid and its N-terminal 82 aa were shown to be associated with inhibition of cellular proliferation, a hallmark of the cytopathic effect caused by SAV. These results highlight that the SAV capsid is a multifunctional protein with possible importance for pathogenesis. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Archives of Virology Springer Journals

The amino terminus of the salmonid alphavirus capsid protein determines subcellular localization and inhibits cellular proliferation

Loading next page...
 
/lp/springer_journal/the-amino-terminus-of-the-salmonid-alphavirus-capsid-protein-chGBUKOPme
Publisher
Springer Vienna
Copyright
Copyright © 2010 by Springer-Verlag
Subject
Biomedicine; Infectious Diseases; Medical Microbiology ; Virology
ISSN
0304-8608
eISSN
1432-8798
D.O.I.
10.1007/s00705-010-0717-x
Publisher site
See Article on Publisher Site

Abstract

Salmonid alphavirus (SAV) is the most divergent member of the family Togaviridae and constitutes a threat to farming of salmonid fish in Europe. Here, we report cloning, expression and preliminary functional analysis of the capsid protein of SAV, confirming it to be expressed as an approximately 31-kDa protein in infected cells. The protein localizes strictly to the cytoplasm in Chinook salmon embryo cells, and either to the nucleus or cytoplasm in bluegill fry cells. An expression study of full-length and different truncated versions of the SAV capsid fused to the enhanced green fluorescent protein demonstrated that the localization is independent of other viral components in both cell lines, and controlled by the N-terminal 82 aa, which include a conserved, predicted helix and a downstream positively charged region. Thus, the results suggest that the SAV capsid possesses a cell-type-dependent potential for nuclear import and export. Moreover, the SAV capsid and its N-terminal 82 aa were shown to be associated with inhibition of cellular proliferation, a hallmark of the cytopathic effect caused by SAV. These results highlight that the SAV capsid is a multifunctional protein with possible importance for pathogenesis.

Journal

Archives of VirologySpringer Journals

Published: Aug 1, 2010

References

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 12 million articles from more than
10,000 peer-reviewed journals.

All for just $49/month

Explore the DeepDyve Library

Unlimited reading

Read as many articles as you need. Full articles with original layout, charts and figures. Read online, from anywhere.

Stay up to date

Keep up with your field with Personalized Recommendations and Follow Journals to get automatic updates.

Organize your research

It’s easy to organize your research with our built-in tools.

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