Characterization and application of monoclonal antibodies to bovine viral diarrhea virus nonstructural protein 5A

Characterization and application of monoclonal antibodies to bovine viral diarrhea virus... Bovine viral diarrhea virus (BVDV) nonstructural protein 5A (NS5A) is one the least studied of the BVDV proteins. Therefore, to develop a tool for unraveling the functions performed by BVDV NS5A, monoclonal antibodies (MAbs) were generated by fusion of myeloma cells with spleen cells from mice immunized with recombinant E. coli -expressed GST-NS5A protein. Two MAbs (1H12 and 2F9) were established on the basis of immunofluorescence and Western blot analysis. Both the MAbs were of IgG1 subclass and recognized an epitope clustered within the N-terminal region of NS5A. Furthermore, the MAb 1H12 was used successfully to detect NS5A protein in BVDV field isolates belonging to genotypes 1 and 2. Temporal expression pattern studies during an infectious cycle revealed that BVDV NS5A could be detected 12–60 h postinfection. Confocal microscopy studies showed a cytoplasmic staining pattern and revealed that NS5A is localized on the endoplasmic reticulum membrane in BVDV infected cells. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Archives of Virology Springer Journals

Characterization and application of monoclonal antibodies to bovine viral diarrhea virus nonstructural protein 5A

Loading next page...
 
/lp/springer_journal/characterization-and-application-of-monoclonal-antibodies-to-bovine-zTrnPCb2mQ
Publisher
Springer Vienna
Copyright
Copyright © 2009 by Springer-Verlag
Subject
Biomedicine; Infectious Diseases; Medical Microbiology ; Virology
ISSN
0304-8608
eISSN
1432-8798
D.O.I.
10.1007/s00705-009-0505-7
Publisher site
See Article on Publisher Site

Abstract

Bovine viral diarrhea virus (BVDV) nonstructural protein 5A (NS5A) is one the least studied of the BVDV proteins. Therefore, to develop a tool for unraveling the functions performed by BVDV NS5A, monoclonal antibodies (MAbs) were generated by fusion of myeloma cells with spleen cells from mice immunized with recombinant E. coli -expressed GST-NS5A protein. Two MAbs (1H12 and 2F9) were established on the basis of immunofluorescence and Western blot analysis. Both the MAbs were of IgG1 subclass and recognized an epitope clustered within the N-terminal region of NS5A. Furthermore, the MAb 1H12 was used successfully to detect NS5A protein in BVDV field isolates belonging to genotypes 1 and 2. Temporal expression pattern studies during an infectious cycle revealed that BVDV NS5A could be detected 12–60 h postinfection. Confocal microscopy studies showed a cytoplasmic staining pattern and revealed that NS5A is localized on the endoplasmic reticulum membrane in BVDV infected cells.

Journal

Archives of VirologySpringer Journals

Published: Nov 1, 2009

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 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