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Title: Advances in alfalfa mosaic virus-mediated expression of anthrax antigen in planta

Abstract

Plant viruses show great potential for production of pharmaceuticals in plants. Such viruses can harbor a small antigenic peptide(s) as a part of their coat proteins (CP) and elicit an antigen-specific immune response. Here, we report the high yield and consistency in production of recombinant alfalfa mosaic virus (AlMV) particles for specific presentation of the small loop 15 amino acid epitope from domain-4 of the Bacillus anthracis protective antigen (PA-D4s). The epitope was inserted immediately after the first 25 N-terminal amino acids of AlMV CP to retain genome activation and binding of CP to viral RNAs. Recombinant AlMV particles were efficiently produced in tobacco, easily purified for immunological analysis, and exhibited extended stability and systemic proliferation in planta. Intraperitional injections of mice with recombinant plant virus particles harboring the PA-D4s epitope elicited a distinct immune response. Western blotting and ELISA analysis showed that sera from immunized mice recognized both native PA antigen and the AlMV CP.

Authors:
 [1];  [1];  [1];  [1];  [2]
  1. Biotechnology Foundation Laboratories, Thomas Jefferson University, Philadelphia, PA 19107 (United States)
  2. Biotechnology Foundation Laboratories, Thomas Jefferson University, Philadelphia, PA 19107 (United States). E-mail: h_koprowski@jefferson.edu
Publication Date:
OSTI Identifier:
20793216
Resource Type:
Journal Article
Resource Relation:
Journal Name: Biochemical and Biophysical Research Communications; Journal Volume: 338; Journal Issue: 2; Other Information: DOI: 10.1016/j.bbrc.2005.09.196; PII: S0006-291X(05)02214-X; Copyright (c) 2005 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; ALFALFA; AMINO ACIDS; ANTIGENS; BACILLUS; CELL PROLIFERATION; DRUGS; ENZYME IMMUNOASSAY; MICE; PEPTIDES; RNA; TOBACCO; VIRUSES

Citation Formats

Brodzik, R., Bandurska, K., Deka, D., Golovkin, M., and Koprowski, H.. Advances in alfalfa mosaic virus-mediated expression of anthrax antigen in planta. United States: N. p., 2005. Web. doi:10.1016/J.BBRC.2005.0.
Brodzik, R., Bandurska, K., Deka, D., Golovkin, M., & Koprowski, H.. Advances in alfalfa mosaic virus-mediated expression of anthrax antigen in planta. United States. doi:10.1016/J.BBRC.2005.0.
Brodzik, R., Bandurska, K., Deka, D., Golovkin, M., and Koprowski, H.. Fri . "Advances in alfalfa mosaic virus-mediated expression of anthrax antigen in planta". United States. doi:10.1016/J.BBRC.2005.0.
@article{osti_20793216,
title = {Advances in alfalfa mosaic virus-mediated expression of anthrax antigen in planta},
author = {Brodzik, R. and Bandurska, K. and Deka, D. and Golovkin, M. and Koprowski, H.},
abstractNote = {Plant viruses show great potential for production of pharmaceuticals in plants. Such viruses can harbor a small antigenic peptide(s) as a part of their coat proteins (CP) and elicit an antigen-specific immune response. Here, we report the high yield and consistency in production of recombinant alfalfa mosaic virus (AlMV) particles for specific presentation of the small loop 15 amino acid epitope from domain-4 of the Bacillus anthracis protective antigen (PA-D4s). The epitope was inserted immediately after the first 25 N-terminal amino acids of AlMV CP to retain genome activation and binding of CP to viral RNAs. Recombinant AlMV particles were efficiently produced in tobacco, easily purified for immunological analysis, and exhibited extended stability and systemic proliferation in planta. Intraperitional injections of mice with recombinant plant virus particles harboring the PA-D4s epitope elicited a distinct immune response. Western blotting and ELISA analysis showed that sera from immunized mice recognized both native PA antigen and the AlMV CP.},
doi = {10.1016/J.BBRC.2005.0},
journal = {Biochemical and Biophysical Research Communications},
number = 2,
volume = 338,
place = {United States},
year = {Fri Dec 16 00:00:00 EST 2005},
month = {Fri Dec 16 00:00:00 EST 2005}
}