Document Type

Article

Publication Date

Winter 2-25-2009

Comments

This article has been peer reviewed. It is the authors' final version prior to publication in Vaccine. Volume 27, Issue 9, February 2009, Pages 1289-1292. The published version is available at . DOI: 10.1016/j.vaccine.2008.12.050. Copyright © Elsevier Inc..

Abstract

Polypeptide variants of the HA1 antigenic domain of the H5N1 avian influenza virus hemagglutinin (HA) molecule were produced in plants using transient and stable expression systems and fused with His/c-myc tags or with mouse or human Fc antibody fragments. The resulting peptides were purified and used for intramuscular immunization of mice. While the recombinant HA1 variants induced a significant serum humoral immune response in the mice, none of the HA1 preparations induced virus-neutralizing antibodies. Fusion with the Fc fragment improved overall yield of the constructs and allowed purification requiring only a single step, but led to no detectable fusion-related enhancement of immunogenicity or quality of immune response.

Figure_1_Flu_corrected.pdf (256 kB)
Figure_1_Flu_corrected.pdf

Figure_2_flu.pdf (197 kB)
Figure_2_flu.pdf

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