NDLI: Soluble recombinant influenza vaccines.

Content Provider	PubMed Central
Author	Fiers, W. Neirynck, S. Deroo, T. Jou, W. M. Saelens, X.
Abstract	Soluble, recombinant forms of influenza A virus haemagglutinin and neuraminidase have been produced in cells of lower eukaryotes, and shown in a mouse model to induce complete protective immunity against a lethal virus challenge. Soluble neuraminidase, produced in a baculovirus system, consisted of tetramers, dimers and monomers. Only the tetramers were enzymatically active. The immunogenicity decreased very considerably in the order tetra > di > mono. Therefore, we fused the head part of the neuraminidase gene to a tetramerizing leucine zipper sequence; the resulting product was enzymatically active, tetrameric neuraminidase. The protective immunity induced by this engineered neuraminidase, however, remained fairly strain-specific. A third influenza A virus protein, the M2 protein, has only 23 amino acids exposed on the outer membrane surface. This extracellular part, M2e, has been remarkably conserved in all human influenza A strains since 1933. By fusing the M2e sequence to hepatitis B virus core protein, we could obtain highly immunogenic particles that induced complete, strain-independent, long-lasting protection in mice against a lethal viral challenge. Native M2 is a tetrameric protein and this conformation of the M2e part can also be mimicked by fusing this sequence to a tetramerizing leucine zipper. The potential of the resulting protein as a vaccine candidate remains to be evaluated.
Related Links	http://dx.doi.org/10.1098/rstb.2001.0980
Ending Page	1963
Page Count	3
Starting Page	1961
File Format	PDF
ISSN	09628436
e-ISSN	14712970
Journal	Philosophical Transactions of the Royal Society of London. Series B
Issue Number	1416
Volume Number	356
Language	English
Publisher Date	2001-12-29
Access Restriction	Open
Subject Keyword	Biochemistry, Genetics and Molecular Biology(all) Agricultural and Biological Sciences(all) Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Biochemistry, Genetics and Molecular Biology Agricultural and Biological Sciences

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