Purification of Influenza Virus Polypeptide Antigens and Studies of Their Immunogenicity and Toxicity
Abstract
Continued development of an 'infection-permissive' neuraminidase- specific vaccine has proceeded. Such a vaccine may be produced either by tailor- making a recombinant virus containing the neuraminidase of the current subtype of influenza virus coupled with an irrelevant hemagglutinin or by isolation of the neuraminidase directly from the virus. Vaccine trials have compared the immune response of a neuraminidase-specific vaccine employing the recombinant X- 38 (Heq1N2) with that of a conventional bispecific vaccine, X-37 (H3N2). A superior antibody response to neuraminidase was observed when the enzyme was coupled with the 'irrelevant' hemagglutinin in the X-38 vaccine as compared with the conventional vaccine. An unexpected finding was the induction of anti-H3 heterotypic antibody by the X-38 vaccine possessing the 'irrelevant' hemagglutinin. Techniques for viral protein purification have been improved and have shown that hemagglutinin as a dimer is immunogenic.
Document Details
- Document Type
- Technical Report
- Publication Date
- Sep 01, 1976
- Accession Number
- ADB014994
Entities
People
- Doris J. Bucher
- Edwin D. Kilbourne
Organizations
- Icahn School of Medicine at Mount Sinai