Purification of Influenza Virus Polypeptide Antigens and Studies of their Immunogenicity and Toxicity.

摘要

A technique for the isolation and purification of the influenza viral polypeptides with special reference to the neuraminidase and hemagglutinin glycoprotein antigens has been improved. A very important finding has been that biologically active and antigenically functional polypeptides can be isolated from influenza vaccine batches which provide a virtually unlimited source of material. Using authenticated vaccine as a starting material prepared in accord with BOB specifications anticipates the use and acceptance of the purified antigens as vaccines. A modification of the Weber and Kuter technique for the renaturation of enzymes has made it possible to remove residual SDS from the hemagglutinin polypeptides with restoration of both biologic and immunogenic activity. Removal of SDS has permitted the beginning of automated amino acid sequence analysis of the viral hemagglutinin. Purification of specific antibodies to the hemagglutinin and its cleavage products has been achieved by immobilization of the antigens on agarose columns. Using another approach,the hemagglutinin and neuraminidase antigens have been isolated together by extraction following Triton X-100disruption.