Impairment of the M-protein and unmasking of a superficial type-specific antigen by proteolytic treatment of influenza A virions with preservation of host-specific antigenicity
Reginster, Monique; Rentier, Bernard; Dierickx, Louis
[en] Influenza PR8 particles resulting from strong treatment with caseinase C are spikeless, devoid of neuraminidase and hemagglutinin 1 and 2 glycopeptides, and contain a Schiff-neg. polypeptide of about 13,000 mol. wt. which exists as traces in intact virions. Their M-protein polypeptide content is reduced to 50% of its original value, but there is no evidence of particle disruption nor of lipid release. They fix complement in the presence of both anti-M-protein and antiserum raised against a host polysaccharide. During exposure to caseinase C, an antigen is unmasked. It is type-specific and its identity with the M-protein is discussed
Disciplines :
Immunology & infectious disease Microbiology
Author, co-author :
Reginster, Monique; Université de Liège - ULiège > Laboratoire de Microbiologie générale et médicale
Rentier, Bernard ; Université de Liège - ULiège > Laboratoire de Microbiologie générale et médicale
Dierickx, Louis; Centre National pour la Production et l'Etude de Substances d'Origine Microbienne, Liège
Language :
English
Title :
Impairment of the M-protein and unmasking of a superficial type-specific antigen by proteolytic treatment of influenza A virions with preservation of host-specific antigenicity
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