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.

Abstract:

: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-negative polypeptide of about 13,000 molecular weight 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 antiserum 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.

journal_name

Intervirology

journal_title

Intervirology

authors

Reginster M,Rentier B,Dierickx L

doi

10.1159/000149478

subject

Has Abstract

pub_date

1975-01-01 00:00:00

pages

239-48

issue

4-5

eissn

0300-5526

issn

1423-0100

journal_volume

6

pub_type

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