|Reference : Impairment of the M-protein and unmasking of a superficial type-specific antigen by p...|
|Scientific journals : Article|
|Human health sciences : Immunology & infectious disease|
Life sciences : Microbiology
|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 [Université de Liège - ULg > Laboratoire de Microbiologie générale et médicale > > >]|
|Rentier, Bernard [Université de Liège - ULg > Laboratoire de Microbiologie générale et médicale > > >]|
|Dierickx, Louis [Centre National pour la Production et l'Etude de Substances d'Origine Microbienne, Liège > > > >]|
|Yes (verified by ORBi)|
|[en] Influenza polypeptides ; Influenza type-specificity ; Orthomyxovirus host antigen ; Proteolytic digestion of myxovirus ; Influenza virus envelope structure|
|[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|
|Researchers ; Professionals|
There is no file associated with this reference.
All documents in ORBi are protected by a user license.