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| Reference : Impairment of the M-protein and unmasking of a superficial type-specific antigen by prot... |
| Scientific journals : Article | |||
| Human health sciences : Immunology & infectious disease Life sciences : Microbiology | |||
| http://hdl.handle.net/2268/694 | |||
| 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 | |
| English | |
| 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 > > > >] | |
| Dec-1976 | |
| Intervirology | |
| Karger | |
| 6 | |
| 4-5 | |
| 239-248 | |
| International | |
| 0300-5526 | |
| [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 | |
| http://hdl.handle.net/2268/694 |
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