Abstract: “Influenza C” virus agglutinates chicken erythrocytes and elutes rapidly from them, in the process destroying receptors for the virus. Virions of influenza C purified by centrifugation into a density gradient retain the ability to agglutinate and elute from red blood cells and to destroy their receptors for influenza C. However, the receptor-destroying activity of influenza C does not affect receptors for prototype ortho- and paramyxoviruses. Purified and concentrated bacterial neuraminidase destroys receptors for influenza A and B and Newcastle disease viruses without affecting receptors for influenza C. These results confirm and extend previous observations by Hirst that influenza C receptors differ from receptors for myxoviruses and suggest they do not contain sialic acid. Direct assay for neuraminidase activity in “influenza C” was carried out employing as substrates compounds containing predominantly N-acetyl, 4-O-acetyl N-acetyl, or 7-O-acetyl and 8-O-acetyl N-acetyl neuraminic acid in 2–3′-, 2–4′-, 2–6′- and 2–8′-α-O-glycosidic linkage. Although differences in specificity were observed between Vibrio cholerae neuraminidase, influenza A and B neuraminidase, and Newcastle disease virus neuraminidase, each neuraminidase was active against several of the substrates whereas “influenza C” did not liberate sialic acid from any substrate. It is concluded that “influenza C” lacks an α-neuraminidase. By acrylamide-gel electrophoretic analysis in the presence of sodium dodecyl sulfate influenza C virions were found to contain three glycoproteins, of sizes about 83,000, 66,000 and 26,000 daltons. The main structural polypeptide was nonglycosylated, had a size of about 28,000 daltons, and was the only polypeptide present in enveloped structures recovered after prolonged proteolytic digestion which destroys all morphologically identifiable components of influenza C virions except for the structural envelope. This component is thus identified as the internal membrane protein. An additional non-glycosylated major polypeptide component in virions, of size about 62,000 daltons, is believed to be the nucleoprotein. The pattern of structural polypeptides is distinct from that of paramyxoviruses, but in some respects similar to orthomyxoviruses. Classification and nomenclature of “influenza C” virus are discussed.

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   |wiki=    Sante
   |area=    H2N2V1
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   |clé=     ISTEX:A719B0B397422E78FA08A933AFE81603A5C5B71C
   |texte=   A comparison of “influenza C” with prototype myxoviruses: Receptor-destroying activity (neuraminidase) and structural polypeptides
}}