The role of antigenically different virus neuraminidases as structures implicated in receptor-binding processes

Influenza A viruses exhibit segmented nucleic acid coding for eight different proteins, two of them as glycoproteins exposed on their lipoprotein envelopes, hemagglutinin (HA) and neuraminidase (NA). Hemagglutinin exhibits recptor-binding activity while neuraminidase develps sialidase cleavage activity which acts on cell receptors. Influenza A strains responsible for human, avian, equine and porcine respiratory infections all over the world present antigenically different hemagglutinin (H1 to H14) and neutraminidase (N1 to N9) structures on their surface. The objective of the present investigation was study the role of N2, N8 and N9, anti-genically diverse neuraminidase structures of human (N2) and animal (N8 and N9) influenza viruses, in the receptor-binding process. REceptor-binding activity of N2 and N8 was anlyzed by crossed tests using H3N2 and H3N8 antisera and the hemagglutination inhibition test as a model. Hemangglutinating activity of antigenically different N2 and N8 structures was demonstrable and was inhibited by homologous antisera (N2-H3N2, N8-H3N8) but not by heterologous antisera (N2-H3-N8,N8-H3-N2). This previously demonstrated N9 hemagglutinating activity was analysed for receptor-binding specificity using hemagglutination test and NeuAc alpha2,3Gal and NeuAc alpha2,6Gal derivatized erythrocytes. This highly purified N9 strain was obtained from a virus strain isolated from terns by Dr. Peter Colman (CSIRO Division of Biomolecular Engineering, Parkville, Victoria, Australia)...

Effects of low pH on hemagglutinating and hemolytic activities of west equine encephalomyelitis virus

1. The hemagglutinating (HA) and hemolytic (HL) activities mediated by egg-propagated west equine encephalomyelitis (WEE) virus preparations were investigated. 2. The purified virus preparation exhibited the best HA and HL activity at pH 6.0 and 6.0-6.2, respectively, as observed in the HA and HL tests. 3. In the virus preparations, both HA and HL activities were completely lost upon pretreatment at low pH (6.0). 4. The present results suggest that the alphavirus-mediated HA and HL activities against chicken erythrocytes can be considered to be a fusion from without