The complex formation of influenza virus envelope glycoproteins with outer membrane proteins of Neisseria meningitidis or Borrelia burgdorferi.

The isolation of influenza virus envelope glycoproteins was achieved by one-step procedure consisting of treatment of purified virus with zwitterionic detergent and separation of viral constituents by sucrose density gradient centrifugation. Viral glycoproteins and proteins of outer membrane of N. meningitidis or B.

Relationship of 2',3'-cyclic nucleotide 3'-phosphohydrolase activity of large enveloped RNA viruses to host cell activity.

Purified virions of the large RNA viruses show 2',3'-cyclic nucleotide 3'-phosphohydrolase (3'-CNPase) activity. The 3'-CNPase activity is virion-associated and stimulated by their treatment with nonionic detergents. Cytopathic viruses such as influenza A2 (Singapore/57), NDV, and VSV showed the specific activity of a virion-associated 3'-CNPase equal to or lower than the specific activity of host cell enzyme.

Localization of 2',3'-decycling phosphodiesterases in the Newcastle disease virus virion.

Purified Newcastle disease virus (NDV) virions possess 2',3'-cyclic nucleotide 2'-phosphohydrolase (2'-CNPase) and 2',3'-cyclic nucleotide 3'-phosphohydrolase (3'-CNPase) activities. These enzyme activities cannot be removed from the virion even after extensive purification by chromatography on controlled-pore glass. In the intact virion, the 3'-CNPase activity was stimulated by Triton X-100, while the 2'-CNPase activity was partially inhibited.

Hydrolysis of ribonucleoside 2',3'-cyclic phosphates by influenza and Newcastle disease viruses.

Two enzymatic activities hydrolysing ribonucleoside 2', 3'-cyclic phosphates (2', 3'-cNMP) to 2'- or 3'- nucleoside monophosphate were found associated with influenza and Newcastle disease viruses. The two enzymatic activities differed from each other by temperature optima and thermoresistance. 2', 3'-Cyclic nucleotide 3'-phosphohydrolase was responsible for splitting of the substrate to 2'-NMP.

Purification of Newcastle disease virus by chromatography on controlled-pore glass bead column.

Newcastle disease virus (NDV) purified by sucrose density gradient centrifugation was chromatographed on a controlled-pore glass (CPG) bead column. By this procedure, the contaminating ribonuclease activity was reduced by 94-96% and the specific viral haemagglutinating activity increased from 3-to 5-fold. Purified NDV moved in two fractions in free electrophoresis.