Neuraminidase Activity in \u3cem\u3eDiplococcus pneumoniae\u3c/em\u3e

Kelly, R. T. (Marquette University School of Medicine, Milwaukee, Wis.), D. Greiff, and S. Farmer. Neuraminidase activity in Diplococcus pneumoniae. J. Bacteriol. 91:601–603. 1966.—A method for the quantitation of neuraminidase in the presence of N-acetylneuraminic acid aldolase is described. The neuraminidase content of Diplococcus pneumoniae was found to be dependent on the media employed for growth; the highest enzyme activity per milligram of bacterial protein was obtained with Todd-Hewitt broth. Neuraminidase production was stimulated in D. pneumoniae by the addition of N-acetylneuraminlactose, N-acetylneuraminic acid, or N-acetylmannosamine to the growth medium. Three rough strains of D. pneumoniae, which were nonpathogenic for mice, lacked neuraminidase activity. Seven of 12 smooth strains contained neuraminidase; enzyme activity was not detected in the remaining 5 smooth strains. There was no correlation between the presence of neuraminidase activity and the capsular type or between neuraminidase production and animal virulence

Flocculation of influenza virus by specific anti-neuraminidase antibody

1. Flocculation of purified preparations of influenza virus has been demonstrated to occur in the presence of low dilutions of specific anti-neuraminidase sera. High dilutions of the sera caused microscopic aggregation of virions. It is suggested that the effects of anti-neuraminidase antibody on the replication of influenza virus observed in vitro could be caused by antibody binding virions to infected cells, rather than by inhibition of neuraminidase enzymic activity.Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/41680/1/705_2005_Article_BF01253756.pd