+ Site Statistics
+ Search Articles
+ PDF Full Text Service
How our service works
Request PDF Full Text
+ Follow Us
Follow on Facebook
Follow on Twitter
Follow on LinkedIn
+ Subscribe to Site Feeds
Most Shared
PDF Full Text
+ Translate
+ Recently Requested

The neuraminidase of human parainfluenza 1 virus ha 2 strain

The neuraminidase of human parainfluenza 1 virus ha 2 strain

Journal of General Virology 37(3): 547-556

Neuraminidase activity could be demonstrated in highly concentrated preparations of human parainfluenza 1 virus, strain C35 (HA2 virus). Among the substrates used, the most suitable are N-acetyl neuramin lactose and fetuin. Mucin type I and type II were not hydrolyzed. The neuraminidase exhibited some characteristics similar to those of the other paramyxoviruses (Sendai, NDV [Newcastle disease virus], mumps, human parainfluenza 2 virus): the optimum pH ranged between 5-5.4 and the Km value was 5 .times. 10-3 M when tested with N-acetyl neuramin lactose. Its optimum activity was between 37.degree.-40.degree. C and it was thermolabile, the enzyme activity being reduced to 50% in 5 min at 45.degree. C and entirely destroyed at 50 C in the same period. The thermal inactivation constants of neuraminidase and hemagglutinin and the temperature which inactivated 50% of both these activities were very similar to those already shown for NDV. Hemagglutinin and neuraminidase activities were rapidly destroyed by ionic detergents, but not by non-ionic detergents.

Please choose payment method:

(PDF emailed within 1 workday: $29.90)

Accession: 006724150

Download citation: RISBibTeXText

Related references

The human parainfluenza virus type-1 prototypic strain contains a heat-labile hemagglutinin-neuraminidase protein. Virus Research 32(1): 85-92, 1994

Neuraminidase activity of a bovine strain of parainfluenza 3 virus. Nature 213(5072): 185-186, 1967

A single amino acid alteration in the human parainfluenza virus type 3 hemagglutinin-neuraminidase glycoprotein confers resistance to the inhibitory effects of zanamivir on receptor binding and neuraminidase activity. Journal of Virology 75(14): 6310-6320, 2001

Antigenic and structural properties of the hemagglutinin-neuraminidase glycoprotein of human parainfluenza virus type 3: sequence analysis of variants selected with monoclonal antibodies which inhibit infectivity, hemagglutination, and neuraminidase activities. Journal of Virology 61(5): 1473-1477, 1987

Regions on the hemagglutinin-neuraminidase proteins of human parainfluenza virus type-1 and Sendai virus important for membrane fusion. Virology 204(2): 506-514, 1994

Structure of the Haemagglutinin-neuraminidase from Human Parainfluenza Virus Type III. Journal of Molecular Biology 335(5): 43-57, 2004

Exposing the flexibility of human parainfluenza virus hemagglutinin-neuraminidase. Journal of the American Chemical Society 134(44): 18447-18452, 2012

Relative affinity of the human parainfluenza virus type 3 hemagglutinin-neuraminidase for sialic acid correlates with virus-induced fusion activity. Journal of Virology 67(11): 6463-6468, 1993

Sequence of the hemagglutinin-neuraminidase gene of human parainfluenza virus type 1. Virus Research 16(1): 107-113, 1990

The Neuraminidase of Human Parainfluenza 1 Virus (Ha2 Virus). Journal of General Virology 37(3): 547-556, 1977

Antigenic variation in the hemagglutinin-neuraminidase protein of human parainfluenza type 3 virus. Virology 143(2): 569-582, 1985

Human parainfluenza virus 3 neuraminidase activity contributes to dendritic cell maturation. Viral Immunology 18(3): 523-533, 2005

The catalytic mechanism of human parainfluenza virus type 3 haemagglutinin-neuraminidase revealed. Angewandte Chemie 54(10): 2936-2940, 2015

The hemagglutinin-neuraminidase glycoproteins of human parainfluenza virus type 1 and Sendai virus have high structure-function similarity with limited antigenic cross-reactivity. Virology 175(1): 211-221, 1990

Receptor-binding specificity of the human parainfluenza virus type 1 hemagglutinin-neuraminidase glycoprotein. Glycobiology 22(2): 174-180, 2012