A recent field isolate of Sendai virus has a temperature-sensitive HN glycoprotein.
A recent field isolate of Sendai virus was found to have a temperature-sensitive (ts) hemagglutinin-neuraminidase (HN) glycoprotein. The ts phenotype was manifested as a loss of cell binding, reduced replication, and virions that were lacking surface HN after growth at the nonpermissive temperature (38 degrees). Low neuraminidase activity and failure of the field isolate to remove sialic acid from receptors on the surface of erythrocytes indicated that rapid elution of the field isolate virions from erythrocytes at the nonpermissive temperature was not due to neuraminidase activity but to a proposed conformational change in the HN molecule. The specific amino acids responsible for the ts phenotype could not be determined due to the number of amino acid differences between the field isolate and Enders strain. Heat inactivation and monoclonal antibody inhibition of HN functions indicated that the HN protein of this isolate was, in addition to ts, an unstable molecule.
Gorman
W L
WL
Department of Virology and Molecular Biology, St. Jude Children's Research Hospital, Memphis, Tennessee 38101.
Portner
A
A
D015707:HN Protein; D006387:Hemagglutination, Viral; D006389:Hemagglutinins, Viral; D009439:Neuraminidase / Q000378:metabolism; D010222:Parainfluenza Virus 1, Human / Q000502:physiology*; D010641:Phenotype; D011487:Protein Conformation; D011991:Receptors, Virus / Q000378:metabolism; D013696:Temperature; D014759:Viral Envelope Proteins / Q000378:metabolism / Q000502:physiology*
D015707:HN Protein; D006389:Hemagglutinins, Viral; D011991:Receptors, Virus; D014759:Viral Envelope Proteins; D009439:Neuraminidase