Crystals of hemagglutinin-neuraminidase of parainfluenza virus contain triple-stranded helices.
When purified dimers of hemagglutinin-neuraminidase molecules released by protease digestion from three strains of human parainfluenza virus 1 were used in crystallization trials, long thin needle crystals formed. Electron microscopic analysis of these needle crystals revealed that they are composed of stacks of triple-stranded helices with each strand of the helix made up of subunits of hemagglutinin-neuraminidase. To our knowledge, this is the first direct demonstration of the assembly of protein subunits into large triple-stranded helices. An understanding of the organization of these triple helices may shed light on the structural properties of the hemagglutinin-neuraminidase molecules that cause them to form these helices.
Department of Virology and Molecular Biology, St. Jude Children's Research Hospital, Memphis, TN 38101.
K G
KG
Murti
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Takimoto
W G
WG
Laver
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Portner
D003460:Crystallization; D004591:Electrophoresis, Polyacrylamide Gel; D015707:HN Protein / Q000302:isolation & purification* / Q000648:ultrastructure*; D046911:Macromolecular Substances; D008854:Microscopy, Electron; D010222:Parainfluenza Virus 1, Human / Q000276:immunology*
D015707:HN Protein; D046911:Macromolecular Substances