Specificity and affinity of sialic acid binding by the rhesus rotavirus VP8* core.
Nuclear magnetic resonance spectroscopy demonstrates that the rhesus rotavirus hemagglutinin specifically binds alpha-anomeric N-acetylneuraminic acid with a K(d) of 1.2 mM. The hemagglutinin requires no additional carbohydrate moieties for binding, does not distinguish 3' from 6' sialyllactose, and has approximately tenfold lower affinity for N-glycolylneuraminic than for N-acetylneuraminic acid. The broad specificity and low affinity of sialic acid binding by the rotavirus hemagglutinin are consistent with this interaction mediating initial cell attachment prior to the interactions that determine host range and cell type specificity.
Dormitzer
Philip R
PR
Laboratory of Molecular Medicine, Enders 673, Children's Hospital, Harvard Medical School, 320 Longwood Avenue, Boston, MA 02115, USA. dormitze@crystal.harvard.edu
Sun
Zhen-Yu J
ZY
Blixt
Ola
O
Paulson
James C
JC
Wagner
Gerhard
G
Harrison
Stephen C
SC
D000818:Animals; D002240:Carbohydrate Sequence; D008253:Macaca mulatta / Q000821:virology; D008969:Molecular Sequence Data; D019158:N-Acetylneuraminic Acid / Q000737:chemistry / Q000378:metabolism*; D016601:RNA-Binding Proteins / Q000378:metabolism*; D011991:Receptors, Virus / Q000378:metabolism*; D012401:Rotavirus / Q000378:metabolism*; D014312:Trisaccharides / Q000737:chemistry / Q000378:metabolism; D017361:Viral Nonstructural Proteins / Q000378:metabolism*
D016601:RNA-Binding Proteins; D011991:Receptors, Virus; D014312:Trisaccharides; D017361:Viral Nonstructural Proteins; C079234:NS35 protein, rotavirus; D019158:N-Acetylneuraminic Acid