A single amino acid substitution in 1918 influenza virus hemagglutinin changes receptor binding specificity.
The receptor binding specificity of influenza viruses may be important for host restriction of human and avian viruses. Here, we show that the hemagglutinin (HA) of the virus that caused the 1918 influenza pandemic has strain-specific differences in its receptor binding specificity. The A/South Carolina/1/18 HA preferentially binds the alpha2,6 sialic acid (human) cellular receptor, whereas the A/New York/1/18 HA, which differs by only one amino acid, binds both the alpha2,6 and the alpha2,3 sialic acid (avian) cellular receptors. Compared to the conserved consensus sequence in the receptor binding site of avian HAs, only a single amino acid at position 190 was changed in the A/New York/1/18 HA. Mutation of this single amino acid back to the avian consensus resulted in a preference for the avian receptor.
Glaser
Laurel
L
Department of Microbiology, Mount Sinai School of Medicine, New York, NY 10029, USA.
Stevens
James
J
Zamarin
Dmitriy
D
Wilson
Ian A
IA
García-Sastre
Adolfo
A
Tumpey
Terrence M
TM
Basler
Christopher F
CF
Taubenberger
Jeffery K
JK
Palese
Peter
P
D019943:Amino Acid Substitution; D000818:Animals; D002645:Chickens; D004912:Erythrocytes; D006386:Hemagglutination Tests; D019267:Hemagglutinin Glycoproteins, Influenza Virus / Q000235:genetics / Q000276:immunology*; D019158:N-Acetylneuraminic Acid / Q000737:chemistry; D009975:Orthomyxoviridae / Q000235:genetics / Q000276:immunology*; D009976:Orthomyxoviridae Infections / Q000821:virology; D011991:Receptors, Virus / Q000737:chemistry / Q000276:immunology*; D013045:Species Specificity
D019267:Hemagglutinin Glycoproteins, Influenza Virus; D011991:Receptors, Virus; C483468:hemagglutinin, human influenza A virus; D019158:N-Acetylneuraminic Acid