Glaser Laurel, Stevens James, Zamarin Dmitriy, Wilson Ian A, García-Sastre Adolfo, Tumpey Terrence M, Basler Christopher F, Taubenberger Jeffery K, Palese Peter
Department of Microbiology, Mount Sinai School of Medicine, New York, NY 10029, USA.
J Virol. 2005 Sep;79(17):11533-6. doi: 10.1128/JVI.79.17.11533-11536.2005.
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.
流感病毒的受体结合特异性可能对人类和禽流感病毒的宿主限制很重要。在此，我们表明，导致1918年流感大流行的病毒的血凝素（HA）在其受体结合特异性上存在毒株特异性差异。A/南卡罗来纳州/1/18 HA优先结合α2,6唾液酸（人类）细胞受体，而仅相差一个氨基酸的A/纽约/1/18 HA则同时结合α2,6和α2,3唾液酸（禽类）细胞受体。与禽类HA受体结合位点的保守共有序列相比，A/纽约/1/18 HA中仅第190位的一个氨基酸发生了变化。将这个单一氨基酸突变为禽类共有序列后，导致其对禽类受体产生偏好。
