Single amino acid substitutions in influenza haemagglutinin change receptor binding specificity

Nature ◽  
1983 ◽  
Vol 304 (5921) ◽  
pp. 76-78 ◽  
Author(s):  
G. N. Rogers ◽  
J. C. Paulson ◽  
R. S. Daniels ◽  
J. J. Skehel ◽  
I. A. Wilson ◽  
...  
Keyword(s):  
Amino Acid ◽  
Receptor Binding ◽  
Binding Specificity ◽  
Single Amino Acid ◽  
Amino Acid Substitutions ◽  
Receptor Binding Specificity

scholarly journals A Single Amino Acid Substitution in 1918 Influenza Virus Hemagglutinin Changes Receptor Binding Specificity

2005 ◽  
Vol 79 (17) ◽  
pp. 11533-11536 ◽  
Author(s):  
Laurel Glaser ◽  
James Stevens ◽  
Dmitriy Zamarin ◽  
Ian A. Wilson ◽  
Adolfo García-Sastre ◽  
...  
Keyword(s):  
New York ◽  
Sialic Acid ◽  
Amino Acid ◽  
Receptor Binding ◽  
Consensus Sequence ◽  
Binding Specificity ◽  
Influenza Viruses ◽  
Single Amino Acid ◽  
1918 Influenza ◽  
Receptor Binding Specificity

ABSTRACT 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 α2,6 sialic acid (human) cellular receptor, whereas the A/New York/1/18 HA, which differs by only one amino acid, binds both the α2,6 and the α2,3 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.

Effect of single amino acid substitutions in the hemagglutinin on the receptor-binding properties of influenza B viruses

2015 ◽  
Vol 70 ◽  
pp. S29
Author(s):  
E. Sorokin ◽  
T. Tsareva ◽  
A. Sominina ◽  
M. Pisareva ◽  
A. Komissarov ◽  
...  
Keyword(s):  
Amino Acid ◽  
Receptor Binding ◽  
Single Amino Acid ◽  
Influenza B ◽  
Amino Acid Substitutions ◽  
Binding Properties

scholarly journals Genetic Variation and Evolution of the 2019 Novel Coronavirus

2021 ◽  
pp. 1-13
Author(s):  
Salvatore Dimonte ◽  
Muhammed Babakir-Mina ◽  
Taib Hama-Soor ◽  
Salar Ali
Keyword(s):  
Amino Acid ◽  
Receptor Binding ◽  
Rapid Evolution ◽  
Single Amino Acid ◽  
Angiotensin Converting Enzyme 2 ◽  
New Type ◽  
Amino Acid Mutations ◽  
Host Infection ◽  
Human Coronaviruses ◽  
Novel Coronavirus

<b><i>Introduction:</i></b> SARS-CoV-2 is a new type of coronavirus causing a pandemic severe acute respiratory syndrome (SARS-2). Coronaviruses are very diverting genetically and mutate so often periodically. The natural selection of viral mutations may cause host infection selectivity and infectivity. <b><i>Methods:</i></b> This study was aimed to indicate the diversity between human and animal coronaviruses through finding the rate of mutation in each of the spike, nucleocapsid, envelope, and membrane proteins. <b><i>Results:</i></b> The mutation rate is abundant in all 4 structural proteins. The most number of statistically significant amino acid mutations were found in spike receptor-binding domain (RBD) which may be because it is responsible for a corresponding receptor binding in a broad range of hosts and host selectivity to infect. Among 17 previously known amino acids which are important for binding of spike to angiotensin-converting enzyme 2 (ACE2) receptor, all of them are conservative among human coronaviruses, but only 3 of them significantly are mutated in animal coronaviruses. A single amino acid aspartate-454, that causes dissociation of the RBD of the spike and ACE2, and F486 which gives the strength of binding with ACE2 remain intact in all coronaviruses. <b><i>Discussion/Conclusion:</i></b> Observations of this study provided evidence of the genetic diversity and rapid evolution of SARS-CoV-2 as well as other human and animal coronaviruses.

Sign in / Sign up

Export Citation Format

Share Document