scholarly journals Change in Receptor-Binding Specificity of Recent Human Influenza A Viruses (H3N2): A Single Amino Acid Change in Hemagglutinin Altered Its Recognition of Sialyloligosaccharides

Virology ◽  
2000 ◽  
Vol 278 (2) ◽  
pp. 587-596 ◽  
Author(s):  
E. Nobusawa ◽  
H. Ishihara ◽  
T. Morishita ◽  
K. Sato ◽  
K. Nakajima
Keyword(s):  
Amino Acid ◽  
Receptor Binding ◽  
Influenza A ◽  
Amino Acid Change ◽  
Binding Specificity ◽  
Single Amino Acid ◽  
Human Influenza ◽  
Influenza A Viruses ◽  
Single Amino Acid Change ◽  
Receptor Binding Specificity

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.

Rapid Identification of the Receptor-Binding Specificity of Influenza A Viruses by Fluorogenic Glycofoldamers

2016 ◽  
Vol 55 (45) ◽  
pp. 13995-13999 ◽  
Author(s):  
Xiao-Peng He ◽  
Ya-Li Zeng ◽  
Xin-Ying Tang ◽  
Na Li ◽  
Dong-Ming Zhou ◽  
...  
Keyword(s):  
Receptor Binding ◽  
Influenza A ◽  
Binding Specificity ◽  
Rapid Identification ◽  
Influenza A Viruses ◽  
Receptor Binding Specificity

Rapid Identification of the Receptor-Binding Specificity of Influenza A Viruses by Fluorogenic Glycofoldamers

2016 ◽  
Vol 128 (45) ◽  
pp. 14201-14205 ◽  
Author(s):  
Xiao-Peng He ◽  
Ya-Li Zeng ◽  
Xin-Ying Tang ◽  
Na Li ◽  
Dong-Ming Zhou ◽  
...  
Keyword(s):  
Receptor Binding ◽  
Influenza A ◽  
Binding Specificity ◽  
Rapid Identification ◽  
Influenza A Viruses ◽  
Receptor Binding Specificity

scholarly journals FlexibilityIn Vitroof Amino Acid 226 in the Receptor-Binding Site of an H9 Subtype Influenza A Virus and Its EffectIn Vivoon Virus Replication, Tropism, and Transmission

2018 ◽  
Vol 93 (6) ◽  
Author(s):  
Adebimpe O. Obadan ◽  
Jefferson Santos ◽  
Lucas Ferreri ◽  
Andrew J. Thompson ◽  
Silvia Carnaccini ◽  
...  
Keyword(s):  
Public Health ◽  
Amino Acids ◽  
Influenza Virus ◽  
Amino Acid ◽  
Influenza A ◽  
Amino Acid Change ◽  
Single Amino Acid ◽  
Receptor Binding Site ◽  
Single Amino Acid Change

ABSTRACTInfluenza A viruses (IAVs) remain a significant public health threat, causing more than 300,000 hospitalizations in the United States during the 2015–2016 season alone. While only a few IAVs of avian origin have been associated with human infections, the ability of these viruses to cause zoonotic infections further increases the public health risk of influenza. Of these, H9N2 viruses in Asia are of particular importance as they have contributed internal gene segments to other emerging zoonotic IAVs. Notably, recent H9N2 viruses have acquired molecular markers that allow for a transition from avian-like to human-like terminal sialic acid (SA) receptor recognition via a single amino acid change at position 226 (H3 numbering), from glutamine (Q226) to leucine (L226), within the hemagglutinin (HA) receptor-binding site (RBS). We sought to determine the plasticity of amino acid 226 and the biological effects of alternative amino acids on variant viruses. We created a library of viruses with the potential of having any of the 20 amino acids at position 226 on a prototypic H9 HA subtype IAV. We isolated H9 viruses that carried naturally occurring amino acids, variants found in other subtypes, and variants not found in any subtype at position 226. Fitness studies in quails revealed that some natural amino acids conferred anin vivoreplication advantage. This study shows the flexibility of position 226 of the HA of H9 influenza viruses and the resulting effect of single amino acid changes on the phenotype of variantsin vivoandin vitro.IMPORTANCEA single amino acid change at position 226 in the hemagglutinin (HA) from glutamine (Q) to leucine (L) has been shown to play a key role in receptor specificity switching in various influenza virus HA subtypes, including H9. We tested the flexibility of amino acid usage and determined the effects of such changes. The results reveal that amino acids other than L226 and Q226 are well tolerated and that some amino acids allow for the recognition of both avian and human influenza virus receptors in the absence of other changes. Our results can inform better avian influenza virus surveillance efforts as well as contribute to rational vaccine design and improve structural molecular dynamics algorithms.

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