scholarly journals Influence of single amino acid substitutions in the hemagglutinin on antigenic and receptor-binding properties of influenza virus B/Florida/04/2006 of Yamagata-like evolutionary lineage

2016 ◽  
Vol 3 (1) ◽  
pp. 56-60
Author(s):  
Evgeniy V. Sorokin ◽  
◽  
Tatyana R. Tsareva ◽  
Anna A. Sominina ◽  
Maria M. Pisareva ◽  
...  
Keyword(s):  
Influenza Virus ◽  
Amino Acid ◽  
Receptor Binding ◽  
Single Amino Acid ◽  
Amino Acid Substitutions ◽  
Binding Properties ◽  
Evolutionary Lineage

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

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

Single Amino Acid Substitutions in Puroindoline-b Mutants Influence Lipid Binding Properties†

Biochemistry ◽  
2007 ◽  
Vol 46 (8) ◽  
pp. 2260-2266 ◽  
Author(s):  
Luke A. Clifton ◽  
Mitaben D. Lad ◽  
Rebecca J. Green ◽  
Richard A. Frazier
Keyword(s):  
Amino Acid ◽  
Lipid Binding ◽  
Single Amino Acid ◽  
Amino Acid Substitutions ◽  
Binding Properties

scholarly journals Antigenic drift in influenza A viruses. I. Selection and characterization of antigenic variants of A/PR/8/34 [HON1] influenza virus with monoclonal antibodies

1978 ◽  
Vol 148 (2) ◽  
pp. 383-392 ◽  
Author(s):  
W Gerhard ◽  
RG Webster
Keyword(s):  
Influenza Virus ◽  
Monoclonal Antibodies ◽  
Amino Acid ◽  
Influenza A ◽  
Antigenic Drift ◽  
Single Amino Acid ◽  
Amino Acid Substitutions ◽  
Parent Virus ◽  
Influenza A Viruses

Antigenic variants of A/PR/8/34 [HON1] influenza virus were selected after a single passage of the parent virus in embryonated chicken eggs in the presence of monoclonal antibodies to this virus. The monoclonal antibodies were produced by a hybridoma and were specific for an antigenic determinant on the HA molecule of the parent virus. Seven antigenic variants were analyzed with 95 monoclonal anti-HA antibodies prepared in vitro in the splenic fragment culture system. Three subgroups of antigenic variants were distinguished. The antigenic changes were primarily recognized by monoclonal antibodies to the strain- specific determinants of the parental hemagglutinin (HA) molecule. Monoclonal antibodies to HA determinants shared (in an identical or cross-reactive form) by parental virus and more than three heterologous viruses of the HON1 and H1N1 subtypes were unable to recognize the antigenic change on the variants. Similarly, heterogeneous antibody preparations could not differentiate between parental and variant viruses. The results are compatible with the idea that the HA of PR8 has available a large repertoire of antigenic modifications that may result from single amino acid substitutions, and that antigenic changes can occur in the strain- specific determinants on the HA molecule in the absence of concomitant changes in the cross-reactive HA determinants. The findings suggest that antigenic drift, in order to be epidemiologically significant, probably requires a series of amino acid substitutions in, or close to, the antigenic area on the HA molecule.

scholarly journals Mutations in the alpha 2 helix of HLA-A2 affect presentation but do not inhibit binding of influenza virus matrix peptide.

1988 ◽  
Vol 168 (2) ◽  
pp. 725-736 ◽  
Author(s):  
K T Hogan ◽  
N Shimojo ◽  
S F Walk ◽  
V H Engelhard ◽  
W L Maloy ◽  
...  
Keyword(s):  
Influenza Virus ◽  
Amino Acid ◽  
Binding Site ◽  
Influenza A ◽  
Matrix Protein ◽  
Peptide Binding ◽  
Single Amino Acid ◽  
Amino Acid Substitutions ◽  
Apparent Difference ◽  
Peptide Binding Site

Previous studies have suggested that MHC class I molecules bind and present peptides to CTL in a manner that is analogous to the presentation of peptides by class II molecules to Th. Crystallographic studies of HLA-A2 have led to the assignment of a putative peptide binding site that is bordered by two alpha helices consisting of residues 50-84 and 138-180. In this study, we have investigated whether residues in the alpha 2 helix are involved in the binding and/or presentation of a peptide to CTL. We have generated CTL to type A influenza virus by stimulation of human PBL with a synthetic peptide from the influenza A virus matrix protein (M1 residues 57-68) in the presence of rIL-2. Such HLA-A2.1-restricted influenza virus-immune CTL do not recognize infected HLA-A2.3+ targets. A2.1 and A2.3 differ by three amino acids in the alpha 2 domain: Ala vs. Thr at position 149, Val vs. Glu at position 152, and Leu vs. Trp at position 156. Site-directed mutants of the A2.1 gene that encode A2 molecules that resemble A2.3 at positions 149, 152, and 156 have been constructed, transfected into human cells, and assayed for their ability to present the M1 peptide. The results demonstrate that most, but not all, A2.1-restricted M1-peptide-specific CTL fail to recognize M1 peptide-exposed transfectants with certain single amino acid substitutions at positions 152 and 156. In contrast, M1 peptide-exposed transfectants that express A2 molecules with an Ala----Thr substitution at position 149 were recognized by all CTL tested, but they exhibited an apparent difference in the kinetics of peptide binding. These results indicate that amino acid substitutions at positions 152 and 156 of the putative peptide binding site of the A2 molecule can affect presentation without eliminating binding, and indicate that the failure to recognize complexes between the peptide and the mutant A2 molecules is due to different TCR specificities and not to the failure to bind the peptide.

scholarly journals Early Alterations of the Receptor-Binding Properties of H1, H2, and H3 Avian Influenza Virus Hemagglutinins after Their Introduction into Mammals

2000 ◽  
Vol 74 (18) ◽  
pp. 8502-8512 ◽  
Author(s):  
Mikhail Matrosovich ◽  
Alexander Tuzikov ◽  
Nikolai Bovin ◽  
Alexandra Gambaryan ◽  
Alexander Klimov ◽  
...  
Keyword(s):  
Amino Acid ◽  
Avian Influenza ◽  
Receptor Binding ◽  
Influenza Viruses ◽  
Interspecies Transmission ◽  
Amino Acid Substitutions ◽  
Single Mutation ◽  
Binding Properties ◽  
Avian Virus ◽  
Human Viruses

ABSTRACT Interspecies transmission of influenza A viruses circulating in wild aquatic birds occasionally results in influenza outbreaks in mammals, including humans. To identify early changes in the receptor binding properties of the avian virus hemagglutinin (HA) after interspecies transmission and to determine the amino acid substitutions responsible for these alterations, we studied the HAs of the initial isolates from the human pandemics of 1957 (H2N2) and 1968 (H3N2), the European swine epizootic of 1979 (H1N1), and the seal epizootic of 1992 (H3N3), all of which were caused by the introduction of avian virus HAs into these species. The viruses were assayed for their ability to bind the synthetic sialylglycopolymers 3′SL-PAA and 6′SLN-PAA, which contained, respectively, 3′-sialyllactose (the receptor determinant preferentially recognized by avian influenza viruses) and 6′-sialyl(N-acetyllactosamine) (the receptor determinant for human viruses). Avian and seal viruses bound 6′SLN-PAA very weakly, whereas the earliest available human and swine epidemic viruses bound this polymer with a higher affinity. For the H2 and H3 strains, a single mutation, 226Q→L, increased binding to 6′SLN-PAA, while among H1 swine viruses, the 190E→D and 225G→E mutations in the HA appeared important for the increased affinity of the viruses for 6′SLN-PAA. Amino acid substitutions at positions 190 and 225 with respect to the avian virus consensus sequence are also present in H1 human viruses, including those that circulated in 1918, suggesting that substitutions at these positions are important for the generation of H1 human pandemic strains. These results show that the receptor-binding specificity of the HA is altered early after the transmission of an avian virus to humans and pigs and, therefore, may be a prerequisite for the highly effective replication and spread which characterize epidemic strains.

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