Immune response of human volunteers and animals to vaccination with egg-grown influenza A (H1N1) virus is influenced by three amino acid substitutions in the haemagglutinin molecule

Vaccine ◽  
1993 ◽  
Vol 11 (4) ◽  
pp. 400-406 ◽  
Author(s):  
R.W. Newman ◽  
R. Jennings ◽  
D.L. Major ◽  
J.S. Robertson ◽  
R. Jenkins ◽  
...  
Keyword(s):  
Immune Response ◽  
Amino Acid ◽  
Influenza A ◽  
H1n1 Virus ◽  
Amino Acid Substitutions ◽  
Human Volunteers ◽  
Influenza A H1n1

scholarly journals Amino Acid Substitutions Analysis of the Putative Epitopes of Neuraminidase Protein from Influenza A H1N1 Virus

2021 ◽  
Vol 22 (1) ◽  
pp. 1-16
Author(s):  
Ludmila Alves Dias Souto ◽  
Alessandra Rejane Ericsson de Oliveira Xavier ◽  
Mauro Aparecido de Sousa Xavier
Keyword(s):  
Amino Acid ◽  
Influenza A ◽  
H1n1 Virus ◽  
Epitope Prediction ◽  
Viral Population ◽  
Amino Acid Substitutions ◽  
Specific Amino Acid ◽  
Influenza A H1n1 ◽  
Virus Sequence ◽  
Clustal Omega

Objective: This study verified whether the neuraminidase protein of Influenza A H1N1 virus sequence has modified from 2009–2017 and its impact on the 2018 Brazilian vaccine. Method: The reference neuraminidase protein sequence from H1N1 Puerto Rico/1934 strain was subjected to three different methods of epitope prediction and the top five from each method were aligned using Clustal omega, resulting in eight putative epitopes. These epitopes were aligned to 7,438 neuraminidase sequences spanning from 2009–2017 and analyzed for specific amino acid substitutions and counted. The resultant neuraminidase protein was aligned against the 2015 and 2018 neuraminidase proteins, from Influenza A H1N1 virus subtypes, used for vaccine production. Result: Twenty-one main substitutions were detected, of which 16/21 (76.2%) substitutions points remained stable and 1/21 (4.8%) returned to the original amino acid residue in the viral population from 2009–2017. Additionally, 19% (4/21) substitutions occurred in Brazil and worldwide in this period, indicating that changes in the neuraminidase viral population profile is time-dependent rather than geographical. Conclusion: The neuraminidase protein containing these amino acid substitutions is more closely related to the neuraminidase protein from influenza A/Michigan/45/2015 than A/California/7/2009, supporting the replacement of this virus subtype in the Brazilian vaccine in 2018.

scholarly journals MOLECULAR AND GENETIC CHARACTERISTICS OF SURFACE AND NONSTRUCTURE PROTEINS OF PANDEMIC INFLUENZA VIRUSES A(H1N1)PDM09 IN 2015-2016 EPIDEMIC SEASON

2016 ◽  
Vol 72 (2) ◽  
pp. 44-48
Author(s):  
O. Smutko ◽  
L. Radchenko ◽  
A. Mironenko
Keyword(s):  
Amino Acid ◽  
Pandemic Influenza ◽  
Influenza A ◽  
Phylogenetic Trees ◽  
Influenza Viruses ◽  
Amino Acid Substitutions ◽  
Ns1 Protein ◽  
Genetic Characteristics ◽  
Epidemic Season ◽  
Influenza A H1n1

The aim of the present study was identifying of molecular and genetic changes in hemaglutinin (HA), neuraminidase (NA) and non-structure protein (NS1) genes of pandemic influenza A(H1N1)pdm09 strains, that circulated in Ukraine during 2015-2016 epidemic season. Samples (nasopharyngeal swabs from patients) were analyzed using real-time polymerase chain reaction (RTPCR). Phylogenetic trees were constructed using MEGA 7 software. 3D structures were constructed in Chimera 1.11.2rc software. Viruses were collected in 2015-2016 season fell into genetic group 6B and in two emerging subgroups, 6B.1 and 6B.2 by gene of HA and NA. Subgroups 6B.1 and 6B.2 are defined by the following amino acid substitutions. In the NS1 protein were identified new amino acid substitutions D2E, N48S, and E125D in 2015-2016 epidemic season. Specific changes were observed in HA protein antigenic sites, but viruses saved similarity to vaccine strain. NS1 protein acquired substitution associated with increased virulence of the influenza virus.

Influenza A (H1N1) vaccine efficacy in animal models is influenced by two amino acid substitutions in the hemagglutinin molecule

Virology ◽  
1989 ◽  
Vol 171 (1) ◽  
pp. 214-221 ◽  
Author(s):  
John M. Wood ◽  
John S. Oxford ◽  
Una Dunleavy ◽  
Robert W. Newman ◽  
Diane Major ◽  
...  
Keyword(s):  
Amino Acid ◽  
Animal Models ◽  
Vaccine Efficacy ◽  
Influenza A ◽  
Amino Acid Substitutions ◽  
H1n1 Vaccine ◽  
Influenza A H1n1

scholarly journals Amino acid substitutions in hemagglutinin of the 2009 pandemic influenza A(H1N1) viruses that might affect the viral antigenicity

2014 ◽  
Vol 7 (1) ◽  
pp. 951 ◽  
Author(s):  
Nathamon Kosoltanapiwat ◽  
Usa Boonyuen ◽  
Phisanu Pooruk ◽  
Sopon Iamsirithaworn ◽  
Anek Mungaomklang ◽  
...  
Keyword(s):  
Amino Acid ◽  
Pandemic Influenza ◽  
Influenza A ◽  
Amino Acid Substitutions ◽  
Influenza A H1n1

scholarly journals Putative amino acid determinants of the emergence of the 2009 influenza A (H1N1) virus in the human population

2011 ◽  
Vol 108 (33) ◽  
pp. 13522-13527 ◽  
Author(s):  
D. Meroz ◽  
S.-W. Yoon ◽  
M. F. Ducatez ◽  
T. P. Fabrizio ◽  
R. J. Webby ◽  
...  
Keyword(s):  
Amino Acid ◽  
Human Population ◽  
Influenza A ◽  
H1n1 Virus ◽  
Influenza A H1n1

scholarly journals Conserved Genomic Terminals of SARS-CoV-2 as Co-evolving Functional Elements and Potential Therapeutic Targets

2020 ◽  
Author(s):  
Agnes. P. Chan ◽  
Yongwook Choi ◽  
Nicholas J. Schork
Keyword(s):  
Immune Response ◽  
Untranslated Region ◽  
Influenza A ◽  
H1n1 Virus ◽  
Therapeutic Targets ◽  
Unique Sequence ◽  
Functional Elements ◽  
Genome Wide ◽  
Influenza A H1n1 ◽  
Multiple Groups

ABSTRACTTo identify features in the genome of the SARS-CoV-2 pathogen responsible for the COVID-19 pandemic that may contribute to its viral replication, host pathogenicity, and vulnerabilities, we investigated how and to what extent the SARS-CoV-2 genome sequence differs from other well-characterized human and animal coronavirus genomes. Our analyses suggest the presence of unique sequence signatures in the 3’-untranslated region (UTR) of betacoronavirus lineage B, which phylogenetically encompasses SARS-CoV-2, SARS-CoV, as well as multiple groups of bat and animal coronaviruses. In addition, we identified genome-wide patterns of variation across different SARS-CoV-2 strains that likely reflect the effects of selection. Finally, we provide evidence for a possible host microRNA-mediated interaction between the 3’-UTR and human microRNA hsa-miR-1307-3p based on predicted, yet extensive, complementary base-pairings and similar interactions involving the Influenza A H1N1 virus. This interaction also suggests a possible survival mechanism, whereby a mutation in the SARS-CoV-2 3’-UTR leads to a weakened host immune response. The potential roles of host microRNAs in SARS-CoV-2 replication and infection, and the exploitation of conserved features in the 3’-UTR as therapeutic targets warrant further investigation.

Pleiotropic effects of hemagglutinin amino acid substitutions of influenza A(H1N1)pdm09 virus escape mutants

2018 ◽  
Vol 251 ◽  
pp. 91-97 ◽  
Author(s):  
Irina A. Rudneva ◽  
Tatiana A. Timofeeva ◽  
Evgenia A. Mukasheva ◽  
Anna V. Ignatieva ◽  
Aleksandr A. Shilov ◽  
...  
Keyword(s):  
Amino Acid ◽  
Influenza A ◽  
Pleiotropic Effects ◽  
Amino Acid Substitutions ◽  
Virus Escape ◽  
Pdm09 Virus ◽  
Influenza A H1n1 ◽  
Escape Mutants

scholarly journals Identification of Low- and High-Impact Hemagglutinin Amino Acid Substitutions That Drive Antigenic Drift of Influenza A(H1N1) Viruses

2016 ◽  
Vol 12 (4) ◽  
pp. e1005526 ◽  
Author(s):  
William T. Harvey ◽  
Donald J. Benton ◽  
Victoria Gregory ◽  
James P. J. Hall ◽  
Rodney S. Daniels ◽  
...  
Keyword(s):  
Amino Acid ◽  
Influenza A ◽  
High Impact ◽  
Antigenic Drift ◽  
Amino Acid Substitutions ◽  
Influenza A H1n1

scholarly journals Identification of Amino Acid Substitutions Supporting Antigenic Change of Influenza A(H1N1)pdm09 Viruses

2015 ◽  
Vol 89 (7) ◽  
pp. 3763-3775 ◽  
Author(s):  
Björn F. Koel ◽  
Ramona Mögling ◽  
Salin Chutinimitkul ◽  
Pieter L. Fraaij ◽  
David F. Burke ◽  
...  
Keyword(s):  
Amino Acid ◽  
Receptor Binding ◽  
Influenza A ◽  
Influenza Pandemic ◽  
Amino Acid Substitutions ◽  
Receptor Binding Site ◽  
Population Immunity ◽  
Influenza A H1n1 ◽  
Hemagglutinin Protein ◽  
2009 Influenza Pandemic

ABSTRACTThe majority of currently circulating influenza A(H1N1) viruses are antigenically similar to the virus that caused the 2009 influenza pandemic. However, antigenic variants are expected to emerge as population immunity increases. Amino acid substitutions in the hemagglutinin protein can result in escape from neutralizing antibodies, affect viral fitness, and change receptor preference. In this study, we constructed mutants with substitutions in the hemagglutinin of A/Netherlands/602/09 in an attenuated backbone to explore amino acid changes that may contribute to emergence of antigenic variants in the human population. Our analysis revealed that single substitutions affecting the loop that consists of amino acid positions 151 to 159 located adjacent to the receptor binding site caused escape from ferret and human antibodies elicited after primary A(H1N1)pdm09 virus infection. The majority of these substitutions resulted in similar or increased replication efficiencyin vitrocompared to that of the virus carrying the wild-type hemagglutinin and did not result in a change of receptor preference. However, none of the substitutions was sufficient for escape from the antibodies in sera from individuals that experienced both seasonal and pandemic A(H1N1) virus infections. These results suggest that antibodies directed against epitopes on seasonal A(H1N1) viruses contribute to neutralization of A(H1N1)pdm09 antigenic variants, thereby limiting the number of possible substitutions that could lead to escape from population immunity.IMPORTANCEInfluenza A viruses can cause significant morbidity and mortality in humans. Amino acid substitutions in the hemagglutinin protein can result in escape from antibody-mediated neutralization. This allows the virus to reinfect individuals that have acquired immunity to previously circulating strains through infection or vaccination. To date, the vast majority of A(H1N1)pdm09 strains remain antigenically similar to the virus that caused the 2009 influenza pandemic. However, antigenic variants are expected to emerge as a result of increasing population immunity. We show that single amino acid substitutions near the receptor binding site were sufficient to escape from antibodies specific for A(H1N1)pdm09 viruses but not from antibodies elicited in response to infections with seasonal A(H1N1) and A(H1N1)pdm09 viruses. This study identified substitutions in A(H1N1)pdm09 viruses that support escape from population immunity but also suggested that the number of potential escape variants is limited by previous exposure to seasonal A(H1N1) viruses.

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