Fitness costs limit influenza A virus hemagglutinin glycosylation as an immune evasion strategy. - Wikidata - awgldk - TriplyDB

Fitness costs limit influenza A virus hemagglutinin glycosylation as an immune evasion strategy.

Fitness costs limit influenza A virus hemagglutinin glycosylation as an immune evasion strategy.

http://www.wikidata.org/entity/Q35650895

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Connecting the study of wild influenza with the potential for pandemic disease Evolution of the receptor binding properties of the influenza A(H3N2) hemagglutinin Structure and receptor binding preferences of recombinant human A(H3N2) virus hemagglutinins The M segment of the 2009 pandemic influenza virus confers increased neuraminidase activity, filamentous morphology, and efficient contact transmissibility to A/Puerto Rico/8/1934-based reassortant viruses Compensatory hemagglutinin mutations alter antigenic properties of influenza viruses Epitope specific T-cell responses against influenza A in a healthy population.Playing hide and seek: how glycosylation of the influenza virus hemagglutinin can modulate the immune response to infection.Bird to human transmission biases and vaccine escape mutants in H5N1 infections Expansion of genotypic diversity and establishment of 2009 H1N1 pandemic-origin internal genes in pigs in China.Molecular determinants of influenza virus pathogenesis in mice.Amino Acid Substitutions Improve the Immunogenicity of H7N7HA Protein and Protect Mice against Lethal H7N7 Viral Challenge.N-linked glycosylation in the hemagglutinin of influenza A viruses.H5N1 receptor specificity as a factor in pandemic risk Genetic requirement for hemagglutinin glycosylation and its implications for influenza A H1N1 virus evolution Glycosylations in the globular head of the hemagglutinin protein modulate the virulence and antigenic properties of the H1N1 influenza viruses Fitness Inference from Short-Read Data: Within-Host Evolution of a Reassortant H5N1 Influenza Virus Compensatory evolution of net-charge in influenza A virus hemagglutinin.A combination of HA and PA mutations enhances virulence in a mouse-adapted H6N6 influenza A virus.Comparative glycomics analysis of influenza Hemagglutinin (H5N1) produced in vaccine relevant cell platforms.Glycan masking of hemagglutinin for adenovirus vector and recombinant protein immunizations elicits broadly neutralizing antibodies against H5N1 avian influenza viruses.Glycosylation of Residue 141 of Subtype H7 Influenza A Hemagglutinin (HA) Affects HA-Pseudovirus Infectivity and Sensitivity to Site A Neutralizing Antibodies The effects of a deleterious mutation load on patterns of influenza A/H3N2's antigenic evolution in humans Glycan-dependent immunogenicity of recombinant soluble trimeric hemagglutinin.Influenza A Virus-Induced Expression of a GalNAc Transferase, GALNT3, via MicroRNAs Is Required for Enhanced Viral Replication.The evolutionary dynamics of receptor binding avidity in influenza A: a mathematical model for a new antigenic drift hypothesis.Defining influenza A virus hemagglutinin antigenic drift by sequential monoclonal antibody selection.Greasing the SCIDs for universal flu antibodies The Molecular Determinants of Antibody Recognition and Antigenic Drift in the H3 Hemagglutinin of Swine Influenza A Virus.A mutant influenza virus that uses an N1 neuraminidase as the receptor-binding protein.Integrated Omics and Computational Glycobiology Reveal Structural Basis for Influenza A Virus Glycan Microheterogeneity and Host Interactions.The paramyxovirus polymerase complex as a target for next-generation anti-paramyxovirus therapeutics.Assessing the oseltamivir-induced resistance risk and implications for influenza infection control strategies Biological roles of glycans.A Perspective on the Structural and Functional Constraints for Immune Evasion: Insights from Influenza Virus.Adaptive mutations of neuraminidase stalk truncation and deglycosylation confer enhanced pathogenicity of influenza A viruses.Expected Effect of Deleterious Mutations on Within-Host Adaptation of Pathogens.Migration of the swine influenza virus δ-cluster hemagglutinin N-linked glycosylation site from N142 to N144 results in loss of antibody cross-reactivity.Guiding the immune response against influenza virus hemagglutinin toward the conserved stalk domain by hyperglycosylation of the globular head domain Molecular characterization of the surface glycoprotein genes of highly pathogenic H5N1 avian influenza viruses detected in Iran in 2011.Antigenicity of the 2015-2016 seasonal H1N1 human influenza virus HA and NA proteins.

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P2860

Fitness costs limit influenza A virus hemagglutinin glycosylation as an immune evasion strategy.

http://www.wikidata.org/entity/Q35650895

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Fitness costs limit influenza ...... as an immune evasion strategy.

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Fitness costs limit influenza ...... as an immune evasion strategy.

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Fitness costs limit influenza ...... as an immune evasion strategy.

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Fitness costs limit influenza ...... as an immune evasion strategy.

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PNAS.1108754108

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Proceedings of the National Academy of Sciences of the United States of America

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Fitness costs limit influenza ...... as an immune evasion strategy

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Jack R Bennink

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James S Gibbs

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Loren Schmidt

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Scott E Hensley

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William L Ince

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P2860

Influenza A virus hemagglutinin antibody escape promotes neuraminidase antigenic variation and drug resistance

Heterosubtypic neutralizing monoclonal antibodies cross-protective against H5N1 and H1N1 recovered from human IgM+ memory B cells

Hemagglutinin receptor binding avidity drives influenza A virus antigenic drift

Antibody recognition of a highly conserved influenza virus epitope

The structure and function of the hemagglutinin membrane glycoprotein of influenza virus

Glycan shielding of the influenza virus hemagglutinin contributes to immunopathology in mice.

Functional contributions of carbohydrate on AIDS virus glycoprotein

Structural basis of influenza virus neutralization.

Glycosylation focuses sequence variation in the influenza A virus H1 hemagglutinin globular domain.

Structural and functional implications of a restricted antibody response to a defined antigenic region on the influenza virus hemagglutinin.

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10.1073/PNAS.1108754108

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51

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108

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Alexandre David

Suman Ranjan Das

Jonathan W Yewdell

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2011-11-21T00:00:00Z

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51817931

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22106257

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3251056

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