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Evidence for influenza B virus hemagglutinin adaptation to the human host: high cleavability, acid-stability and preference for cool temperature

https://doi.org/10.1101/736678
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Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1002/biot.201300225openalex-snapshot
Egg‐ or cell culture‐derived hemagglutinin mutations impair virus stability and antigen content of inactivated influenza vaccines
inferredcites →https://doi.org/10.1002/j.1460-2075.1986.tb04576.xopenalex-snapshot
Mutations blocking the transport of the influenza virus hemagglutinin between the rough endoplasmic reticulum and the Golgi apparatus.
inferredcites →https://doi.org/10.1006/viro.1997.8749openalex-snapshot
Expression of Influenza B Virus Hemagglutinin Containing Multibasic Residue Cleavage Sites
inferredcites →https://doi.org/10.1006/viro.2002.1730openalex-snapshot
DC-SIGN and DC-SIGNR Bind Ebola Glycoproteins and Enhance Infection of Macrophages and Endothelial Cells
inferredcites →https://doi.org/10.1007/82_2014_393openalex-snapshot
Acid-Induced Membrane Fusion by the Hemagglutinin Protein and Its Role in Influenza Virus Biology
inferredcites →https://doi.org/10.1007/978-3-319-75474-1openalex-snapshot
Activation of Viruses by Host Proteases
inferredcites →https://doi.org/10.1007/s00232-006-0861-0openalex-snapshot
Mechanisms of Acid and Base Secretion by the Airway Epithelium
inferredcites →https://doi.org/10.1007/s007050050428openalex-snapshot
Endogenous protease-dependent replication of human influenza viruses in two MDCK cell lines
inferredcites →https://doi.org/10.1016/0042-6822(75)90284-6openalex-snapshot
Activation of influenza A viruses by trypsin treatment
inferredcites →https://doi.org/10.1016/0300-9629(91)90122-sopenalex-snapshot
Body temperature in birds
inferredcites →https://doi.org/10.1016/0966-842x(94)90123-6openalex-snapshot
Host cell proteases controlling virus pathogenicity
inferredcites →https://doi.org/10.1016/j.ab.2011.04.018openalex-snapshot
An unbiased approach for analysis of protein glycosylation and application to influenza vaccine hemagglutinin
inferredcites →https://doi.org/10.1016/j.antiviral.2015.01.011openalex-snapshot
Protease inhibitors targeting coronavirus and filovirus entry
inferredcites →https://doi.org/10.1016/j.biochi.2015.09.023openalex-snapshot
Kallikreins – The melting pot of activity and function
inferredcites →https://doi.org/10.1016/j.cell.2014.02.040openalex-snapshot
Identification, Characterization, and Natural Selection of Mutations Driving Airborne Transmission of A/H5N1 Virus
inferredcites →https://doi.org/10.1016/j.cell.2018.05.050openalex-snapshot
Direct Visualization of the Conformational Dynamics of Single Influenza Hemagglutinin Trimers
inferredcites →https://doi.org/10.1016/j.cell.2018.06.024openalex-snapshot
Toward a Choate View of Fate
inferredcites →https://doi.org/10.1016/j.cmi.2019.02.011openalex-snapshot
European all-cause excess and influenza-attributable mortality in the 2017/18 season: should the burden of influenza B be reconsidered?
inferredcites →https://doi.org/10.1016/j.coviro.2017.03.018openalex-snapshot
Airway proteases: an emerging drug target for influenza and other respiratory virus infections
inferredcites →https://doi.org/10.1016/j.ejcb.2015.05.013openalex-snapshot
Influenza virus activating host proteases: Identification, localization and inhibitors as potential therapeutics
inferredcites →https://doi.org/10.1016/j.tim.2018.03.005openalex-snapshot
Influenza Hemagglutinin Protein Stability, Activation, and Pandemic Risk
inferredcites →https://doi.org/10.1016/j.vaccine.2012.10.001openalex-snapshot
Hemagglutinin activating host cell proteases provide promising drug targets for the treatment of influenza A and B virus infections
inferredcites →https://doi.org/10.1016/j.virol.2008.08.010openalex-snapshot
Molecular studies of temperature-sensitive replication of the cold-adapted B/Ann Arbor/1/66, the master donor virus for live attenuated influenza FluMist® vaccines
inferredcites →https://doi.org/10.1016/j.virol.2013.07.035openalex-snapshot
Structural basis for the divergent evolution of influenza B virus hemagglutinin
inferredcites →https://doi.org/10.1016/j.virol.2016.02.021openalex-snapshot
Intravirion cohesion of matrix protein M1 with ribonucleocapsid is a prerequisite of influenza virus infectivity
inferredcites →https://doi.org/10.1016/s0006-3495(02)75275-2openalex-snapshot
Measuring pKa of Activation and pKi of Inactivation for Influenza Hemagglutinin from Kinetics of Membrane Fusion of Virions and of HA Expressing Cells
inferredcites →https://doi.org/10.1016/s0092-8674(00)81771-7openalex-snapshot
Structure of the Hemagglutinin Precursor Cleavage Site, a Determinant of Influenza Pathogenicity and the Origin of the Labile Conformation
inferredcites →https://doi.org/10.1016/s0140-6736(17)33293-2openalex-snapshot
Estimates of global seasonal influenza-associated respiratory mortality: a modelling study
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The CF mouse: an important tool for studying cystic fibrosis
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Mechanisms of cell entry by influenza virus
inferredcites →https://doi.org/10.1038/nature02951openalex-snapshot
Enhanced virulence of influenza A viruses with the haemagglutinin of the 1918 pandemic virus
inferredcites →https://doi.org/10.1038/nature10831openalex-snapshot
Experimental adaptation of an influenza H5 HA confers respiratory droplet transmission to a reassortant H5 HA/H1N1 virus in ferrets
inferredcites →https://doi.org/10.1038/ncomms7553openalex-snapshot
Mammalian adaptation of influenza A(H7N9) virus is limited by a narrow genetic bottleneck
inferredcites →https://doi.org/10.1038/nrm934openalex-snapshot
Furin at the cutting edge: From protein traffic to embryogenesis and disease
inferredcites →https://doi.org/10.1038/s41579-018-0115-zopenalex-snapshot
Host and viral determinants of influenza A virus species specificity
inferredcites →https://doi.org/10.1038/srep29430openalex-snapshot
TMPRSS2 Independency for Haemagglutinin Cleavage In Vivo Differentiates Influenza B Virus from Influenza A Virus
inferredcites →https://doi.org/10.1042/bj20071496openalex-snapshot
Hepatocyte growth factor activator inhibitor-1 has a complex subcellular itinerary
inferredcites →https://doi.org/10.1046/j.1365-2273.1999.00223.xopenalex-snapshot
Nasal pH measurement: a reliable and repeatable parameter
inferredcites →https://doi.org/10.1046/j.1365-2273.2002.00544.xopenalex-snapshot
Nasal mucosal temperature during respiration
inferredcites →https://doi.org/10.1063/1.335663openalex-snapshot
Electrolyte thickness dependence of the electrochromic behavior of ‘‘a-WO3’’ films
inferredcites →https://doi.org/10.1073/pnas.0807771105openalex-snapshot
Single-particle kinetics of influenza virus membrane fusion
inferredcites →https://doi.org/10.1073/pnas.1524384113openalex-snapshot
Molecular requirements for a pandemic influenza virus: An acid-stable hemagglutinin protein
inferredcites →https://doi.org/10.1074/jbc.m111.262048openalex-snapshot
Biochemical Impact of the Host Adaptation-associated PB2 E627K Mutation on the Temperature-dependent RNA Synthesis Kinetics of Influenza A Virus Polymerase Complex
inferredcites →https://doi.org/10.1074/jbc.m112.440362openalex-snapshot
Cleavage Activation of Human-adapted Influenza Virus Subtypes by Kallikrein-related Peptidases 5 and 12
inferredcites →https://doi.org/10.1074/jbc.r110.129809openalex-snapshot
Influenza Hemagglutinin and Neuraminidase Membrane Glycoproteins
inferredcites →https://doi.org/10.1083/jcb.139.3.613openalex-snapshot
The Number and Location of Glycans on Influenza Hemagglutinin Determine Folding and Association with Calnexin and Calreticulin
inferredcites →https://doi.org/10.1093/infdis/jiv246openalex-snapshot
Identification ofTMPRSS2as a Susceptibility Gene for Severe 2009 Pandemic A(H1N1) Influenza and A(H7N9) Influenza
inferredcites →https://doi.org/10.1093/oxfordjournals.aje.a118408openalex-snapshot
A SIMPLE METHOD OF ESTIMATING FIFTY PER CENT ENDPOINTS12
inferredcites →https://doi.org/10.1093/oxfordjournals.molbev.a004105openalex-snapshot
Origin and Evolution of Influenza Virus Hemagglutinin Genes
inferredcites →https://doi.org/10.1099/0022-1317-65-11-1889openalex-snapshot
Physiological Characterization of Influenza Virus Temperature-sensitive Mutants Defective in the Haemagglutinin Gene
inferredcites →https://doi.org/10.1099/jgv.0.001235openalex-snapshot
Influenza virus entry via the GM3 ganglioside-mediated platelet-derived growth factor receptor β signalling pathway
inferredcites →https://doi.org/10.1099/jgv.0.001274openalex-snapshot
Tmprss2 knock-out mice are resistant to H10 influenza A virus pathogenesis
inferredcites →https://doi.org/10.1099/vir.0.035782-0openalex-snapshot
Altered receptor specificity and fusion activity of the haemagglutinin contribute to high virulence of a mouse-adapted influenza A virus
inferredcites →https://doi.org/10.1111/irv.12258openalex-snapshot
Estimates of mortality attributable to influenza and RSV in the U nited S tates during 1997–2009 by influenza type or subtype, age, cause of death, and risk status
inferredcites →https://doi.org/10.1126/science.1093373openalex-snapshot
Structure of the Uncleaved Human H1 Hemagglutinin from the Extinct 1918 Influenza Virus
inferredcites →https://doi.org/10.1126/science.1119392openalex-snapshot
Characterization of the Reconstructed 1918 Spanish Influenza Pandemic Virus
inferredcites →https://doi.org/10.1126/science.288.5468.1051openalex-snapshot
Influenza B Virus in Seals
inferredcites →https://doi.org/10.1128/jvi.00058-19openalex-snapshot
Influenza Virus with Increased pH of Hemagglutinin Activation Has Improved Replication in Cell Culture but at the Cost of Infectivity in Human Airway Epithelium
inferredcites →https://doi.org/10.1128/jvi.00124-15openalex-snapshot
A Mutant H3N2 Influenza Virus Uses an Alternative Activation Mechanism in TMPRSS2 Knockout Mice by Loss of an Oligosaccharide in the Hemagglutinin Stalk Region
inferredcites →https://doi.org/10.1128/jvi.00239-10openalex-snapshot
TMPRSS2 and TMPRSS4 Facilitate Trypsin-Independent Spread of Influenza Virus in Caco-2 Cells
inferredcites →https://doi.org/10.1128/jvi.00246-17openalex-snapshot
pH Optimum of Hemagglutinin-Mediated Membrane Fusion Determines Sensitivity of Influenza A Viruses to the Interferon-Induced Antiviral State and IFITMs
inferredcites →https://doi.org/10.1128/jvi.00301-18openalex-snapshot
New Threats from H7N9 Influenza Virus: Spread and Evolution of High- and Low-Pathogenicity Variants with High Genomic Diversity in Wave Five
inferredcites →https://doi.org/10.1128/jvi.00306-12openalex-snapshot
Cleavage Activation of the Human-Adapted Influenza Virus Subtypes by Matriptase Reveals both Subtype and Strain Specificities
inferredcites →https://doi.org/10.1128/jvi.00441-17openalex-snapshot
Identification of Interleukin-27 (IL-27)/IL-27 Receptor Subunit Alpha as a Critical Immune Axis for In Vivo HIV Control
inferredcites →https://doi.org/10.1128/jvi.00649-19openalex-snapshot
TMPRSS2 Is the Major Activating Protease of Influenza A Virus in Primary Human Airway Cells and Influenza B Virus in Human Type II Pneumocytes
inferredcites →https://doi.org/10.1128/jvi.01427-14openalex-snapshot
DESC1 and MSPL Activate Influenza A Viruses and Emerging Coronaviruses for Host Cell Entry
inferredcites →https://doi.org/10.1128/jvi.01925-12openalex-snapshot
Intrinsic Temperature Sensitivity of Influenza C Virus Hemagglutinin-Esterase-Fusion Protein
inferredcites →https://doi.org/10.1128/jvi.02205-08openalex-snapshot
Proteolytic Activation of the 1918 Influenza Virus Hemagglutinin
inferredcites →https://doi.org/10.1128/jvi.02320-12openalex-snapshot
Matriptase, HAT, and TMPRSS2 Activate the Hemagglutinin of H9N2 Influenza A Viruses
inferredcites →https://doi.org/10.1128/jvi.02325-09openalex-snapshot
Novel Inhibitors of Influenza Virus Fusion: Structure-Activity Relationship and Interaction with the Viral Hemagglutinin
inferredcites →https://doi.org/10.1128/jvi.02332-15openalex-snapshot
H1N1 Swine Influenza Viruses Differ from Avian Precursors by a Higher pH Optimum of Membrane Fusion
inferredcites →https://doi.org/10.1128/jvi.02753-12openalex-snapshot
1918 Influenza Virus Hemagglutinin (HA) and the Viral RNA Polymerase Complex Enhance Viral Pathogenicity, but Only HA Induces Aberrant Host Responses in Mice
inferredcites →https://doi.org/10.1128/jvi.03005-12openalex-snapshot
Matriptase Proteolytically Activates Influenza Virus and Promotes Multicycle Replication in the Human Airway Epithelium
inferredcites →https://doi.org/10.1128/jvi.03110-12openalex-snapshot
The pH of Activation of the Hemagglutinin Protein Regulates H5N1 Influenza Virus Replication and Pathogenesis in Mice
inferredcites →https://doi.org/10.1128/jvi.03677-13openalex-snapshot
The Host Protease TMPRSS2 Plays a Major Role in In Vivo Replication of Emerging H7N9 and Seasonal Influenza Viruses
inferredcites →https://doi.org/10.1128/jvi.03799-13openalex-snapshot
TMPRSS2 Is a Host Factor That Is Essential for Pneumotropism and Pathogenicity of H7N9 Influenza A Virus in Mice
inferredcites →https://doi.org/10.1128/jvi.66.12.7136-7145.1992openalex-snapshot
Glycosylation requirements for intracellular transport and function of the hemagglutinin of influenza virus
inferredcites →https://doi.org/10.1128/jvi.67.6.3048-3060.1993openalex-snapshot
Role of conserved glycosylation sites in maturation and transport of influenza A virus hemagglutinin
inferredcites →https://doi.org/10.1128/jvi.75.11.5398-5404.2001openalex-snapshot
Residue 627 of PB2 Is a Determinant of Cold Sensitivity in RNA Replication of Avian Influenza Viruses
inferredcites →https://doi.org/10.1136/thoraxjnl-2018-211929openalex-snapshot
Gene correlation network analysis to identify regulatory factors in idiopathic pulmonary fibrosis
inferredcites →https://doi.org/10.1152/jappl.1985.58.2.564openalex-snapshot
Thermal mapping of the airways in humans
inferredcites →https://doi.org/10.1183/09031936.03.00027603openalex-snapshot
Airway surface pH in subjects with cystic fibrosis
inferredcites →https://doi.org/10.1371/journal.pone.0015556openalex-snapshot
The Low-pH Stability Discovered in Neuraminidase of 1918 Pandemic Influenza A Virus Enhances Virus Replication
inferredcites →https://doi.org/10.1371/journal.pone.0075014openalex-snapshot
Heterogeneity of the MDCK Cell Line and Its Applicability for Influenza Virus Research
inferredcites →https://doi.org/10.1371/journal.ppat.1000424openalex-snapshot
Avian Influenza Virus Glycoproteins Restrict Virus Replication and Spread through Human Airway Epithelium at Temperatures of the Proximal Airways
inferredcites →https://doi.org/10.1371/journal.ppat.1003151openalex-snapshot
Influenza HA Subtypes Demonstrate Divergent Phenotypes for Cleavage Activation and pH of Fusion: Implications for Host Range and Adaptation
inferredcites →https://doi.org/10.1371/journal.ppat.1003774openalex-snapshot
Tmprss2 Is Essential for Influenza H1N1 Virus Pathogenesis in Mice
inferredcites →https://doi.org/10.1515/hsz-2012-0155openalex-snapshot
TMPRSS4 is a type II transmembrane serine protease involved in cancer and viral infections
inferredcites →https://doi.org/10.1515/hsz-2017-0340openalex-snapshot
Kallikrein-related peptidase 5 and seasonal influenza viruses, limitations of the experimental models for activating proteases
inferredcites →https://doi.org/10.2105/ajph.2012.301137openalex-snapshot
The Burden of Influenza B: A Structured Literature Review
inferredcites →https://doi.org/10.2217/fmb.15.120openalex-snapshot
Knowns and Unknowns of Influenza B Viruses
inferredcites →https://doi.org/10.3201/eid1201.050979openalex-snapshot
1918 Influenza: the Mother of All Pandemics
inferredcites →https://doi.org/10.3201/eid1201.051442openalex-snapshot
Influenza Revisited
inferredcites →https://doi.org/10.3389/fcimb.2018.00343openalex-snapshot
Back to the Future: Lessons Learned From the 1918 Influenza Pandemic
inferredcites →https://doi.org/10.3390/ijms18071541openalex-snapshot
The Interplay between the Host Receptor and Influenza Virus Hemagglutinin and Neuraminidase
inferredcites →https://doi.org/10.3390/v4071144openalex-snapshot
Influenza Virus-Mediated Membrane Fusion: Determinants of Hemagglutinin Fusogenic Activity and Experimental Approaches for Assessing Virus Fusion
inferredcites →https://doi.org/10.7554/elife.00333openalex-snapshot
Influenza-virus membrane fusion by cooperative fold-back of stochastically induced hemagglutinin intermediates
inferredcites →https://doi.org/10.7554/elife.05055openalex-snapshot
The contrasting phylodynamics of human influenza B viruses

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

inferred← citeshttps://doi.org/10.1128/jvi.01430-19openalex-snapshot
Hemagglutinin Cleavability, Acid Stability, and Temperature Dependence Optimize Influenza B Virus for Replication in Human Airways
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