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1. Full Text Broadly neutralizing hemagglutinin stalk-specific antibodies require Fc gamma R interactions for protection against influenza virus in vivo
by DiLillo, DJ and Tan, GS and Palese, P and Ravetch, JV
NATURE MEDICINE, ISSN 1078-8956, 02/2014, Volume 20, Issue 2, pp. 143 - 151
Neutralizing antibodies against influenza viruses have traditionally been thought to provide protection exclusively through their variable region; the... 
MEDICINE, RESEARCH & EXPERIMENTAL | IMMUNITY | BIOCHEMISTRY & MOLECULAR BIOLOGY | MONOCLONAL-ANTIBODY | IDENTIFICATION | INDUCED CONFORMATIONAL-CHANGES | CELL BIOLOGY | DEPENDENT CELLULAR CYTOTOXICITY | UNIVERSAL VACCINE | RECEPTOR-BINDING | CONSTANT-REGION | ANTIGEN | EPITOPES | Influenza A Virus, H1N1 Subtype - immunology | Surface Plasmon Resonance | Cell Line | Enzyme-Linked Immunosorbent Assay | Humans | Mice, Inbred C57BL | Antibodies, Neutralizing - metabolism | Kaplan-Meier Estimate | Neutralization Tests | Hemagglutinin Glycoproteins, Influenza Virus - immunology | Receptors, IgG - immunology | Chick Embryo | Receptors, IgG - metabolism | Mice, Knockout | Antibodies, Neutralizing - immunology | Animals | Dogs | Killer Cells, Natural - immunology | Mice | Antibodies, Monoclonal - metabolism | Antigen-Antibody Complex - immunology | Antibodies, Monoclonal - immunology
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2. Full Text Influenza hemagglutinin and neuraminidase membrane glycoproteins
by Gamblin, Steven J and Skehel, John J
Journal of Biological Chemistry, ISSN 0021-9258, 09/2010, Volume 285, Issue 37, pp. 28403 - 28409
Considerable progress has been made toward understanding the structural basis of the interaction of the two major surface glycoproteins of influenza A virus... 
COMPLEX | RECEPTOR-BINDING PROPERTIES | CELL-SURFACE RECEPTOR | A H1N1 VIRUSES | CLEAVAGE SITE | SPECIFICITY | BIOCHEMISTRY & MOLECULAR BIOLOGY | RESISTANCE | SIALIC-ACID | GLYCOSYLATION | STALK-LENGTH | Protein Structure, Tertiary | Hemagglutinin Glycoproteins, Influenza Virus - chemistry | Antiviral Agents - pharmacology | Antiviral Agents - therapeutic use | Humans | Influenza, Human - enzymology | Neuraminidase - metabolism | Structure-Activity Relationship | Influenza A virus - enzymology | Hemagglutinin Glycoproteins, Influenza Virus - metabolism | N-Acetylneuraminic Acid - metabolism | Virus Attachment - drug effects | Drug Resistance, Viral - physiology | Animals | Neuraminidase - chemistry | Drug Resistance, Viral - drug effects | Neuraminidase - antagonists & inhibitors | Influenza, Human - drug therapy | Virus Structure | Virus | Virus Entry | Viral Protein | Minireviews | Glycobiology and Extracellular Matrices | Viral Immunology | Virus Assembly
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3. Full Text Hemagglutinin-stem nanoparticles generate heterosubtypic influenza protection
by Yassine, Hadi M and Boyington, Jeffrey C and McTamney, Patrick M and Wei, Chih-Jen and Kanekiyo, Masaru and Kong, Wing-Pui and Gallagher, John R and Wang, Lingshu and Zhang, Yi and Joyce, M Gordon and Lingwood, Daniel and Moin, Syed M and Andersen, Hanne and Okuno, Yoshinobu and Rao, Srinivas S and Harris, Audray K and Kwong, Peter D and Mascola, John R and Nabel, Gary J and Graham, Barney S
Nature Medicine, ISSN 1078-8956, 09/2015, Volume 21, Issue 9, pp. 1065 - 1070
The antibody response to influenza is primarily focused on the head region of the hemagglutinin (HA) glycoprotein, which in turn undergoes antigenic drift,... 
MEDICINE, RESEARCH & EXPERIMENTAL | IMMUNITY | CELLS | DESIGN | COMPLEX | DOMAIN | VIRUS | BIOCHEMISTRY & MOLECULAR BIOLOGY | CELL BIOLOGY | DEPENDENT CELLULAR CYTOTOXICITY | IMMUNOGEN | MICE | MONOCLONAL-ANTIBODIES | Nanoparticles | Hemagglutinin Glycoproteins, Influenza Virus - chemistry | Animals | Influenza Vaccines - immunology | Influenza A Virus, H5N1 Subtype - immunology | Vaccination | Female | Mice | Mice, Inbred BALB C | Hemagglutinin Glycoproteins, Influenza Virus - immunology | Ferrets | Antibodies, Viral - blood | Influenza vaccines | Avian influenza | Prevention | Physiological aspects | Lectins | Research | B cells | Health aspects | Immunoglobulins | Influenza | Rodents
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4. Full Text Etymologia: Hemagglutinin and Neuraminidase
by Henry, Ronnie and Murphy, Frederick A
Emerging Infectious Diseases, ISSN 1080-6040, 10/2018, Volume 24, Issue 10, pp. 1849 - 1849
influenza | red blood cells | sialidase | viruses | Etymologia | hemagglutinin | neuraminic acid | subtypes | erythrocytes | Alfred Gottschalk | sialic acid | neuraminidase | influenza virus | agglutination | glycoprotein | Hemagglutinin and Neuraminidase | George K. Hirst
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5. Full Text Influenza hemagglutinin membrane anchor
by Benton, Donald J and Nans, Andrea and Calder, Lesley J and Turner, Jack and Neu, Ursula and Lin, Yi Pu and Ketelaars, Esther and Kallewaard, Nicole L and Corti, Davide and Lanzavecchia, Antonio and Gamblin, Steven J and Rosenthal, Peter B and Skehel, John J
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 10/2018, Volume 115, Issue 40, pp. 10112 - 10117
Viruses with membranes fuse them with cellular membranes, to transfer their genomes into cells at the beginning of infection. For Influenza virus, the membrane... 
Membrane fusion | Membrane protein | Hemagglutinin | Cryo-EM | Influenza | influenza | FUSION | PROTEIN | hemagglutinin | MULTIDISCIPLINARY SCIENCES | ANTIGENIC DRIFT | TRANSMEMBRANE DOMAIN | VIRUS HEMAGGLUTININ | CONFORMATION | membrane fusion | STRUCTURAL BASIS | membrane protein | CRYO-EM STRUCTURE | RECEPTOR-BINDING | cryo-EMI | Influenza viruses | Physiological aspects | Glycoproteins | Biological Sciences | cryo-EM
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6. Full Text Evaluation of the safety, reactogenicity and immunogenicity of FluBlok® trivalent recombinant baculovirus-expressed hemagglutinin influenza vaccine administered intramuscularly to healthy adults 50–64 years of age
by Baxter, R and Patriarca, P.A and Ensor, K and Izikson, R and Goldenthal, K.L and Cox, M.M
Vaccine, ISSN 0264-410X, 2011, Volume 29, Issue 12, pp. 2272 - 2278
Abstract Background Alternative methods for influenza vaccine production are needed to ensure adequate supplies. Methods Healthy adults 50–64 years were... 
Allergy and Immunology | Baculovirus | Hemagglutinin | Comparative immunogenicity | Influenza vaccine | Recombinant | MORTALITY | MEDICINE, RESEARCH & EXPERIMENTAL | CONTROLLED-TRIAL | CELLS | DOSE-RELATED SAFETY | IMMUNOLOGY | IMMUNE-RESPONSES | H3N2 VIRUS | ELDERLY ADULTS | Influenza A Virus, H1N1 Subtype - immunology | Single-Blind Method | Influenza Vaccines - administration & dosage | Humans | Middle Aged | Influenza Vaccines - adverse effects | Male | Hemagglutinin Glycoproteins, Influenza Virus - immunology | Vaccines, Synthetic - immunology | Influenza A Virus, H3N2 Subtype - immunology | Antibodies, Viral - blood | Vaccines, Inactivated - adverse effects | Vaccines, Inactivated - immunology | Influenza Vaccines - immunology | Vaccines, Inactivated - administration & dosage | Vaccines, Synthetic - adverse effects | Antibody Formation | Female | Vaccines, Synthetic - administration & dosage | Influenza, Human - prevention & control | Influenza, Human - immunology | Proteins | Immunization | Pain | Influenza | Licenses | Vaccines | Manufacturing | Age | Eggs | Methods
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7. Full Text Safety and Immunogenicity of a Baculovirus-Expressed Hemagglutinin Influenza Vaccine: A Randomized Controlled Trial
by Treanor, John J and Schiff, Gilbert M and Hayden, Frederick G and Brady, Rebecca C and Hay, C. Mhorag and Meyer, Anthony L and Holden-Wiltse, Jeanne and Liang, Hua and Gilbert, Adam and Cox, Manon
JAMA, ISSN 0098-7484, 04/2007, Volume 297, Issue 14, pp. 1577 - 1582
CONTEXT A high priority in vaccine research is the development of influenza vaccines that do not use embryonated eggs as the substrate for vaccine production.... 
A VIRUS | RECOMBINANT HEMAGGLUTININ | MEDICINE, GENERAL & INTERNAL | HEALTHY-ADULTS | IMMUNE-RESPONSES | H3N2 VIRUS | ELDERLY ADULTS | Influenza A Virus, H1N1 Subtype - immunology | Double-Blind Method | Humans | Immunodiffusion | Middle Aged | Baculoviridae - genetics | Male | Vaccines, DNA | Hemagglutinin Glycoproteins, Influenza Virus - immunology | Influenza A Virus, H3N2 Subtype - immunology | Hemagglutination Inhibition Tests | Influenza Vaccines - immunology | Adolescent | Adult | Female | Influenza B virus - immunology | Influenza vaccines | Prevention | Research | Baculoviruses | Human immunogenetics | Influenza | Clinical trials | Glycoproteins | Vaccines | Clinical outcomes
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8. Full Text Evaluation of the safety, reactogenicity and immunogenicity of FluBlok® trivalent recombinant baculovirus-expressed hemagglutinin influenza vaccine administered intramuscularly to healthy children aged 6–59 months
by King, James C and Cox, Manon M and Reisinger, Keith and Hedrick, James and Graham, Irene and Patriarca, Peter
Vaccine, ISSN 0264-410X, 2009, Volume 27, Issue 47, pp. 6589 - 6594
Abstract Background Recombinant baculovirus-expressed hemagglutinin (rHA [FluBlok® ]) influenza vaccine is unique in avoiding production in eggs and its rapid... 
Allergy and Immunology | Baculovirus vaccine | Children | Safety | Immunogenicity | Influenza | MEDICINE, RESEARCH & EXPERIMENTAL | VIRUS HEMAGGLUTININ | INSECT | IMMUNOLOGY | ANTIBODY-RESPONSES | Influenza A Virus, H1N1 Subtype - immunology | Double-Blind Method | Humans | Insecta | Influenza Vaccines - adverse effects | Child, Preschool | Infant | Hemagglutinin Glycoproteins, Influenza Virus - immunology | Vaccines, Synthetic - immunology | Influenza A Virus, H3N2 Subtype - immunology | Antibodies, Viral - blood | Baculoviridae - immunology | Animals | Influenza Vaccines - immunology | Influenza, Human - prevention & control | Influenza, Human - immunology | Confidence intervals | Antigens | Vaccines | Laboratories | Age
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9. Full Text An aptamer that binds efficiently to the hemagglutinins of highly pathogenic avian influenza viruses (H5N1 and H7N7) and inhibits hemagglutinin–glycan interactions
by Suenaga, Emi and Kumar, Penmetcha K.R
Acta Biomaterialia, ISSN 1742-7061, 03/2014, Volume 10, Issue 3, pp. 1314 - 1323
Highly pathogenic avian influenza (HPAI) H5 and H7 viruses have ravaged the poultry industry in numerous countries in Asia, Europe, Africa and the Middle East,... 
H5N1 | H7N7 | Aptamer | Influenza virus | Hemagglutinin | MATERIALS SCIENCE, BIOMATERIALS | ENGINEERING, BIOMEDICAL | CLEAVABILITY | H1N1 | CONNECTING PEPTIDE | DETERMINES | TRANSMISSION | ORIGIN | EVOLUTION | RNA APTAMER | RECEPTOR-BINDING | Surface Plasmon Resonance | Humans | Aptamers, Nucleotide - chemistry | Molecular Sequence Data | Aptamers, Nucleotide - metabolism | Hemagglutinin Glycoproteins, Influenza Virus - metabolism | Polysaccharides - metabolism | Aptamers, Nucleotide - genetics | Base Sequence | Protein Binding | Ligands | Influenza A Virus, H5N1 Subtype - metabolism | Kinetics | Nucleic Acid Conformation | Influenza A Virus, H7N7 Subtype - metabolism | Virus diseases | Avian influenza | Lectins | Avian influenza viruses | Analysis | Vietnam | Surveillance | Influenza | Reagents | Deletion | Viruses | Affinity | Evolution
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10. Full Text Glycan Receptor Binding of the Influenza A Virus H7N9 Hemagglutinin
by Tharakaraman, Kannan and Jayaraman, Akila and Raman, Rahul and Viswanathan, Karthik and Stebbins, Nathan W and Johnson, David and Shriver, Zachary and Sasisekharan, Ram and Sasisekharan, V
Cell, ISSN 0092-8674, 06/2013, Volume 153, Issue 7, pp. 1486 - 1493
The advent of H7N9 in early 2013 is of concern for a number of reasons, including its capability to infect humans, the lack of clarity in the etiology of... 
PATHOGENESIS | RESPIRATORY-TRACT | TRANSMISSION | BIOCHEMISTRY & MOLECULAR BIOLOGY | ADAPTATION | SITES | CELL BIOLOGY | Amino Acid Sequence | Hemagglutinin Glycoproteins, Influenza Virus - chemistry | Influenza A virus - chemistry | Influenza A virus - physiology | Receptors, Virus - metabolism | Humans | Influenza A virus - genetics | Models, Molecular | Molecular Sequence Data | Host Specificity | Phylogeny | Hemagglutinin Glycoproteins, Influenza Virus - metabolism | Trachea - virology | Hemagglutinin Glycoproteins, Influenza Virus - genetics | Polysaccharides - metabolism | Influenza Vaccines - immunology | Receptors, Virus - chemistry | Influenza, Human - virology | Mutation | Influenza A virus - classification | Lectins | Development and progression | Amino acids | Chemical properties | Analysis | Influenza
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11. Full Text Human Infection with a Triple-Reassortant Swine Influenza A(H1N1) Virus Containing the Hemagglutinin and Neuraminidase Genes of Seasonal Influenza Virus
by Nathalie Bastien and Nick A. Antonishyn and Ken Brandt and Christine E. Wong and Khami Chokani and Niki Vegh and Greg B. Horsman and Shaun Tyler and Morag R. Graham and Frank A. Plummer and Paul N. Levett and Yan Li
The Journal of Infectious Diseases, ISSN 0022-1899, 4/2010, Volume 201, Issue 8, pp. 1178 - 1182
A reassortant influenza A(H1N1) virus of swine origin distinct from the pandemic H1N1 2009 strain was isolated from 3 patients, all of whom worked at the same... 
H1N1 subtype influenza A virus | Pandemics | Disease transmission | Influenza A virus | Swine | Medical genetics | Viruses | Orthomyxoviridae | Infections | Human genetics | PIGS | INFECTIOUS DISEASES | CANADA | A VIRUSES | MICROBIOLOGY | IMMUNOLOGY | H1N1 | Reassortant Viruses - pathogenicity | Orthomyxoviridae Infections - veterinary | Saskatchewan - epidemiology | Humans | Molecular Sequence Data | Neuraminidase - genetics | Reassortant Viruses - genetics | Male | Phylogeny | Reverse Transcriptase Polymerase Chain Reaction | Hemagglutinin Glycoproteins, Influenza Virus - genetics | Animals | Base Sequence | Adult | Female | Influenza, Human - virology | Influenza A Virus, H1N1 Subtype - genetics | Orthomyxoviridae Infections - virology | Swine - virology | Polymerase chain reaction | Usage | Agglutinins | Swine influenza | Development and progression | Genetic aspects | Research
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12. Full Text Membrane fusion by single influenza hemagglutinin trimers: Kinetic evidence from image analysis of hemagglutinin-reconstituted vesicles
by Imai, Masaki and Mizuno, Takafumi and Kawasaki, Kazunori
Journal of Biological Chemistry, ISSN 0021-9258, 05/2006, Volume 281, Issue 18, pp. 12729 - 12735
Influenza hemagglutinin, the receptor-binding and membrane fusion protein of the virus, is a prototypic model for studies of biological membrane fusion in... 
VIRAL ENVELOPE PROTEIN | SURFACE-DENSITY | FLUORESCENCE | BIOCHEMISTRY & MOLECULAR BIOLOGY | PORE | VIRUS HEMAGGLUTININ | GLYCOPROTEIN | RECEPTOR-BINDING | CELL-FUSION | INITIAL-STAGES | Cell Line | Hemagglutinin Glycoproteins, Influenza Virus - chemistry | Membrane Fusion | Humans | Erythrocyte Membrane - metabolism | Microscopy, Electron | Animals | Time Factors | Models, Biological | Dogs | Protein Binding | Fluorescent Dyes - pharmacology | Kinetics | Rhodamines - chemistry | Binding Sites | Dimerization
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13. Full Text Evolution of the receptor binding properties of the influenza A(H3N2) hemagglutinin
by Yi Pu Lin and Xiaoli Xiong and Stephen A. Wharton and Stephen R. Martin and Peter J. Coombs and Sebastien G. Vachieri and Evangelos Christodoulou and Philip A. Walker and Junfeng Liu and John J. Skehel and Steven J. Gamblin and Alan J. Hay and Rodney S. Daniels and John W. McCauley
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 12/2012, Volume 109, Issue 52, pp. 21474 - 21479
The hemagglutinin (HA) of influenza A(H3N2) virus responsible for the 1968 influenza pandemic derived from an avian virus. On introduction into humans, its... 
Medical research | Receptors | Hydrogen bonds | Cell lines | Erythrocytes | Viruses | Orthomyxoviridae | Viral morphology | Infections | H3N2 subtype influenza A virus | A VIRUS | MDCK CELLS | EMBRYONATED CHICKEN EGGS | H3N2 VIRUSES | SPECIFICITY | RECOGNITION | VARIANTS | MULTIDISCIPLINARY SCIENCES | AMINO-ACID SUBSTITUTIONS | MONOCLONAL-ANTIBODY | CRYSTALLOGRAPHY | Hemagglutinin Glycoproteins, Influenza Virus - chemistry | Receptors, Virus - metabolism | Humans | Protein Multimerization | Influenza A Virus, H3N2 Subtype - metabolism | Models, Molecular | Static Electricity | Hemagglutinin Glycoproteins, Influenza Virus - metabolism | N-Acetylneuraminic Acid - metabolism | Hemagglutinin Glycoproteins, Influenza Virus - genetics | Animals | Madin Darby Canine Kidney Cells | Protein Binding | Binding Sites | Evolution, Molecular | Interferometry | Influenza viruses | Development and progression | Properties | Influenza | Natural history | Index Medicus | Biological Sciences
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14. Full Text Technology transfer and scale-up of the Flublok® recombinant hemagglutinin (HA) influenza vaccine manufacturing process
by Buckland, Barry and Boulanger, Robert and Fino, Mireli and Srivastava, Indresh and Holtz, Kathy and Khramtsov, Nikolai and McPherson, Clifton and Meghrous, Jamal and Kubera, Paul and Cox, Manon M.J
Vaccine, ISSN 0264-410X, 2014, Volume 32, Issue 42, pp. 5496 - 5502
Highlights • Successful fivefold scale-up to 2500 L scale of first FDA licensed recombinant influenza vaccine. • FDA licensed process is reproducible for a... 
Allergy and Immunology | Recombinant HA | Pandemic | Flublok | H7N9 | Insect cell | Influenza vaccine | Scale-up | MEDICINE, RESEARCH & EXPERIMENTAL | INFECTIONS | VIRUS | Flublok (R) | IMMUNOLOGY | Cell Line | Animals | Baculoviridae | Recombinant Proteins - immunology | Bioreactors | Hemagglutinin Glycoproteins, Influenza Virus - biosynthesis | Insecta - cytology | Influenza Vaccines - chemistry | Hemagglutinin Glycoproteins, Influenza Virus - isolation & purification | Influenza A Virus, H7N9 Subtype | Technology Transfer | Vaccines, Synthetic - chemistry | Proteins | Antigens | Hepatitis | Gas flow | Influenza | Mortality | Vaccines | Mutation | FDA approval | Eggs | Methods
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