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1. Full Text Structural Basis of Preexisting Immunity to the 2009 H1N1 Pandemic Influenza Virus
by Rui Xu and Damian C. Ekiert and Jens C. Krause and Rong Hai and James E. Crowe and Ian A. Wilson
Science, ISSN 0036-8075, 4/2010, Volume 328, Issue 5976, pp. 357 - 360
The 2009 H1N1 swine flu is the first influenza pandemic in decades. The crystal structure of the hemagglutinin from the A/California/04/2009 H1N1 virus shows... 
H1N1 subtype influenza A virus | Polysaccharides | Pandemics | Vaccination | Antibodies | Viruses | Reports | Viral morphology | Epitopes | Immunity | Crystal structure | ORIGIN | HEMAGGLUTININ | EMERGENCE | MULTIDISCIPLINARY SCIENCES | RECEPTOR-BINDING | Influenza A Virus, H1N1 Subtype - immunology | Age Factors | Humans | Molecular Sequence Data | Crystallography, X-Ray | Hemagglutinin Glycoproteins, Influenza Virus - immunology | Antibodies, Neutralizing - immunology | Disease Outbreaks | Influenza, Human - virology | Amino Acid Sequence | Hemagglutinin Glycoproteins, Influenza Virus - chemistry | Antigenic Variation | Models, Molecular | Influenza, Human - epidemiology | Glycosylation | Hemagglutinins, Viral - immunology | Cross Reactions | Hemagglutinins, Viral - chemistry | Influenza Vaccines - immunology | Antibodies, Neutralizing - chemistry | Immunoglobulin Fab Fragments - chemistry | Antibodies, Viral - chemistry | Antibodies, Viral - immunology | Protein Conformation | Immunoglobulin Fab Fragments - immunology | Influenza, Human - immunology | Usage | Swine influenza | Crystals | Natural immunity | Genetic aspects | Research | Structure | Epidemiologic methods | International aspects | Immunology | Swine flu | Crystallography
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2. Full Text A non-VH1-69 heterosubtypic neutralizing human monoclonal antibody protects mice against H1N1 and H5N1 viruses
by de Marco, Donata and Clementi, Nicola and Mancini, Nicasio and Solforosi, Laura and Moreno, Guisella J and Sun, Xiangjie and Tumpey, Terrence M and Gubareva, Larisa V and Mishin, Vasiliy and Clementi, Massimo and Burioni, Roberto
PLoS ONE, ISSN 1932-6203, 04/2012, Volume 7, Issue 4, p. e34415
Influenza viruses are among the most important human pathogens and are responsible for annual epidemics and sporadic, potentially devastating pandemics. The... 
IMMUNIZATION | INFLUENZA-A | EPITOPE | HEMAGGLUTININ | MULTIDISCIPLINARY SCIENCES | RESISTANCE | IDENTIFICATION | STRAIN | OSELTAMIVIR | Influenza A Virus, H1N1 Subtype - immunology | Orthomyxoviridae Infections - prevention & control | Humans | Molecular Sequence Data | Antibodies, Monoclonal - therapeutic use | Neutralization Tests | Influenza A Virus, H5N1 Subtype - genetics | Hemagglutinin Glycoproteins, Influenza Virus - immunology | Hemagglutinins - immunology | Epitopes - immunology | Hemagglutinins - metabolism | Influenza Vaccines - therapeutic use | Female | Influenza A Virus, H1N1 Subtype - genetics | Antibodies, Monoclonal - immunology | Amino Acid Sequence | Hemagglutinin Glycoproteins, Influenza Virus - chemistry | Epitopes - genetics | Mutation - genetics | Hemagglutinin Glycoproteins, Influenza Virus - metabolism | Hemagglutinins - genetics | Sequence Homology, Amino Acid | Animals | Influenza Vaccines - immunology | Mutagenesis | Influenza A Virus, H5N1 Subtype - immunology | Antibodies, Viral - immunology | Protein Conformation | Mice | Mice, Inbred BALB C | Orthomyxoviridae Infections - virology | Orthomyxoviridae Infections - immunology | Virus diseases | Avian influenza | Antiviral agents | Epidemics | Lectins | Avian influenza viruses | Monoclonal antibodies | Vaccines | Antigenic determinants | Pandemics | Laboratories | Prophylaxis | Viruses | Infections | Drug resistance | Avian flu | Immunosuppressive agents | Proteins | Hepatitis | Older people | Hemagglutinins | Immune system | Immunization | Immunoglobulins | Immune response | Glycoprotein | Disease control | Immune response (humoral) | Virology | Disease prevention | Influenza | Respiratory diseases | Mutation | Human behavior
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3. Full Text Airborne Transmission of Influenza A/H5N1 Virus Between Ferrets
by Sander Herfst and Eefje J. A. Schrauwen and Martin Linster and Salin Chutinimitkul and Emmie de Wit and Vincent J. Munster and Erin M. Sorrell and Theo M. Bestebroer and David F. Burke and Derek J. Smith and Guus F. Rimmelzwaan and Albert D. M. E. Osterhaus and Ron A. M. Fouchier
Science, ISSN 0036-8075, 6/2012, Volume 336, Issue 6088, pp. 1534 - 1541
Highly pathogenic avian influenza A/H5N1 virus can cause morbidity and mortality in humans but thus far has not acquired the ability to be transmitted by... 
Receptors | Inoculation | Experimental infection | Disease transmission | Pandemics | REPORTS | Viruses | Orthomyxoviridae | Ferrets | Genetic mutation | Amino acid substitution | A VIRUS | TO-PERSON TRANSMISSION | MEDIATED SELECTION | H5N1 VIRUS | HEMAGGLUTININ | MULTIDISCIPLINARY SCIENCES | HOST | INFECTION | MODEL | RECEPTOR SPECIFICITY | PATHOGENIC AVIAN INFLUENZA | Immune Sera | Reassortant Viruses - pathogenicity | Influenza A Virus, H5N1 Subtype - physiology | Poultry | Receptors, Virus - metabolism | Air Microbiology | Humans | Virulence | Molecular Sequence Data | Influenza A Virus, H5N1 Subtype - genetics | Virus Shedding | Hemagglutinin Glycoproteins, Influenza Virus - immunology | Hemagglutinin Glycoproteins, Influenza Virus - genetics | Respiratory System - virology | Female | Influenza, Human - virology | Oseltamivir - pharmacology | Disease Models, Animal | Hemagglutinin Glycoproteins, Influenza Virus - chemistry | Reverse Genetics | Antiviral Agents - pharmacology | Mutagenesis, Site-Directed | RNA Replicase - genetics | Viral Proteins - chemistry | Sialic Acids - metabolism | Viral Proteins - genetics | Influenza, Human - epidemiology | Containment of Biohazards | Influenza A Virus, H5N1 Subtype - drug effects | Influenza in Birds - epidemiology | Influenza, Human - transmission | Hemagglutinin Glycoproteins, Influenza Virus - metabolism | Animals | Orthomyxoviridae Infections - transmission | Virus Replication | RNA Replicase - chemistry | Influenza in Birds - virology | Influenza A Virus, H5N1 Subtype - pathogenicity | Mutation | Serial Passage | Orthomyxoviridae Infections - virology | Amino Acid Substitution | Avian influenza | Diseases and pests | Physiological aspects | Development and progression | Research | Animal diseases | Amino acids | Avian flu | Small mammals | Index Medicus | Polymerase | Human | Proteins | Influenza | Droplets | Genetic modification
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4. Full Text An Influenza A/H1N1/2009 hemagglutinin vaccine produced in Escherichia coli
by Aguilar-Yáñez, José M and Portillo-Lara, Roberto and Mendoza-Ochoa, Gonzalo I and García-Echauri, Sergio A and López-Pacheco, Felipe and Bulnes-Abundis, David and Salgado-Gallegos, Johari and Lara-Mayorga, Itzel M and Webb-Vargas, Yenny and León-Angel, Felipe O and Rivero-Aranda, Ramón E and Oropeza-Almazán, Yuriana and Ruiz-Palacios, Guillermo M and Zertuche-Guerra, Manuel I and DuBois, Rebecca M and White, Stephen W and Schultz-Cherry, Stacey and Russell, Charles J and Alvarez, Mario M
PLoS ONE, ISSN 1932-6203, 2010, Volume 5, Issue 7, p. e11694
Background: The A/H1N1/2009 influenza pandemic made evident the need for faster and higher-yield methods for the production of influenza vaccines. Platforms... 
PATHOGENESIS | H5N1 VIRUS | ANTIGENIC STRUCTURE | MULTIDISCIPLINARY SCIENCES | ANTIBODY | VIRUS HEMAGGLUTININ | CELL CULTURE | SIZE-DISTRIBUTION ANALYSIS | PROTEINS | EXPRESSION | RECEPTOR-BINDING | Influenza A Virus, H1N1 Subtype - immunology | Hemagglutinins, Viral - metabolism | Enzyme-Linked Immunosorbent Assay | Humans | Ferrets | Reverse Transcriptase Polymerase Chain Reaction | Antibodies, Viral - blood | Hemagglutinins, Viral - immunology | Influenza Vaccines - metabolism | Protein Folding | Animals | Hemagglutinins, Viral - chemistry | Influenza Vaccines - genetics | Escherichia coli - genetics | Escherichia coli - metabolism | Antibodies, Viral - immunology | Influenza A Virus, H1N1 Subtype - genetics | Influenza vaccines | Epidemics | Immune response | Analysis | Influenza | Escherichia coli | Lectins | Recombinant proteins | Cell culture | Pandemics | Guillain-Barre syndrome | Antibodies | Viruses | Biochemistry | Ultracentrifugation | Vaccines | Avian flu | Eggs | Proteins | E coli | Hemagglutinins | Bacteria | HA protein | Sedimentation & deposition | Recombinant | Antigens | Effectiveness | Glycosylation | Children & youth | Infectious diseases | Immunogenicity | Insects | Swine flu | Production methods | Insect cells
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5. Full Text A Highly Conserved Neutralizing Epitope on Group 2 Influenza A Viruses
by Damian C. Ekiert and Robert H. E. Friesen and Gira Bhabha and Ted Kwaks and Mandy Jongeneelen and Wenli Yu and Carla Ophorst and Freek Cox and Hans J.W.M. Korse and Boerries Brandenburg and Ronald Vogels and Just P.J. Brakenhoff and Ronald Kompier and Martin H. Koldijk and Lisette A.H.M. Cornelissen and Leo L. M. Poon and Malik Peiris and Wouter Koudstaal and Ian A. Wilson and Jaap Goudsmit
Science, ISSN 0036-8075, 8/2011, Volume 333, Issue 6044, pp. 843 - 850
Current flu vaccines provide only limited coverage against seasonal strains of influenza viruses. The identification of V H 1-69 antibodies that broadly... 
Influenza A virus | RESEARCH ARTICLES | Vaccination | Cardiopulmonary resuscitation | Antibodies | Viruses | Orthomyxoviridae | Infections | Epitopes | H3N2 subtype influenza A virus | Crystal structure | FUSION | HEMAGGLUTININ | RECOGNITION | AVIAN INFLUENZA | SUBTYPES | MULTIDISCIPLINARY SCIENCES | VACCINATION | MONOCLONAL-ANTIBODIES | PEPTIDE | SEASON | Orthomyxoviridae Infections - prevention & control | Antibody Specificity | Humans | Molecular Sequence Data | Antigens, Viral - genetics | Crystallography, X-Ray | Neutralization Tests | Hemagglutinin Glycoproteins, Influenza Virus - immunology | Hemagglutinin Glycoproteins, Influenza Virus - genetics | Epitopes - immunology | Antibodies, Neutralizing - immunology | Conserved Sequence | Influenza A Virus, H7N7 Subtype - immunology | Influenza A virus - immunology | Influenza, Human - therapy | Antibodies, Monoclonal - immunology | Amino Acid Sequence | Hemagglutinin Glycoproteins, Influenza Virus - chemistry | Models, Molecular | Antigens, Viral - chemistry | Antibodies, Monoclonal - isolation & purification | Influenza A Virus, H3N2 Subtype - immunology | Antibodies, Viral - isolation & purification | Antibodies, Neutralizing - isolation & purification | Antigens, Viral - immunology | Animals | Influenza Vaccines - immunology | Antibodies, Viral - immunology | Protein Conformation | Mice | Influenza A Virus, H7N7 Subtype - genetics | Mutation | Binding Sites, Antibody | Influenza, Human - prevention & control | Orthomyxoviridae Infections - immunology | Influenza, Human - immunology | Influenza viruses | Influenza vaccines | Crystals | Monoclonal antibodies | Physiological aspects | Research | Properties | Structure | Vaccines | Influenza | Public health | Virology | fusion | peptide | avian influenza | hemagglutinin | recognition | monoclonal-antibodies | season | vaccination | subtypes
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6. Full Text A recommended numbering scheme for influenza A HA subtypes
by Burke, David F and Burke, David F and Smith, Derek J and Smith, Derek J
PloS one, ISSN 1932-6203, 2014, Volume 9, Issue 11, p. e112302
Comparisons of residues between sub-types of influenza virus is increasingly used to assess the zoonotic potential of a circulating strain and for comparative... 
AMINO-ACID | TRANSMISSION | EVOLUTION | SPECIFICITY | MULTIDISCIPLINARY SCIENCES | HUMAN-TYPE RECEPTOR | FERRETS | VIRUS HEMAGGLUTININ | HEMAGGLUTININ PROTEIN | CLEAVAGE | BINDING | Hemagglutinins - metabolism | Amino Acid Sequence | Hemagglutinins - classification | Phenotype | Sequence Alignment | Influenza A virus - metabolism | Influenza, Human - pathology | Hemagglutinins - chemistry | Humans | Molecular Sequence Data | Influenza, Human - virology | Amino acids | Influenza | Analysis | Pathogens | Pandemics | Viruses | Vaccines | Pathogenicity | Equivalence | Comparative studies | Influenza A | Numbering schemes | Strains (organisms) | Binding sites
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7. Full Text Assessment of Influenza Virus Hemagglutinin Stalk-Based Immunity in Ferrets
by Florian Krammer and Rong Hai and Mark Yondola and Gene S. Tan and Victor H. Leyva-Grado and Alex B. Ryder and Matthew S. Miller and John K. Rose and Peter Palese and Adolfo García-Sastre and Randy A. Albrecht
Journal of Virology, ISSN 0022-538X, 03/2014, Volume 88, Issue 6, pp. 3432 - 3442
Classifications Services JVI Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit... 
A VIRUS | ANTIBODIES | NEURAMINIDASE | PROTECTIVE IMMUNITY | HUMAN INFECTION | VIROLOGY | OSELTAMIVIR-RESISTANT | SEASONAL INFLUENZA | H3N2 VIRUS | VACCINIA VIRUS | H1N1 | Influenza A Virus, H1N1 Subtype - immunology | Protein Structure, Tertiary | Hemagglutinin Glycoproteins, Influenza Virus - chemistry | Influenza Vaccines - administration & dosage | Hemagglutinin Glycoproteins, Influenza Virus - administration & dosage | Humans | Male | Hemagglutinin Glycoproteins, Influenza Virus - immunology | Ferrets | Hemagglutinin Glycoproteins, Influenza Virus - genetics | Antibodies, Neutralizing - immunology | Animals | Influenza Vaccines - immunology | Influenza Vaccines - genetics | Influenza Vaccines - chemistry | Hemagglutinins | Antibodies, Viral - immunology | Influenza, Human - virology | Influenza A Virus, H1N1 Subtype - genetics | Influenza, Human - prevention & control | Disease Models, Animal | Influenza, Human - immunology | Vaccines and Antiviral Agents
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8. Full Text The Stabilities of the Soluble Ectodomain and Fusion Peptide Hairpins of the Influenza Virus Hemagglutinin Subunit II Protein Are Positively Correlated with Membrane Fusion
by Ranaweera, Ahinsa and Ratnayake, Punsisi U and Weliky, David P
Biochemistry, ISSN 0006-2960, 09/2018, Volume 57, Issue 37, pp. 5480 - 5493
Cellular entry of influenza virus is mediated by the viral protein hemagglutinin (HA), which forms an initial complex of three HA1 and three HA2 subunits. Each... 
SOLID-STATE NMR | A-VIRUSES | HA SUBUNIT | BIOCHEMISTRY & MOLECULAR BIOLOGY | HEMIFUSION PHENOTYPE | NEUTRAL PH | TRANSMEMBRANE DOMAIN | ELECTRON-MICROSCOPY | PORE FORMATION | COILED-COIL | GP41 ECTODOMAIN | Hemagglutinins - metabolism | Amino Acid Sequence | Hemagglutinin Glycoproteins, Influenza Virus - chemistry | Protein Subunits | Hemagglutinins, Viral - metabolism | Hemagglutinins, Viral - chemistry | Humans | Protein Domains | Protein Conformation | Hemagglutinin Glycoproteins, Influenza Virus - metabolism | Virus Internalization
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9. Full Text Influenza hemagglutinin stem-fragment immunogen elicits broadly neutralizing antibodies and confers heterologous protection
by Vamsee V. A. Mallajosyula and Michael Citron and Francesca Ferrara and Xianghan Lu and Cheryl Callahan and Gwendolyn J. Heidecker and Siddhartha P. Sarma and Jessica A. Flynn and Nigel J. Temperton and Xiaoping Liang and Raghavan Varadarajan
Proceedings of the National Academy of Sciences, ISSN 0027-8424, 06/2014, Volume 111, Issue 25, pp. E2514 - E2523
Influenza hemagglutinin (HA) is the primary target of the humoral response during infection/vaccination. Current influenza vaccines typically fail to... 
Cross-protection | Stabilization | Pandemic preparedness | Escherichia coli | Hemagglutinin stalk | DESIGN | PROTEIN | stabilization | RECOGNITION | STALK DOMAIN | MULTIDISCIPLINARY SCIENCES | ESCHERICHIA-COLI | VIRUS HEMAGGLUTININ | MONOCLONAL-ANTIBODY | GP120 | GLOBULAR HEAD | hemagglutinin stalk | RECEPTOR-BINDING SITE | cross-protection | pandemic preparedness | Influenza A Virus, H1N1 Subtype - immunology | Orthomyxoviridae Infections - prevention & control | Protein Structure, Tertiary | Hemagglutinin Glycoproteins, Influenza Virus - chemistry | Hemagglutinin Glycoproteins, Influenza Virus - immunology | Hemagglutinin Glycoproteins, Influenza Virus - genetics | Orthomyxoviridae Infections - genetics | Cross Reactions | Antibodies, Neutralizing - immunology | Animals | Antibodies, Viral - immunology | Female | Influenza A Virus, H1N1 Subtype - chemistry | Mice, Inbred BALB C | Influenza A Virus, H1N1 Subtype - genetics | Orthomyxoviridae Infections - immunology | Biological Sciences | PNAS Plus
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10. Full Text A stable trimeric influenza hemagglutinin stem as a broadly protective immunogen
by Impagliazzo, Antonietta and Milder, Fin and Kuipers, Harmjan and Wagner, Michelle V and Zhu, Xueyong and Hoffman, Ryan M. B and van Meersbergen, Ruud and Huizingh, Jeroen and Wanningen, Patrick and Verspuij, Johan and de Man, Martijn and Ding, Zhaoqing and Apetri, Aian and Kükrer, Başak and Sneekes-Vriese, Eveline and Tomkiewicz, Danuta and Laursen, Nick S and Lee, Peter S and Zakrzewska, Anna and Dekking, Liesbeth and Tolboom, Jeroen and Tettero, Lisanne and van Meerten, Sander and Yu, Wenli and Koudstaal, Wouter and Goudsmit, Jaap and Ward, Anew B and Meijberg, Wim and Wilson, Ian A and Radošević, Katarina
Science, ISSN 0036-8075, 2015, Volume 349, Issue 6254, pp. 1301 - 1306
The identification of human broadly neutralizing antibodies (bnAbs) targeting the hemagglutinin (HA) stem revitalized hopes of developing a universal influenza... 
CELLS | DESIGN | NEUTRALIZING ANTIBODIES | EPITOPE | STALK DOMAIN | A VIRUSES | MULTIDISCIPLINARY SCIENCES | VACCINE | THERAPEUTIC ANTIBODIES | VIRUS HEMAGGLUTININ | GLOBULAR HEAD | Influenza A Virus, H1N1 Subtype - immunology | Hemagglutinin Glycoproteins, Influenza Virus - chemistry | Protein Structure, Secondary | Humans | Protein Multimerization | Hemagglutinin Glycoproteins, Influenza Virus - immunology | Antibodies, Neutralizing - immunology | Animals | Influenza Vaccines - immunology | Influenza A Virus, H5N1 Subtype - immunology | Antibodies, Viral - immunology | Mice | Influenza, Human - prevention & control | Lectins | Antigens | Influenza | Viral antibodies | Influenza viruses | Antibodies | Health aspects | Proteins | Vaccines | Mutation | Binding | Design engineering | Primates | Viruses
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11. Full Text Contemporary H3N2 influenza viruses have a glycosylation site that alters binding of antibodies elicited by egg-adapted vaccine strains
by Zost, Seth J and Parkhouse, Kaela and Gumina, Megan E and Kim, Kangchon and Perez, Sebastian Diaz and Wilson, Patrick C and Treanor, John J and Sant, Andrea J and Cobey, Sarah and Hensley, Scott E
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 11/2017, Volume 114, Issue 47, pp. 12578 - 12583
H3N2 viruses continuously acquire mutations in the hemagglutinin (HA) glycoprotein that abrogate binding of human antibodies. During the 2014-2015 influenza... 
Vaccine | Antibody | Hemagglutinin | Influenza |