Bacterial HA1 vaccine against pandemic H5N1 influenza virus: evidence of oligomerization, hemagglutination, and cross-protective immunity in ferrets. - Test2 - elhamkhani - TriplyDB

Bacterial HA1 vaccine against pandemic H5N1 influenza virus: evidence of oligomerization, hemagglutination, and cross-protective immunity in ferrets.

Bacterial HA1 vaccine against pandemic H5N1 influenza virus: evidence of oligomerization, hemagglutination, and cross-protective immunity in ferrets.

http://www.wikidata.org/entity/Q30396343

about

Purification and immunogenicity of hemagglutinin from highly pathogenic avian influenza virus H5N1 expressed in Nicotiana benthamiana.Clinical vaccine development for H5N1 influenza.Comparative analysis of antibody induction and protection against influenza virus infection by DNA immunization with HA, HAe, and HA1 in mice.Single-dose monomeric HA subunit vaccine generates full protection from influenza challenge.A live attenuated influenza A(H5N1) vaccine induces long-term immunity in the absence of a primary antibody response.Oral priming with replicating adenovirus serotype 4 followed by subunit H5N1 vaccine boost promotes antibody affinity maturation and expands H5N1 cross-clade neutralization.A novel hemagglutinin protein produced in bacteria protects chickens against H5N1 highly pathogenic avian influenza viruses by inducing H5 subtype-specific neutralizing antibodies Expression of HA1 antigen of H5N1 influenza virus as a potent candidate for vaccine in bacterial system.MF59 adjuvant enhances diversity and affinity of antibody-mediated immune response to pandemic influenza vaccines.Recombinant HA1 produced in E. coli forms functional oligomers and generates strain-specific SRID potency antibodies for pandemic influenza vaccines H5N1 virus-like particle vaccine elicits cross-reactive neutralizing antibodies that preferentially bind to the oligomeric form of influenza virus hemagglutinin in humans.Vaccination with drifted variants of avian H5 hemagglutinin protein elicits a broadened antibody response that is protective against challenge with homologous or drifted live H5 influenza virus.Decreased serologic response in vaccinated military recruits during 2011 correspond to genetic drift in concurrent circulating pandemic A/H1N1 viruses.Oligomeric recombinant H5 HA1 vaccine produced in bacteria protects ferrets from homologous and heterologous wild-type H5N1 influenza challenge and controls viral loads better than subunit H5N1 vaccine by eliciting high-affinity antibodies.Different immunity elicited by recombinant H5N1 hemagglutinin proteins containing pauci-mannose, high-mannose, or complex type N-glycans Antigenic and immunogenic properties of recombinant hemagglutinin proteins from H1N1 A/Brisbane/59/07 and B/Florida/04/06 when produced in various protein expression systems.Recombinant trimeric HA protein immunogenicity of H5N1 avian influenza viruses and their combined use with inactivated or adenovirus vaccines.A carboxy-terminal trimerization domain stabilizes conformational epitopes on the stalk domain of soluble recombinant hemagglutinin substrates.DNA priming prior to inactivated influenza A(H5N1) vaccination expands the antibody epitope repertoire and increases affinity maturation in a boost-interval-dependent manner in adults Nonglycosylated G-Protein Vaccine Protects against Homologous and Heterologous Respiratory Syncytial Virus (RSV) Challenge, while Glycosylated G Enhances RSV Lung Pathology and Cytokine Levels.Receptor-binding domains of spike proteins of emerging or re-emerging viruses as targets for development of antiviral vaccines.Development of a universal CTL-based vaccine for influenza.Influenza vaccines: from whole virus preparations to recombinant protein technology.Evaluation of Epic® label-free technology to quantify functional recombinant hemagglutinin Development of a simple, rapid, sensitive, high-throughput luciferase reporter based microneutralization test for measurement of virus neutralizing antibodies following Respiratory Syncytial Virus vaccination and infection.A nonfusogenic antigen mimic of influenza hemagglutinin glycoproteins constituted with soluble full-length HA1 and truncated HA2 proteins expressed in E. coli.ELPylated haemagglutinins produced in tobacco plants induce potentially neutralizing antibodies against H5N1 viruses in mice.Harnessing an RNA-mediated chaperone for the assembly of influenza hemagglutinin in an immunologically relevant conformation.Immunoprotective effects of a hemin-binding peptide derived from hemagglutinin-2 against infection with Porphyromonas gingivalis.How can we develop universal H5N1 vaccines.AS03-adjuvanted H5N1 vaccine promotes antibody diversity and affinity maturation, NAI titers, cross-clade H5N1 neutralization, but not H1N1 cross-subtype neutralization Oligomerization of bacterially expressed H1N1 recombinant hemagglutinin contributes to protection against viral challenge

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Bacterial HA1 vaccine against pandemic H5N1 influenza virus: evidence of oligomerization, hemagglutination, and cross-protective immunity in ferrets.

http://www.wikidata.org/entity/Q30396343

description

2010 nî lūn-bûn

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2010 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

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2010年の論文

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Bacterial HA1 vaccine against ...... rotective immunity in ferrets.

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Corey J Crevar

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Donald M Carter

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Hana Golding

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Jody Manischewitz

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Lisa R King

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Nitin Verma

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Surender Khurana

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Swati Verma

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Ted M Ross

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Human and avian influenza viruses target different cells in the lower respiratory tract of humans and other mammals

Structure of the uncleaved human H1 hemagglutinin from the extinct 1918 influenza virus

Structure, Receptor Binding, and Antigenicity of Influenza Virus Hemagglutinins from the 1957 H2N2 Pandemic

Structural Basis of Preexisting Immunity to the 2009 H1N1 Pandemic Influenza Virus

Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 A resolution

Solvation energy in protein folding and binding

An influenza A/H1N1/2009 hemagglutinin vaccine produced in Escherichia coli

Safety and immunogenicity of a recombinant hemagglutinin vaccine for H5 influenza in humans.

Expression and purification of an influenza hemagglutinin--one step closer to a recombinant protein-based influenza vaccine.

Glycan microarray analysis of the hemagglutinins from modern and pandemic influenza viruses reveals different receptor specificities.

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1246-1256

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10.1128/JVI.02107-10

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3

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85

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