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#27396155   2016/07/11 Save this To Up

[Preparation and Identification of High Immunogenic A/PR/8/34 Maternal Strain HA Protein for Influenza Virus Classical Reassortment].

Preparation of maternal strain A/PR/8/34 HA antiserum for influenza virus classical reassortment. A/PR/8/34 virus was digested by bromelain after inactivation and purification. 5%-20% sucrose continuous density gradient centrifugation method was used to purify HA protein. SIRD method was used to select the target protein. SDS-PAGE method was used to identified HA protein. High Immunogenic A/PR/8/34 HA protein was successfully prepared and HI titer reached 10240. High purity HA antiserum was identified by SIRD method. The key reagent in the classical reassortment of influenza virus was prepared, and the complete set of technical methods were explored, which laid the foundation for the independent research and development of seasonal influenza vaccine strains of China.

1981 related Products with: [Preparation and Identification of High Immunogenic A/PR/8/34 Maternal Strain HA Protein for Influenza Virus Classical Reassortment].

Native Influenza HA (A Br Native Influenza HA (A Br Native Influenza HA (A Br Native Influenza HA (A Ca Native Influenza HA (A Ca Native Influenza HA (A Ca Recombinant Influenza HA Recombinant Influenza HA Recombinant Influenza HA Native Influenza HA (B Fl Native Influenza HA (B Fl Native Influenza HA (B Fl

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#26799790   2016/01/22 Save this To Up

Platform technology to generate broadly cross-reactive antibodies to α-helical epitopes in hemagglutinin proteins from influenza a viruses.

We have utilized a de novo designed two-stranded α-helical coiled-coil template to display conserved α-helical epitopes from the stem region of hemagglutinin (HA) glycoproteins of influenza A. The immunogens have all the surface-exposed residues of the native α-helix in the native HA protein of interest displayed on the surface of the two-stranded α-helical coiled-coil template. This template when used as an immunogen elicits polyclonal antibodies which bind to the α-helix in the native protein. We investigated the highly conserved sequence region 421-476 of HA by inserting 21 or 28 residue sequences from this region into our template. The cross-reactivity of the resulting rabbit polyclonal antibodies prepared to these immunogens was determined using a series of HA proteins from H1N1, H2N2, H3N2, H5N1, H7N7 and H7N9 virus strains which are representative of Group 1 and Group 2 virus subtypes of influenza A. Antibodies from region 449-476 were Group 1 specific. Antibodies to region 421-448 showed the greatest degree of cross-reactivity to Group 1 and Group 2 and suggested that this region has a great potential as a "universal" synthetic peptide vaccine for influenza A. This article is protected by copyright. All rights reserved.

1608 related Products with: Platform technology to generate broadly cross-reactive antibodies to α-helical epitopes in hemagglutinin proteins from influenza a viruses.

Native Influenza HA (A To Native Influenza HA (A To Native Influenza HA (A To Goat Anti-Human TOM1L1 SR Influenza B (B Tokio 53 9 Influenza A H5N1 (Avian) Influenza A H5N1 (Avian) Influenza A H5N1 (Avian) Rabbit Anti-Human Toll In Shiga Toxin 1 antibody, M Shiga Toxin 2 antibody, M Cholera toxin antibody, M

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#25746201   2015/08/11 Save this To Up

Vector optimization and needle-free intradermal application of a broadly protective polyvalent influenza A DNA vaccine for pigs and humans.

The threat posed by the 2009 pandemic H1N1 virus emphasized the need for new influenza A virus vaccines inducing a broad cross-protective immune response for use in both humans and pigs. An effective and broad influenza vaccine for pigs would greatly benefit the pork industry and contribute to public health by diminishing the risk of emerging highly pathogenic reassortants. Current inactivated protein vaccines against swine influenza produce only short-lived immunity and have no efficacy against heterologous strains. DNA vaccines are a potential alternative with advantages such as the induction of cellular and humoral immunity, inherent safety and rapid production time. We have previously developed a DNA vaccine encoding selected influenza proteins of pandemic origin and demonstrated broad protective immune responses in ferrets and pigs. In this study, we evaluated our DNA vaccine expressed by next-generation vectors. These new vectors can improve gene expression, but they are also efficiently produced on large scales and comply with regulatory guidelines by avoiding antibiotic resistance genes. In addition, a new needle-free delivery of the vaccine, convenient for mass vaccinations, was compared with intradermal needle injection followed by electroporation. We report that when our DNA vaccine is expressed by the new vectors and delivered to the skin with the needle-free device in the rabbit model, it can elicit an antibody response with the same titers as a conventional vector with intradermal electroporation. The needle-free delivery is already in use for traditional protein vaccines in pigs but should be considered as a practical alternative for the mass administration of broadly protective influenza DNA vaccines.

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MOUSE ANTI BOVINE ROTAVIR Androgen Receptor (Phosph Androgen Receptor (Phosph Rabbit Anti-Human Androge Rabbit Anti-Human Androge Androgen Receptor (Ab 650 DNAI2 antibody Source Rab DNAJB2 antibody Source Ra DNAJC7 antibody Source Ra succinate-CoA ligase, GDP DNAJA2 antibody Source Ra DNA ligase 3 antibody Sou

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#25716614   2015/05/08 Save this To Up

Predicting peptide vaccine candidates against H1N1 influenza virus through theoretical approaches.

Identification of potential epitopes that might activate the immune system has been facilitated by the employment of algorithms that use experimental data as templates. However, in order to prove the affinity and the map of interactions between the receptor (major histocompatibility complex, MHC, or T-cell receptor) and the potential epitope, further computational studies are required. Docking and molecular dynamics (MDs) simulations have been an effective source of generating structural information at molecular level in immunology. Herein, in order to provide a detailed understanding of the origins of epitope recognition and to select the best peptide candidate to develop an epitope-based vaccine, docking and MDs simulations in combination with MMGBSA free energy calculations and per-residue free energy decomposition were performed, taking as starting complexes those formed between four designed epitopes (P1-P4) from hemagglutinin (HA) of the H1N1 influenza virus and MHC-II anchored in POPC membrane. Our results revealed that the energetic contributions of individual amino acids within the pMHC-II complexes are mainly dictated by van der Waals interactions and the nonpolar part of solvation energy, whereas the electrostatic interactions corresponding to hydrogen bonds and salt bridges determine the binding specificity, being the most favorable interactions formed between p4 and MHC-II. Then, P1-P4 epitopes were synthesized and tested experimentally to compare theoretical and experimental results. Experimental results show that P4 elicited the highest strong humoral immune response to HA of the H1N1 and may induce antibodies that are cross-reactive to other influenza subtypes, suggesting that it could be a good candidate for the development of a peptide-based vaccine.

1516 related Products with: Predicting peptide vaccine candidates against H1N1 influenza virus through theoretical approaches.

Influenza A Virus Hemaggl Goat Anti-Influenza A Vir Rabbit Anti-Influenza-A H Rabbit Anti-Influenza-A H Rabbit Anti-Influenza-A H Mouse Anti-Influenza-A HA Mouse Anti-Influenza-A HA Mouse Anti-Influenza-A HA Recombinant Influenza B V Recombinant Influenza B V Recombinant Influenza B V Native Influenza A Virus

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#24216235   2013/12/30 Save this To Up

High-yield soluble expression of recombinant influenza virus antigens from Escherichia coli and their potential uses in diagnosis.

Although antiviral drugs and vaccines have been successful for mitigating influenza virus infections, the lack of general technical platform for the timely supply of soluble and highly purified influenza viral antigens presents a serious bottleneck for the subsequent analysis for the effective control of the viral disease. Using the Escherichia coli (E. coli) lysyl tRNA synthetase (LysRS) as a novel fusion partner, this study reports the soluble expression of influenza viral proteins in E. coli host, construction of antibody library against the virus, and detection of anti-influenza antibodies using the expressed viral antigens. When influenza A and B viral proteins were fused with the LysRS, the fusion proteins were expressed predominantly as soluble forms and their production yields were high enough to be amenable to immunization protocols in rabbits for antibody generation. The produced antibodies showed high level binding specificity against the respective viral proteins, with cross-reactivity across heterologous viruses within the same type of influenza viruses. In addition, LysRS-HA fusion protein could bind specifically to anti-HA antibodies in the virus-infected mouse serum in widely accepted two detection methods, Western blot and ELISA. These results present a convenient tool for the production of antibodies specific to the virus as well as the rapid detection of influenza viral infections, ultimately contributing to the control of influenza viruses including highly pathogenic H5N1, pandemic H1N1, or the recent H7N9 influenza viruses.

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Recombinant Hemagglutinin Recombinant Influenza B V Recombinant Influenza B V Recombinant Influenza B V Recombinant Influenza A V Recombinant Influenza A V Recombinant Influenza A V Recombinant Influenza A V Recombinant Influenza A V Recombinant Influenza A V Recombinant Viral Antige RANK Ligand Soluble, Huma

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#23884239   2013/12/30 Save this To Up

Cross reactivity of serum antibody responses elicited by DNA vaccines expressing HA antigens from H1N1 subtype influenza vaccines in the past 30 years.

In the past three decades, ten H1 subtype influenza vaccines have been recommended for global seasonal flu vaccination. Some of them were used only for one year before being replaced by another H1 flu vaccine while others may be used for up to seven years. While the selection of a new seasonal flu vaccine was based on the escape of a new emerging virus that was not effectively protected by the existing flu formulation, there is limited information on the magnitude and breadth of cross reactivity among H1 subtype virus circulation over a long period. In the current study, HA-expressing DNA vaccines were constructed to express individual HA antigens from H1 subtype vaccines used in the past 30 y. Rabbits naïve to HA antibody responses were immunized with these HA DNA vaccines and the cross reactivity of these sera against HA antigen and related H1 viruses in the same period was studied. Our data indicate that the level of cross reactivity was different for different viral isolates and the key mutations responsible for the cross reactivity may involve only a limited number of residues. Our results provide useful information for the development of improved seasonal vaccines than can achieve broad protection against viruses within the same H1 subtype.

1653 related Products with: Cross reactivity of serum antibody responses elicited by DNA vaccines expressing HA antigens from H1N1 subtype influenza vaccines in the past 30 years.

Rabbit Anti-Influenza-A H Rabbit Anti-Influenza-A H Rabbit Anti-Influenza-A H Mouse Anti-Influenza-A HA Mouse Anti-Influenza-A HA Mouse Anti-Influenza-A HA Primary antibody DRAK1 A Primary antibody DRAK2 A HA (Influenza A Virus Hem FDA Standard Frozen Tissu FDA Standard Frozen Tissu FDA Standard Frozen Tissu

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#23661027   2013/05/10 Save this To Up

Antigenically intact hemagglutinin in circulating avian and swine influenza viruses and potential for H3N2 pandemic.

The 2009 swine-origin H1N1 influenza, though antigenically novel to the population at the time, was antigenically similar to the 1918 H1N1 pandemic influenza, and consequently was considered to be "archived" in the swine species before reemerging in humans. Given that the H3N2 is another subtype that currently circulates in the human population and is high on WHO pandemic preparedness list, we assessed the likelihood of reemergence of H3N2 from a non-human host. Using HA sequence features relevant to immune recognition, receptor binding and transmission we have identified several recent H3 strains in avian and swine that present hallmarks of a reemerging virus. IgG polyclonal raised in rabbit with recent seasonal vaccine H3 fail to recognize these swine H3 strains suggesting that existing vaccines may not be effective in protecting against these strains. Vaccine strategies can mitigate risks associated with a potential H3N2 pandemic in humans.

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Mouse Anti-Influenza-A He Mouse Anti-Influenza-A He Native Influenza A Virus Native Influenza A Virus Native Influenza A Virus Recombinant Influenza A V Recombinant Influenza A V Recombinant Influenza A V Recombinant Influenza A V Recombinant Influenza A V Recombinant Influenza A V Polyclonal Rabbit Anti In

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#22796139   2012/08/13 Save this To Up

Development of VAX128, a recombinant hemagglutinin (HA) influenza-flagellin fusion vaccine with improved safety and immune response.

We evaluated the safety and immunogenicity profiles of 3 novel influenza vaccine constructs consisting of the globular head of the HA1 domain of the Novel H1N1 genetically fused to the TLR5 ligand, flagellin. HA1 was fused to the C-terminus of flagellin in VAX128A, replaced the D3 domain of flagellin in VAX128B and was fused in both positions in VAX128C.

2673 related Products with: Development of VAX128, a recombinant hemagglutinin (HA) influenza-flagellin fusion vaccine with improved safety and immune response.

HA (Influenza A Virus Hem Recombinant Hemagglutinin Influenza A H5N1 (Avian) Influenza A H5N1 (Avian) Influenza A H5N1 (Avian) Mouse Anti-Influenza A He Rabbit Anti-Influenza A H Rabbit Anti-Influenza-A H Rabbit Anti-Influenza-A H Rabbit Anti-Influenza-A H Mouse Anti-Influenza-A HA Mouse Anti-Influenza-A HA

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#22126628   2012/01/05 Save this To Up

Yeast expressed recombinant Hemagglutinin protein of novel H1N1 elicits neutralising antibodies in rabbits and mice.

Currently available vaccines for the pandemic Influenza A (H1N1) 2009 produced in chicken eggs have serious impediments viz limited availability, risk of allergic reactions and the possible selection of sub-populations differing from the naturally occurring virus, whereas the cell culture derived vaccines are time consuming and may not meet the demands of rapid global vaccination required to combat the present/future pandemic. Hemagglutinin (HA) based subunit vaccine for H1N1 requires the HA protein in glycosylated form, which is impossible with the commonly used bacterial expression platform. Additionally, bacterial derived protein requires extensive purification and refolding steps for vaccine applications. For these reasons an alternative heterologous system for rapid, easy and economical production of Hemagglutinin protein in its glycosylated form is required. The HA gene of novel H1N1 A/California/04/2009 was engineered for expression in Pichia pastoris as a soluble secreted protein. The full length HA- synthetic gene having α-secretory tag was integrated into P. pastoris genome through homologous recombination. The resultant Pichia clones having multiple copy integrants of the transgene expressed full length HA protein in the culture supernatant. The Recombinant yeast derived H1N1 HA protein elicited neutralising antibodies both in mice and rabbits. The sera from immunised animals also exhibited Hemagglutination Inhibition (HI) activity. Considering the safety, reliability and also economic potential of Pichia expression platform, our preliminary data indicates the feasibility of using this system as an alternative for large-scale production of recombinant influenza HA protein in the face of influenza pandemic threat.

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Recombinant Human Insulin Recombinant Human Insulin Recombinant Human Insulin Recombinant Influenza HA Bone Morphogenetic Protei Rabbit Anti-Influenza-A H Rabbit Anti-Influenza-A H Rabbit Anti-Influenza-A H Mouse Anti-Influenza-A HA Mouse Anti-Influenza-A HA Mouse Anti-Influenza-A HA Recombinant Yeast ATP sul

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#22022458   2011/10/24 Save this To Up

Minor changes in the hemagglutinin of influenza A(H1N1)2009 virus alter its antigenic properties.

The influenza A(H1N1)2009 virus has been the dominant type of influenza A virus in Finland during the 2009-2010 and 2010-2011 epidemic seasons. We analyzed the antigenic characteristics of several influenza A(H1N1)2009 viruses isolated during the two influenza seasons by analyzing the amino acid sequences of the hemagglutinin (HA), modeling the amino acid changes in the HA structure and measuring antibody responses induced by natural infection or influenza vaccination.

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Recombinant Influenza B V Recombinant Influenza B V Recombinant Influenza B V Native Influenza A Virus Native Influenza A Virus Native Influenza A Virus Recombinant Influenza A V Recombinant Influenza A V Recombinant Influenza A V Recombinant Influenza A V Recombinant Influenza A V Recombinant Influenza A V

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