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           Search results for: HA (Influenza A Virus Hemagglutinin) Antibody   

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#29049310   2017/10/19 Save this To Up

Molecular epidemiology of influenza B virus among hospitalized pediatric patients in Northern Italy during the 2015-16 season.

The influenza B viruses belong to two lineages distinguished by their genetic and antigenic characteristics, which are referred to as the Yamagata and Victoria lineages, designated after their original isolates, B/Yamagata/16/88 and B/Victoria/2/87. The primary aim of this study was to evaluate the molecular characteristics of influenza B viruses circulating in a region of Northern Italy, Lombardia, during the influenza season of 2015-2016.

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Influenza A Virus Hemaggl Recombinant Hemagglutinin Human Epstein-Barr Virus Mouse Epstein-Barr Virus Native Influenza HA (A Br Native Influenza HA (A Br Native Influenza HA (A Br Native Influenza HA (A Be Native Influenza HA (A Be Native Influenza HA (A Be Recombinant Influenza B V Recombinant Influenza B V

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#29046433   2017/10/19 Save this To Up

A multimechanistic antibody targeting the receptor binding site potently cross-protects against influenza B viruses.

Influenza B virus causes considerable disease burden worldwide annually, highlighting the limitations of current influenza vaccines and antiviral drugs. In recent years, broadly neutralizing antibodies (bnAbs) against hemagglutinin (HA) have emerged as a new approach for combating influenza. We describe the generation and characterization of a chimeric monoclonal antibody, C12G6, that cross-neutralizes representative viruses spanning the 76 years of influenza B antigenic evolution since 1940, including viruses belonging to the Yamagata, Victoria, and earlier lineages. Notably, C12G6 exhibits broad cross-lineage hemagglutination inhibition activity against influenza B viruses and has higher potency and breadth of neutralization when compared to four previously reported influenza B bnAbs. In vivo, C12G6 confers stronger cross-protection against Yamagata and Victoria lineages of influenza B viruses in mice and ferrets than other bnAbs or the anti-influenza drug oseltamivir and has an additive antiviral effect when administered in combination with oseltamivir. Epitope mapping indicated that C12G6 targets a conserved epitope that overlaps with the receptor binding site in the HA region of influenza B virus, indicating why it neutralizes virus so potently. Mechanistic analyses revealed that C12G6 inhibits influenza B viruses via multiple mechanisms, including preventing viral entry, egress, and HA-mediated membrane fusion and triggering antibody-dependent cell-mediated cytotoxicity and complement-dependent cytotoxicity responses. C12G6 is therefore a promising candidate for the development of prophylactics or therapeutics against influenza B infection and may inform the design of a truly universal influenza vaccine.

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ribosome binding protein ribosome binding protein IL-12 Receptor beta2 anti calcium binding protein P Cortisol Binding Globulin SH3 domain-binding protei Guanylate-binding protein amyloid beta precursor pr Retinoid X Receptor beta TGF beta Receptor III ant zona pellucida binding pr RNA binding motif protein

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#29042201   2017/10/18 Save this To Up

Newcastle disease virus (NDV) recombinant expressing the hemagglutinin of H7N9 avian influenza virus protects chickens against NDV and highly pathogenic avian influenza A (H7N9) virus challenges.

The emerged highly pathogenic avian influenza A (H7N9) (HPAI) viruses in China pose a dual challenge to public health and poultry industry. Thus H7N9 vaccines are in an urgent need. In this study, we constructed a Newcastle disease virus (NDV)-vectored vaccine (rLXHAF) expressing the hemagglutinin (HA) of H7N9 virus fused with the transmembrane/cytoplasmic tail domain of the NDV fusion protein. rLXHAF stably expressed the HA protein, exhibited similar growth kinetics and pathogenicity as the parental virus. rLXHAF induced positive NDV-specific hemagglutination inhibition (HI), virus neutralization (VN) and total IgY antibodies and completely protected chickens from NDV challenge. Unexpectedly, rLXHAF elicited undetectable HI and VN titers but high overall IgY antibody titers against H7N9 measured by ELISA. The vaccine provided 80% protection against HPAI H7N9 challenge. Virus shedding of NDV and H7N9 challenge strains was reduced. Our results suggest that rLXHAF is immunogenic and efficacious against HPAI H7N9 virus in chickens.

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Avian Influenza virus (H7 Recombinant Hemagglutinin Mouse Anti-Newcastle Dise Avian Influenza virus H5N Avian Influenza Virus H5N Avian Influenza virus H5N Avian Influenza virus H5N Recombinant Influenza B V Recombinant Influenza B V Recombinant Influenza B V Recombinant Influenza A V Recombinant Influenza A V

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#29024492   2017/10/12 Save this To Up

Experimental infection of clade 1.1.2 (H5N1), clade 2.3.2.1c (H5N1) and clade 2.3.4.4 (H5N6) highly pathogenic avian influenza viruses in dogs.

Since the emergence of highly pathogenic avian influenza (HPAI) H5N1 in Asia, the haemagglutinin (HA) gene of this virus lineage has continued to evolve in avian populations, and H5N1 lineage viruses now circulate concurrently worldwide. Dogs may act as an intermediate host, increasing the potential for zoonotic transmission of influenza viruses. Virus transmission and pathologic changes in HPAI clade 1.1.2 (H5N1)-, 2.3.2.1c (H5N1)- and 2.3.4.4 (H5N6)-infected dogs were investigated. Mild respiratory signs and antibody response were shown in dogs intranasally infected with the viruses. Lung histopathology showed lesions that were associated with moderate interstitial pneumonia in the infected dogs. In this study, HPAI H5N6 virus replication in dogs was demonstrated for the first time. Dogs have been suspected as a "mixing vessel" for reassortments between avian and human influenza viruses to occur. The replication of these three subtypes of the H5 lineage of HPAI viruses in dogs suggests that dogs could serve as intermediate hosts for avian-human influenza virus reassortment if they are also co-infected with human influenza viruses.

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Avian Influenza virus H5N Avian Influenza Virus H5N Avian Influenza virus H5N Avian Influenza virus H5N Influenza A H5N1 (Avian F Influenza A H5N1 (Avian) Influenza A H5N1 (Avian) Influenza A H5N1 (Avian) Influenza A H5N1 (Avian) Mouse Anti-Influenza-A HA Mouse Anti-Influenza-A HA Mouse Anti-Influenza-A HA

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#29021304   2017/10/12 Save this To Up

Kinetics, longevity and cross-reactivity of anti-neuraminidase antibody after natural infection with influenza A viruses.

The kinetics, longevity and breadth of antibodies to influenza neuraminidase (NA) in archival, sequential serum/plasma samples from influenza A virus (IAV) H5N1 survivors, and from patients infected with the 2009 pandemic IAV (H1N1) virus were determined using an enzyme linked lectin based assay. The reverse genetics-derived H4N1 viruses harboring an hemagglutinin (HA) segment from A/duck/Shan Tou/461/2000 (H4N9) and an NA segment derived from either IAV H5N1 clade 1, IAV H5N1 clade 2.3.4, the 2009 pandemic IAV (H1N1) (H1Npdm) or A/Puerto Rico/8/1934 (H1N1) virus were used as the test antigens. These sera/plasma samples were also investigated by microneutralization (MN) and/or hemagglutination-inhibition (HI) assays. Neuraminidase-inhibiting (NI) antibodies against N1 NA of both homologous and heterologous viruses were observed in H5N1 survivors and H1N1pdm patients. H5N1 survivors who never exposed to H1N1pdm virus developed NI antibodies to H1N1pdm NA. Seroconversion of NI antibodies was observed in 65% of the H1N1pdm patients at day 7 after disease onset, but an increase in titer was not observed in late serum samples. On the other hand, an increase in seroconversion rate with HI assay was observed in the follow-up series of sera obtained on days 7, 14, 28 and 90 after infection. The study also showed that NI antibodies are broadly reactive, while MN and HI antibodies are more strain specific.

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#29018438   2017/10/11 Save this To Up

Antibody Immunity Induced by H7N9 Avian Influenza Vaccines: Evaluation Criteria, Affecting Factors, and Implications for Rational Vaccine Design.

Severe H7N9 avian influenza virus (AIV) infections in humans have public health authorities around the world on high alert for the potential development of a human influenza pandemic. Currently, the newly-emerged highly pathogenic avian influenza A (H7N9) virus poses a dual challenge for public health and poultry industry. Numerous H7N9 vaccine candidates have been generated using various platforms. Immunization trials in animals and humans showed that H7N9 vaccines are apparently poorly immunogenic because they induced low hemagglutination inhibition and virus neutralizing antibody titers. However, H7N9 vaccines elicit comparable levels of total hemagglutinin (HA)-reactive IgG antibody as the seasonal influenza vaccines, suggesting H7N9 vaccines are as immunogenic as their seasonal counterparts. A large fraction of overall IgG antibody is non-neutralizing antibody and they target unrecognized epitopes outside of the traditional antigenic sites in HA. Further, the Treg epitope identified in H7 HA may at least partially contribute to regulation of antibody immunity. Here, we review the latest advances for the development of H7N9 vaccines and discuss the influence of serological criteria on evaluation of immunogenicity of H7N9 vaccines. Next, we discuss factors affecting antibody immunity induced by H7N9 vaccines, including the change in antigenic epitopes in HA and the presence of the Treg epitope. Last, we present our perspectives for the unique features of antibody immunity of H7N9 vaccines and propose some future directions to improve or modify antibody response induced by H7N9 vaccines. This perspective would provide critical implications for rational design of H7N9 vaccines for human and veterinary use.

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#28986672   2017/10/07 Save this To Up

High accumulation in tobacco seeds of hemagglutinin antigen from avian (H5N1) influenza.

Tobacco seeds can be used as a cost effective system for production of recombinant vaccines. Avian influenza is an important respiratory pathogen that causes a high degree of mortality and becomes a serious threat for the poultry industry. A safe vaccine against avian flu produced at low cost could help to prevent future outbreaks. We have genetically engineered tobacco plants to express extracellular domain of hemagglutinin protein from H5N1 avian influenza virus as an inexpensive alternative for production purposes. Two regulatory sequences of seed storage protein genes from Phaseolus vulgaris L. were used to direct the expression, yielding 3.0 mg of the viral antigen per g of seeds. The production and stability of seed-produced recombinant HA protein was characterized by different molecular techniques. The aqueous extract of tobacco seed proteins was used for subcutaneous immunization of chickens, which developed antibodies that inhibited the agglutination of erythrocytes after the second application of the antigen. The feasibility of using tobacco seeds as a vaccine carrier is discussed.

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Influenza A H5N1 (Avian) Influenza A H5N1 (Avian) Influenza A H5N1 (Avian) Influenza A H5N1 (Avian F Recombinant Hemagglutinin Influenza A H5N1 (Avian) Avian Influenza virus H5N Avian Influenza Virus H5N Avian Influenza virus H5N Avian Influenza virus H5N Mouse Anti-Influenza A He Rabbit Anti-Influenza A H

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#28978710   2017/10/05 Save this To Up

COBRA HA elicits hemagglutination-inhibition antibodies against a panel of H3N2 influenza virus co-circulating variants.

Each influenza season, a set of wild-type viruses, representing one H1N1, one H3N2, 1-2 influenza B isolates, are selected for inclusion in the annual seasonal influenza vaccine. In order to develop broadly reactive subtype specific influenza vaccines, a methodology called computationally optimized broadly reactive antigens (COBRA) was used to design novel hemagglutinin (HA) vaccine immunogens. COBRA technology was effectively used to design HA immunogens that elicited antibodies that neutralized H5N1 and H1N1 isolates. In this report, the development and characterization of seventeen prototype H3N2 COBRA HA proteins were screened in mice and ferrets for the elicitation of antibodies with HAI activity against human seasonal H3N2 viruses that were isolated over the last 48 years. The most effective COBRA HA vaccine regimens elicited antibodies with broader HAI activity against a panel of H3N2 viruses compared to wild-type H3 HA vaccines. The top leading COBRA HA candidates were tested against co-circulating variants. These variants were not efficiently detected by antibodies elicited by the wild-type HA from viruses selected as the vaccine candidates. The T-11 COBRA HA vaccine elicited antibodies with HAI and neutralization activity against all co-circulating variants from 2004-2007. This is the first report demonstrating broader breadth of vaccine induced antibodies against co-circulating H3N2 strains compared to the wild-type HA antigens that were represented in commercial influenza vaccines.IMPORTANCE There is a need for an improved influenza vaccine that elicits immune responses that recognize a broader number of influenza virus strains to prevent infection and transmission. Using the COBRA approach, a set of vaccines against influenza viruses in the H3N2 subtype were tested for the ability to elicit antibodies that neutralize virus infection against not only historical vaccine strains of H3N2, but also a set of co-circulating variants that circulated between 2004-2007. Three of the H3N2 COBRA vaccines recognized all the co-circulating strains during this era, but the chosen wild-type vaccine strains were not able to elicit antibodies with HAI activity against these co-ciruclating strains. Therefore, the COBRA vaccines have the ability to not only elicit protective antibodies against the dominant vaccine strains, but also minor circulating strains that can evolve into the dominant vaccine strains in the future.

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#28971971   2017/10/03 Save this To Up

Potent peptidic fusion inhibitors of influenza virus.

Influenza therapeutics with new targets and mechanisms of action are urgently needed to combat potential new pandemics, emerging viruses, and constantly mutating circulating strains. We report here on design and structural characterization of potent peptidic inhibitors against influenza hemagglutinin (HA). The peptide design was based on complementarity determining region (CDR) loops of anti-HA human broadly neutralizing antibodies, FI6v3 and CR9114. The optimized peptides exhibit nanomolar affinity and neutralization against group 1 influenza A viruses including the 2009 H1N1 pandemic and avian H5N1 strains. The peptide inhibitors bind to the highly conserved stem epitope and block the low pH-induced conformational rearrangements associated with membrane fusion. These peptidic compounds and their advantageous biological properties should accelerate development of novel small molecule and peptide-based therapeutics against influenza virus.

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#28966056   2017/10/02 Save this To Up

A Potent Germline-like Human Monoclonal Antibody Targets a pH-Sensitive Epitope on H7N9 Influenza Hemagglutinin.

The H7N9 influenza virus causes high-mortality disease in humans but no effective therapeutics are available. Here we report a human monoclonal antibody, m826, that binds to H7 hemagglutinin (HA) and protects against H7N9 infection. m826 binds to H7N9 HA with subnanomolar affinity at acidic pH and 10-fold lower affinity at neutral pH. The high-resolution (1.9 Å) crystal structure of m826 complexed with H7N9 HA indicates that m826 binds an epitope that may be fully exposed upon pH-induced conformational changes in HA. m826 fully protects mice against lethal challenge with H7N9 virus through mechanisms likely involving antibody-dependent cell-mediated cytotoxicity. Interestingly, immunogenetic analysis indicates that m826 is a germline antibody, and m826-like sequences can be identified in H7N9-infected patients, healthy adults, and newborn babies. These m826 properties offer a template for H7N9 vaccine immunogens, a promising candidate therapeutic, and a tool for exploring mechanisms of virus infection inhibition by antibodies.

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