Vaccine Technologies Against Avian Influenza: Current Approaches and New Directions

Ross, Kathleen A.; Lm, Huntimer; Je, Vela Ramirez; Adams, Alexandra; Sl, Carpenter; Ml, Kohut; Bronich, Tatiana K.; Webby, R; Legge, Kevin L.; Sk, Mallapragadal; Mj, Wannemuehler; Narasimhan, Balaji

doi:10.1166/jbn.2014.1983

Cited by 8 publications

(7 citation statements)

References 196 publications

(256 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The finding fortifies the notion that the H7N9 VLPs may serve as a compelling vaccine candidate in poultry farming, which typically employs inactivated or subunit vaccines for disease management [29–31]. …”

Section: Discussionmentioning

confidence: 78%

Multi-antigen avian influenza a (H7N9) virus-like particles: particulate characterizations and immunogenicity evaluation in murine and avian models

Liu

et al. 2017

BMC Biotechnol

View full text Add to dashboard Cite

BackgroundHuman infection with avian influenza A virus (H7N9) was first reported in China in March 2013. Since then, hundreds of cases have been confirmed showing severe symptoms with a high mortality rate. The virus was transmitted from avian species to humans and has spread to many neighboring areas, raising serious concerns over its pandemic potential. Towards containing the disease, the goal of this study is to prepare a virus-like particle (VLP) that consists of hemagglutinin (HA), neuraminidase (NA) and matrix protein 1 (M1) derived from the human isolate A/Taiwan/S02076/2013(H7N9) for potential vaccine development.ResultsFull length HA, NA, and M1 protein genes were cloned and expressed using a baculoviral expression system, and the VLPs were generated by co-infecting insect cells with three respective recombinant baculoviruses. Nanoparticle tracking analysis and transmission electron microscopy were applied to verify the VLPs’ structure and antigenicity, and the multiplicity of infection of the recombinant baculoviruses was adjusted to achieve the highest hemagglutination activity. In animal experiments, BALB/c mice and specific-pathogen-free chickens receiving the VLP immunization showed elevated hemagglutination inhibition serum titer and antibodies against NA and M1 proteins. In addition, examination of cellular immunity showed the VLP-immunized mice and chickens exhibited an increased splenic antigen-specific cytokines production.ConclusionsThe H7N9 VLPs possess desirable immunogenicity in vivo and may serve as a candidate for vaccine development against avian influenza A (H7N9) infection.Electronic supplementary materialThe online version of this article (doi:10.1186/s12896-016-0321-6) contains supplementary material, which is available to authorized users.

show abstract

Section: Discussionmentioning

confidence: 78%

Multi-antigen avian influenza a (H7N9) virus-like particles: particulate characterizations and immunogenicity evaluation in murine and avian models

Liu

et al. 2017

BMC Biotechnol

View full text Add to dashboard Cite

show abstract

“…Among them, H7N9 infection causes high numbers of severe human cases, causing serious damage to human health ( 23 ). Prophylactic vaccination against AIV helps in disease’s prevention in animals, and different vaccination strategies are often used to combat AIV infection ( 24 ). The selection of a broad-spectrum, effective vaccine that can be produced quickly and cost-effectively during a pandemic outbreak has become critical.…”

Section: Discussionmentioning

confidence: 99%

Immune Evaluation of Recombinant Lactobacillus plantarum With Surface Display of HA1-DCpep in Mice

et al. 2021

View full text Add to dashboard Cite

Avian influenza viruses can be efficiently transmitted through mucous membranes, and conventional vaccines are not effective in protecting against mucosal infection by influenza viruses. To induce multiple immune responses in an organism, we constructed a recombinant Lactobacillus plantarum expressing the influenza virus antigen HA1 with the adjuvant dendritic cell-targeting peptide (DCpep). The recombinant L. plantarum strains NC8Δ-pWCF-HA1 and NC8Δ-pWCF-HA1-DCpep were used to immunize mice via oral administration, and the humoral, cellular and mucosal immune responses were evaluated. In addition, the serum levels of specific antibodies and hemagglutination inhibition (HI) levels were also measured. Our results showed that recombinant L. plantarum activated dendritic cells in Peyer’s patches (PPs), increased the numbers of CD4+IFN-γ+ and CD8+IFN-γ+ cells in the spleen and mesenteric lymph nodes (MLNs), and affected the ability of CD4+ and CD8+ cells to proliferate in the spleen and MLNs. Additionally, recombinant L. plantarum increased the number of B220+IgA+ cells in PPs and the level of IgA in the lungs and different intestinal segments. In addition, specific IgG, IgG1 and IgG2a antibodies were induced at high levels in the mice serum, specific IgA antibodies were induced at high levels in the mice feces, and HI potency was significantly increased. Thus, the recombinant L. plantarum strains NC8Δ-pWCF-HA1 and NC8Δ-pWCF-HA1-DCpep have potential as vaccine candidates for avian influenza virus.

show abstract

“…The ordinary sickness can be quite taxing on the elderly, the very young, and others who are immunocompromised, all groups recommended to receive treatment. The development of flu vaccines has helped boost the immunity of the recipients, and the drug Oseltamivir , known as Tamiflu, has been developed. However, drug resistant strains have emerged .…”

Section: Background and Theorymentioning

confidence: 99%

Structure prediction and analysis of neuraminidase sequence variants

Thayer

2016

Biochem Molecular Bio Educ

View full text Add to dashboard Cite

Analyzing protein structure has become an integral aspect of understanding systems of biochemical import. The laboratory experiment endeavors to introduce protein folding to ascertain structures of proteins for which the structure is unavailable, as well as to critically evaluate the quality of the prediction obtained. The model system used is the highly mutable influenza virus protein neuraminidase, which is the key target in the development of therapeutics. In light of recent pandemics, understanding how mutations confer drug resistance, which translates at the molecular level to understanding how different sequence variants differ, constitutes an area of great interest because of the ramifications in public health. This lab targets upper level undergraduate biochemistry students, and aims to introduce tools to be used to explore protein folding and protein visualization in the context of the neuraminidase case study. Students proceed to critically evaluate the folded models by comparison with crystallographic structures. When validity is established, they fold a neuraminidase sequence for which a structure is not available. Through structural alignment and visual inspection of the 150 loop, students gain molecular insight into two possible conformations of the protein, which are actively being studied. Folding the third chosen sequence mimics a true research environment in allowing students to generate a structure from a sequence for which a structure was not previously available, and to assess whether their particular variant has an open or closed loop. From this vantage, they are then challenged to speculate about the connection between loop conformation and drug susceptibility. © 2016 by The International Union of Biochemistry and Molecular Biology, 44(4):361-376, 2016.

show abstract

Vaccine Technologies Against Avian Influenza: Current Approaches and New Directions

Cited by 8 publications

References 196 publications

Multi-antigen avian influenza a (H7N9) virus-like particles: particulate characterizations and immunogenicity evaluation in murine and avian models

Multi-antigen avian influenza a (H7N9) virus-like particles: particulate characterizations and immunogenicity evaluation in murine and avian models

Immune Evaluation of Recombinant Lactobacillus plantarum With Surface Display of HA1-DCpep in Mice

Structure prediction and analysis of neuraminidase sequence variants

Contact Info

Product

Resources

About