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Open AccessJournal ArticleDOI

Influenza virus hemagglutinin stalk-based antibodies and vaccines.

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TLDR
Broadly protective vaccine candidates based on the epitopes of these antibodies, for example, chimeric and headless hemagglutinin structures, are under development and show promising results in animals models, and could be developed into universal influenza virus vaccines that protect from infection with drifted seasonal as well as novel pandemic influenza virus strains therefore obviating the need for annual vaccination, and enhancing pandemic preparedness.
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This article is published in Current Opinion in Virology.The article was published on 2013-10-01 and is currently open access. It has received 301 citations till now. The article focuses on the topics: Influenza A virus & H5N1 genetic structure.

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Citations
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Recombinant hemagglutinin influenza vaccine provides broader spectrum protection

TL;DR: These data suggest that the rHA proteins produced in Lepidopteran cells offer broader-spectrum protection and result in clinical benefit, and may be achieved with immunity directed at more conserved viral antigens.
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Sustainable vaccine development: a vaccine manufacturer's perspective

TL;DR: This work states that vaccine development can be fast-tracked through strengthening international collaborations, and the continuous innovation of technologies to accelerate their design, development, and manufacturing, but these processes should be supported by a balanced project portfolio, and by managing sustainable vaccine procurement strategies for different types of markets.
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Accurate measurement of the effects of all amino-acid mutations to influenza hemagglutinin

TL;DR: The authors' measurements confirm that antigenic sites on the globular head of hemagglutinin are highly tolerant of mutations, but other regions – including stalk epitopes targeted by broadly neutralizing antibodies – have a limited capacity to evolve.
References
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Journal ArticleDOI

Antibody Recognition of a Highly Conserved Influenza Virus Epitope

TL;DR: TheCR6261 epitope identified here should accelerate the design and implementation of improved vaccines that can elicit CR6261-like antibodies, as well as antibody-based therapies for the treatment of influenza.
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Structural and Functional Bases for Broad-Spectrum Neutralization of Avian and Human Influenza A Viruses

TL;DR: The crystal structure of one such nAb bound to H5 shows that it blocks infection by inserting its heavy chain into a conserved pocket in the stem region, thus preventing membrane fusion, and suggests that nAb-based immunotherapy is a promising strategy for broad-spectrum protection against seasonal and pandemic influenza viruses.
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Rapid cloning of high-affinity human monoclonal antibodies against influenza virus

TL;DR: The panel of influenza-virus-specific human mAbs allowed us to address the issue of original antigenic sin (OAS): the phenomenon where the induced antibody shows higher affinity to a previously encountered influenza virus strain compared with the virus strain present in the vaccine.
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