2019
DOI: 10.1016/j.csbj.2019.03.009
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Structural Insights for Anti-Influenza Vaccine Design

Abstract: Influenza A virus are a persistent and significant threat to human health, and current vaccines do not provide sufficient protection due to antigenic drift, which allows influenza viruses to easily escape immune surveillance and antiviral drug activity. Influenza hemagglutinin (HA) is a glycoprotein needed for the entry of enveloped influenza viruses into host cells and is a potential target for anti-influenza humoral immune responses. In recent years, a number of broadly neutralizing antibodies (bnAbs) have b… Show more

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Cited by 8 publications
(6 citation statements)
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“…It can be hypothesized that immunogenic epitopes on the head domain of these rare HA subtypes are not under strong immune pressure in their natural avian reservoir and are unlikely to undergo genetic changes due to this pressure, but are more likely to be influenced by stochastic effects that conserve antigenic site sequences [92,93]. This results in the preservation of important antigenic epitopes such as the membrane-distal receptor-binding site (RBS) on the HA head containing key highly conserved amino acids involved in receptor binding [94][95][96][97] and can partially explain cross-subtype neutralization seen in our vaccination results. Nevertheless, our pseudotype library has enabled us to test immune responses brought about by vaccination against a variety of IAV and IBV pseudotypes.…”
Section: Discussionmentioning
confidence: 99%
“…It can be hypothesized that immunogenic epitopes on the head domain of these rare HA subtypes are not under strong immune pressure in their natural avian reservoir and are unlikely to undergo genetic changes due to this pressure, but are more likely to be influenced by stochastic effects that conserve antigenic site sequences [92,93]. This results in the preservation of important antigenic epitopes such as the membrane-distal receptor-binding site (RBS) on the HA head containing key highly conserved amino acids involved in receptor binding [94][95][96][97] and can partially explain cross-subtype neutralization seen in our vaccination results. Nevertheless, our pseudotype library has enabled us to test immune responses brought about by vaccination against a variety of IAV and IBV pseudotypes.…”
Section: Discussionmentioning
confidence: 99%
“…How to expose highly cross-protective epitopes to the immune system has been investigated using glycan engineering of HA and NA proteins [68]. Researchers have also devised chimeric HAs by transferring unique HA globular head domains from exotic novel strains to the HA stalk domains of presently circulating human influenza viruses [71]. Moreover, adenoviruses have been transformed into vaccine vectors by disabling genes responsible for their replication, exhibiting the potential for developing a "universal" flu vaccine.…”
Section: Novel Approaches To Vaccine Designmentioning
confidence: 99%
“…The HA head domain is highly variable among IAV strains and is immunologically dominant by harboring the receptor binding sites [125]. The stalk domain of HA that is relatively conserved between different subtypes of IAV and elicits stalk specific antibodies is key for the development of a universal influenza vaccine (UIV).…”
Section: Universal Influenza Vaccine Approachesmentioning
confidence: 99%