Recently, researchers at the NIH have been able to target neuraminidase (NAs) on influenza with two monoclonal antibodies 1G01 and DA03E17.
NA proteins contain a globular head and a narrow stalk portion. They are responsible for cleaving sialic acids from glycoproteins and glycolipids to allow the release of progeny virus from host cells.
The antibodies were isolated from the blood of two people who had recovered from H3N2. The antibodies were found to inhibit the propagation of both H3N2, a predominant subtype of the virus, and H2N2, a variant. Researchers used cryogenic electron microscopes to visualize and analyze the structure of the antibodies.
The antibodies target the NA’s catalytic site with an extended complementarity determining the H3 loop, and effectively inhibiting all NA subtypes of influenza A B.
This method might prove more useful than regular vaccine methods as the underside of NA proteins are considered “conserved” regions of the influenza virus, regions that do not change based on mutations.
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