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Comment
. 2023 Jul 5;31(7):1865-1867.
doi: 10.1016/j.ymthe.2023.04.014. Epub 2023 May 17.

Always a bridesmaid, never a bride: Committing to flu neuraminidase as a vaccine target

Cosette Schneider  1 , Lynda Coughlan  2
Affiliations
Comment

Always a bridesmaid, never a bride: Committing to flu neuraminidase as a vaccine target

Cosette Schneider et al. Mol Ther. .
No abstract available

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Conflict of interest statement

Declaration of interests The authors do not have any interests to disclose.

Figures

Figure 1
Figure 1
Mechanisms of action of NA-specific antibodies (A) Current influenza virus vaccine development is focused on trimeric hemagglutinin (HA), the major viral surface glycoprotein important for virus binding to the viral entry receptor, sialic acid (SA). However, tetrameric neuraminidase (NA), the second viral surface glycoprotein, important for releasing virus from SA through its sialidase activity, is reemerging as a potential target. (B) Anti-NA Abs act to antagonize the virus by (1) blocking NA-mediated enzymatic cleavage of virus from mucins in the airway, (2) indirectly blocking HA binding to SA through steric hindrance, (3) acting synergistically with HA stalk Abs to activate FcγR effector functions, such as antibody-dependent cellular cytotoxicity (ADCC), and (4) blocking NA enzymatic activity at the point of viral egress to prevent cleavage of viral aggregates or inhibit viral release and onward spread within the host. Figure created with BioRender.com.
Figure 2
Figure 2
Novel dimeric NA-based APC-targeting DNA vaccine elicits protective anti-NA antibodies in vivo Vaccine DNA plasmids were engineered as three-component fusion constructs encoding (1) an APC-targeting unit (svFv-MHC II), (2) a dimerization unit containing either the acid or base (A/B) component of a modified Jun/Fos leucine zipper motif, and (3) a dimeric antigen unit encoding the ectodomain of N1 from H1N1 virus A/Puerto Rico/8/34/Mount Sinai. Following immunization of mice, in vivo expression and dimerization of A/B-fused NA targeted to MHC II resulted in the induction of NA-based, Ab-mediated protection against homologous virus through a mechanism considered to enhance B cell receptor (BCR) cross-linking. Figure created with BioRender.com.
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