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Influenza

Influenza

Influenza is an acute, highly communicable viral disease that affects the respiratory tract and is responsible for seasonal epidemics worldwide. Influenza A is the most prevalent type associated with widespread outbreaks and is subtyped based on two surface glycoproteins: hemagglutinin (H) and neuraminidase (N), as in H1N1. These glycoproteins are essential for viral infectivity, transmission, and immune recognition. Transmission occurs primarily through respiratory droplets and contaminated...

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Mechanism of a decrease in potency for the recombinant influenza A virus hemagglutinin H3 antigen during storage.

John M Hickey¹, Kathleen M Holtz, Prakash Manikwar

¹Department of Pharmaceutical Chemistry, Macromolecule and Vaccine Stabilization Center, University of Kansas, Lawrence, Kansas, 66047.

Journal of Pharmaceutical Sciences

|January 16, 2014

Summary

The recombinant hemagglutinin (rHA) influenza vaccine Flublok experienced a significant potency loss upon storage. This loss was linked to disulfide-mediated cross-linking and reduced free thiols in the rHA antigen.

Keywords:

Flublok®influenza mass spectrometry physicochemical potency protein formulation recombinant hemagglutinin single-radial immunodiffusion assay stability vaccines

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Area of Science:

Vaccinology
Protein Biochemistry
Biophysical Chemistry

Background:

Flublok®, a recombinant hemagglutinin (rHA)-based influenza vaccine, offers an alternative to traditional egg-derived vaccines.
This vaccine contains threefold higher hemagglutinin content compared to standard inactivated influenza vaccines.

Purpose of the Study:

To investigate the causes and mechanisms behind the observed in vitro potency loss of rHA.
To evaluate the biophysical and chemical stability of rHA under various formulations and storage conditions.

Main Methods:

Characterization of rHA protein antigen.
Assessment of higher order structure and hydrodynamic size.
Measurement of free thiol content and disulfide-linked multimer formation.

Main Results:

A rapid loss of in vitro potency (∼50%) was observed in rHA after 1 month of storage.
Potency loss did not correlate with changes in higher order structure or hydrodynamic size.
Disulfide-mediated cross-linking, forming non-native multimers, correlated with potency loss.

Conclusions:

The primary mechanism for early potency loss in rHA is likely disulfide-mediated cross-linking.
Loss of free thiol content, especially in C-terminal cysteine residues, is associated with decreased SRID potency.