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Analytical technologies for influenza virus-like particle candidate vaccines: challenges and emerging approaches. Thompson, C.M. et al. Virology Journal 2013, 10:141.   PubMed




Playing hide and seek: how glycosylation of the influenza virus hemagglutinin can modulate the immune response to infection. Tate, M.D. et al. Viruses 2014, 6, 1294-1316.   PubMed



Lectin-affinity chromatography for downstream processing of MDCK cell culture derived human influenza A viruses. Opitz,  L. et al. Vaccine 2007, 25(5): 939-47.   PubMed





Related Literature

Vaccines - Isolation of Viral Particles & Glycoproteins

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RPL Functionalised Analytical Platforms: could enable simple, rapid and efficient detection and analysis of viral particles and glycoproteins. RPL functionalised biosensor based platforms may also present opportunities, as process analytical tools (PAT), for efficient monitoring of production processes for which there is a current unmet need.

​​​RPL Affinity Chromatography: could be used to efficiently and selectively isolate glycosylated viral particles and glycoproteins. Given the impact of glycosylation on immunogenicity the use of a glycoselective purification process may also enable the development of more efficacious vaccines. Bound molecules can be efficiently recovered under physiological conditions through the incorporation of appropriate sugars into elution buffers. RPL production is readily scalable enabling their use for large scale applications.

The glycans displayed on viral glycoproteins are usually complex structures terminating in mannose or galactose. GLycoSeLect's mannose and galactose specific RPL Products could therefore be used to enable highly efficient detection, analysis and isoalation of viral particles and glycoproteins.  

Many viruses display glycoproteins on their surface that play important roles in the viral life cycle. They are often key antigens against which immune responses are directed making them important components of vaccines. The glycans attached to viral glycoproteins can have a significant impact on the function and immunogenicity of these glycoproteins.

The Influenza Virus: displays two glycoproteins on its surface: Heamagglutinin (HA) and Neuraminidase (N). The number and locations of the glycans on the HA protein vary significantly among different strains. This variability is known to play an important role in modulating the immunogenicity of the protein as the glycans can mask antigenic sites and affect the nature and extent of the bodies immune responses to the virus.