Glycan site loss in two egg-adapted live attenuated influenza vaccine strains does not cause antigenic mismatches.

The haemagglutinin (HA) proteins of contemporary human H3N2 influenza viruses are heavily glycosylated. Glycans influence the protein's receptor-binding properties and antigenic profile and can be lost when candidate influenza vaccine strains are propagated in embryonated chicken eggs. Glycan changes in egg-derived vaccine strains have been linked to reduced vaccine effectiveness in inactivated influenza vaccines due to changes in antigenicity, but this has not been investigated in live attenuated influenza vaccines (LAIVs).

In Vitro Inhibitory Activity of Corilagin and Punicalagin Against and Their Mechanism(s) of Action.

Toxoplasmosis is a zoonotic disease caused by . The parasite infection in humans continues to rise due to an increasing seroprevalence rate in domestic and wild warm-blooded animals that serve as a major reservoir of the parasite. There are fewer drugs available for the treatment of toxoplasmosis.

Proactive vaccination using multiviral Quartet Nanocages to elicit broad anti-coronavirus responses.

Defending against future pandemics requires vaccine platforms that protect across a range of related pathogens. Nanoscale patterning can be used to address this issue. Here, we produce quartets of linked receptor-binding domains (RBDs) from a panel of SARS-like betacoronaviruses, coupled to a computationally designed nanocage through SpyTag/SpyCatcher links.