K. Grehan

Risk-free polio vaccine: Recombinant expression systems for production of stabilised virus-like particles

This study produces stabilized poliovirus VLPs using recombinant systems, showing equivalent or better immunogenicity than current vaccines.

Mechanism of enterovirus VP0 maturation cleavage based on the structure of a stabilised assembly intermediate.

The paper determines the molecular mechanism of VP0 cleavage in enteroviruses using structural and bioinformatic analysis of a provirion intermediate.

Production of antigenically stable enterovirus A71 virus-like particles in Pichia pastoris as a vaccine candidate.

This study produces antigenically stable EVA71 virus-like particles in Pichia pastoris, showing they retain native antigenic conformation and elicit neutralising antibodies comparable to inactivated virus vaccines.

Protease-independent production of poliovirus virus-like particles in Pichia pastoris: Implications for efficient vaccine development and insights into capsid assembly.

This study produces protease-independent poliovirus VLPs in Pichia pastoris, showing they maintain native antigenicity and thermostability, suggesting potential for improved vaccine development.

Production and characterisation of stabilised PV-3 virus-like particles using Pichia pastoris

This paper produces and characterizes stabilized PV-3 virus-like particles using Pichia pastoris, showing improved thermostability and antigen ratio compared to wild-type PV-3.

A conserved glutathione binding site in poliovirus is a target for antivirals and vaccine stabilisation

This study identifies a conserved glutathione binding site in poliovirus VLPs that can be targeted by antivirals and used to stabilize vaccines.

VelcroVax: a bolt-on vaccine platform technology improves antibody titres against a viral glycoprotein in mice

VelcroVax is a vaccine platform that enhances antibody titres against a viral glycoprotein in mice by combining a modified VLP with a SUMO-tagged antigen.

The bat influenza H17N10 can be neutralized by broadly-neutralizing monoclonal antibodies and its neuraminidase can facilitate viral egress.

This paper shows that bat influenza H17N10 can be neutralized by human antibodies and its neuraminidase N10 aids viral release without using sialic acid as a receptor.