News & Events

08 Mar, 2021
Pneumagen Announces Neumifil™ is Efficacious In an Established Model of COVID-19 Infection

Neumifil Binds with Equally High Affinity to Spike Proteins of Wuhan, UK and South African Variants

8th March 2021 – St. Andrews, Scotland – Pneumagen Ltd, a biotech company developing a universal pan-viral intranasal drug for protection against respiratory tract infections (RTIs), today announced a further milestone in the development of Neumifil™ for the treatment of COVID-19. Utilizing a hamster model of COVID-19 infection, researchers showed Neumifil was efficacious, significantly reducing clinical signs and weight loss in animals infected with SARS-CoV-2.

Pneumagen scientists located at the University of St. Andrews confirmed that Neumifil binds with equally high affinity to SARS-CoV-2 spike proteins from the Wuhan (Wuhan-Hu-1), UK (B.1.1.7) and South Africa (B.1.351) variants. In further experiments, Pneumagen also demonstrated high affinity Neumifil binding to the ACE2 receptor, which is used by the SARS-CoV-2 virus to infect the host.

Neumifil is a first-in-class Carbohydrate Binding Module (mCBMs), generated from the Company’s proprietary GlycoTarge™ platform. It is being developed for the universal treatment of RTIs caused by influenza viruses, RSV, and coronaviruses including SARS-CoV-2. Neumifil has the potential to revolutionize the treatment of RTIs, providing patients total protection against respiratory pathogens including COVID-19 variant strains.

Douglas Thomson, CEO of Pneumagen, said, “This exciting data confirms Neumifil’s potential as a treatment against variant strains of COVID-19. Neumifil, our universal pan-viral intranasal product, targets glycans to provide both prophylaxis and treatment for COVID-19, and other emerging viruses with pandemic potential. We are preparing for a Phase I clinical study in mid-2021.”

The underlying science and mechanism of action of Neumifil is well defined and validated. Neumifil binds with high affinity to terminal sialic acid glycans on the viral spike protein, which remain present in the UK and South African variants. Furthermore, Neumifil binds to ACE2 (the human receptor for SARS-CoV-2). Glycans on both the viral spike protein and ACE2 have been shown to be important in virus-host recognition [1,2,3]. The ability to target not only the virus’s spike protein (including new variants) but also its target on the host, reduces Neumifil’s susceptibility to viral resistance compared to more conventional approaches.

References

1. Shajahan, A. et al. Comprehensive characterization of N- and O- glycosylation of SARS-CoV-2 human receptor angiotensin converting enzyme 2. (2020) Anal. Glycobiol. doi: 10.1093/glycob/cwaa101

2. Zhao, P. et al. Virus-Receptor Interactions of Glycosylated SARSCoV-2 Spike and Human ACE2 Receptor (2020) Cell Host & Microbe. 28, 586–601

3. Casalino, L. et al. Beyond Shielding: The Roles of Glycans in the SARS-CoV-2 Spike Protein (2020) ACS Cent. Sci. 6, 10, 1722–1734