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NostrumBiodiscovery contributed to the structural characterization of the recently approved HIPRA's COVID-19 vaccine

The European Medicines Agency (EMA) and the European Commission has approved HIPRA's COVID-19 vaccine, BIMERVAX®, as a booster dose in persons older than 16 years, previously vaccinated with a COVID-19 mRNA vaccine

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Corporate

The European Medicines Agency (EMA) and the European Commission has approved HIPRA's COVID-19 vaccine, BIMERVAX®, as a booster dose in persons older than 16 years, previously vaccinated with a COVID-19 mRNA vaccine. Nostrum Biodiscovery (Nostrum), as a leading company in the field of computational modelling and machine learning, has contributed to the structural characterization of the developed  BIMERVAX® protein antigen by applying its advanced technology and experience.

BIMERVAX® is a bivalent adjuvanted vaccine containing a recombinant protein based on the receptor-binding domain (RBD) of the Beta and Alpha variants of SARS-CoV-2. The rationale behind this antigenic construct relies on an affinity maximisation towards its human target receptor, hACE2. Nostrum computationally generated a three-dimensional structural model of the approved antigen and highlighted the main structural determinants of its exceptional affinity towards its human protein receptor, as observed experimentally. 

The collaboration also resulted in a key contribution to the scientific publication  “Preclinical evaluation of a COVID-19 vaccine candidate based on a recombinant RBD fusion heterodimer of SARS-CoV-2” published in iScience in March. 

On the other hand, within the framework of the VSRVAC project led by HIPRA and other biotechnological companies, including Nostrum, a new vaccine against the human respiratory syncytial virus is being investigated. Nostrum is contributing in the molecular research, engineering and optimization of the immunogenic potential of the encoded protein.

gráfico-AseBio-Biotecnologia
 

* Computation modelling for PHH-1V vaccine. This highlights the presence of two different construct conformations: (1) Stabilized N-/C-terminal conformation and (2) adopting protein-protein interactions. Bottom: hACE2 receptor-construct model derived from MD calculations of the B.1.351-B.1.1.7 construct