In Vaccine Design, Artificial Proteins Start Mimicking Real Immunogens

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This week, Lab.Equipment has sourced a new Biotech article published from GEN just for you:

Proteins designed from the ground up are usually too regular and continuous to be useful in vaccine design, which must grapple with irregular and discontinuous epitopes, that is, the complex antigenic features that are recognized by the immune system’s antibodies. And so, these proteins, which are called de novo proteins, have been limited to mimicking the simplest epitopes.

Impatient with the sorts of de novo proteins that have been designed with existing computational systems, scientists based at École Polytechnique Fédérale de Lausanne (EPFL) built a computational system of their own, one capable of designing artificial proteins that rival the complexity of real proteins. The system, called TopoBuilder, designs scaffolds for irregular and discontinuous neutralization epitopes.

The EPFL scientists, led by Bruno Correia, a professor at the Laboratory of Protein Design and Immunoengineering (LPDI), described TopoBuilder in an article that appeared May 15 in Science, in an article entitled, “De novo protein design enables the precise induction of RSV-neutralizing antibodies.” The scientists decided to train TopoBuilder on respiratory syncytial virus (RSV), which causes serious lung infections and is a leading cause of hospitalization in infants and the elderly, because it seemed a suitable test object.

“Despite several decades of research,” noted Correia, “there is still no vaccine or cure for respiratory syncytial virus.”

“When a vaccine doesn’t work well,” he continued, “we tend to think that it’s because the antibodies produced are not protective. It’s usually because our immune system is simply making the wrong type of antibodies.”

To demonstrate TopoBuilder’s abilities, Correia and colleagues generated three epitope-focused immunogens designed to induce a targeted neutralizing antibody response to RSV... Read the whole article at the GEN Blog.

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