Enhancing antibody responses by multivalent antigen display on thymus-independent DNA origami scaffolds

Nat Commun. 2024 Jan 30;15(1):795. doi: 10.1038/s41467-024-44869-0.

Abstract

Protein-based virus-like particles (P-VLPs) are commonly used to spatially organize antigens and enhance humoral immunity through multivalent antigen display. However, P-VLPs are thymus-dependent antigens that are themselves immunogenic and can induce B cell responses that may neutralize the platform. Here, we investigate thymus-independent DNA origami as an alternative material for multivalent antigen display using the receptor binding domain (RBD) of the SARS-CoV-2 spike protein, the primary target of neutralizing antibody responses. Sequential immunization of mice with DNA-based VLPs (DNA-VLPs) elicits protective neutralizing antibodies to SARS-CoV-2 in a manner that depends on the valency of the antigen displayed and on T cell help. Importantly, the immune sera do not contain boosted, class-switched antibodies against the DNA scaffold, in contrast to P-VLPs that elicit strong B cell memory against both the target antigen and the scaffold. Thus, DNA-VLPs enhance target antigen immunogenicity without generating scaffold-directed immunity and thereby offer an important alternative material for particulate vaccine design.

MeSH terms

  • Animals
  • Antibodies, Blocking
  • Antibodies, Neutralizing
  • Antibodies, Viral
  • Antibody Formation*
  • DNA
  • Humans
  • Mice
  • Spike Glycoprotein, Coronavirus*
  • Vaccines, Virus-Like Particle* / genetics

Substances

  • spike protein, SARS-CoV-2
  • Antibodies, Blocking
  • Vaccines, Virus-Like Particle
  • Antibodies, Neutralizing
  • DNA
  • Antibodies, Viral
  • Spike Glycoprotein, Coronavirus