N-terminal chimeras of primate erythroparvovirus 1 VP2 protein self-assemble into virus-like particles.
VLPs are stable and 35% of their N-termini are exposed on the surface of the particles.
N-terminal chimeras of PE1V VP2 co-assemble in vitro with non-chimeric VP2.
PE1V VLPs constructed with different chimeras in defined ratios may lead to multifunctional particles.