title: Peptide display on a surface loop of human parvovirus B19 VP2: Assembly and characterization of virus-like particles.
abstract: Virus-like particles (VLPs) are valuable tools for nanotechnology and nanomedicine. These particles are obtained by the self-assembly, either in vivo or in vitro, of structural proteins of viral capsids. VLPs are excellent scaffolds for surface display of molecules. The N-termini of the structural proteins of human parvovirus B19 (B19V) have been already modified to display peptides or proteins. However, other surface-exposed elements have not been studied as potential locations for peptide display. In this research, we tested the potential of surface loop 62-75 of VP2 protein for the presentation of a 64-residue heterologous peptide. The chimeric protein was able to self-assemble in vitro into VLPs. Improved colloidal stability was observed for these particles, indicating that the peptide is on the surface of the particle. AFM analysis of the chimeric particles shows no obvious difference between the surfaces of particles assembled with VP2 and those assembled with the chimeric VP2. Our results indicate that loop 62-75 is a good candidate for heterologous peptide presentation on the surface of B19V VLPs.
authors.affiliation: Department of Biochemistry, Faculty of Medicine, National Autonomous University of Mexico, Mexico City 04510, Mexico.
authors.forename: José Sebastián
authors.initials: JS
authors.lastname: Santillán-Uribe
authors.affiliation: Department of Biochemistry, Faculty of Medicine, National Autonomous University of Mexico, Mexico City 04510, Mexico.
authors.forename: Josefina
authors.initials: J
authors.lastname: Valadez-García
authors.affiliation: Department of Biochemistry, Faculty of Medicine, National Autonomous University of Mexico, Mexico City 04510, Mexico.
authors.forename: Areli Del Carmen
authors.initials: Adel C
authors.lastname: Morán-García
authors.affiliation: Department of Biochemistry, Faculty of Medicine, National Autonomous University of Mexico, Mexico City 04510, Mexico.
authors.forename: Hugo César
authors.initials: HC
authors.lastname: Santillán-Uribe
authors.affiliation: Department of Biochemistry, Faculty of Medicine, National Autonomous University of Mexico, Mexico City 04510, Mexico. Electronic address: ismaelb@unam.mx.
authors.forename: Ismael
authors.initials: I
authors.lastname: Bustos-Jaimes
mesh_terms: D036022:Capsid Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D061505:Cell Surface Display Techniques; D006801:Humans; D018625:Microscopy, Atomic Force; D055503:Protein Multimerization; D055550:Protein Stability; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D022701:Virosomes / Q000235:genetics / Q000378:metabolism*
chemical_list: D036022:Capsid Proteins; D011993:Recombinant Fusion Proteins; D022701:Virosomes; C095548:capsid protein VP2, parvovirus B19
keywords: Parvovirus B19; Peptide display; Protein self-assembly; VLPs technology