Single-Point Mutations in Qβ Virus-like Particles Change Binding to Cells.

ABSTRACT: Virus-like particles (VLPs) constitute large, polyvalent platforms onto which a wide variety of functional units can be grafted. Their use in biological settings often depends on their specific binding to cells or receptors of interest; this can be compromised by excessive nonspecific association with other cells. We found that lysine residues mediate such nonspecific interactions, presumably by virtue of protonation and interaction with anionic membrane lipid headgroups and/or complementary residues of cell surface proteins and polysaccharides. Chemical acylation of surface-exposed amines of the Qβ VLP led to a significant reduction in the association of particles with mammalian cells. Single-point mutations of particular lysine residues to either glutamine, glutamic acid, tryptophan, or

SUBMITTER: Martino ML 

PROVIDER: S-EPMC9068229 | biostudies-literature | 2021 Aug

REPOSITORIES: biostudies-literature