Low-affinity binding in cis to P2Y₂R mediates force-dependent integrin activation during hantavirus infection.

ABSTRACT: Pathogenic hantaviruses bind to the plexin-semaphorin-integrin (PSI) domain of inactive, β₃ integrins. Previous studies have implicated a cognate cis interaction between the bent conformation β₅/β₃ integrins and an arginine-glycine-aspartic acid (RGD) sequence in the first extracellular loop of P2Y₂R. With single-molecule atomic force microscopy, we show a specific interaction between an atomic force microscopy tip decorated with recombinant α_IIbβ₃ integrins and (RGD)P2Y₂R expressed on cell membranes. Mutation of the RGD sequence to RGE in the P2Y₂R removes this interaction. Binding of inactivated and fluorescently labeled Sin Nombre virus (SNV) to the integrin PSI domain stimulates higher affini

SUBMITTER: Bondu V 

PROVIDER: S-EPMC5638590 | biostudies-literature | 2017 Oct

REPOSITORIES: biostudies-literature