Rabies virus utilizes neuropilin 2 as an endocytic receptor to trigger TGFBR1-mediated actin polymerization.

ABSTRACT: Rabies virus (RABV), belonging to the rhabdovirus, is a typical large virus that enters cells via clathrin-mediated endocytosis (CME). RABV-containing pits are only partially clathrin-coated and require local actin polymerization for efficient internalization. This unconventional entry process suggests that a specific receptor may be required to initiate actin polymerization during RABV entry. Here, we found that RABV uses the cell membrane protein neuropilin 2 (NRP2) to initiate F-actin polymerization. NRP2 is required for RABV infection and directly interacts with RABV glycoprotein. An antibody against the ectodomain of NRP2 and the soluble ectodomain of NRP2 blocked RABV infection in cells. Expression of human NRP2 in non-susceptible DU145 cells enabled RABV infection. We further found

SUBMITTER: Sun Z 

PROVIDER: S-EPMC12282144 | biostudies-literature | 2025 Jul

REPOSITORIES: biostudies-literature