Respiratory syncytial virus glycoprotein G impedes CX₃CR1-activation by CX₃CL1 and monocyte function.

ABSTRACT: The soluble form of the Respiratory Syncytial Virus (RSV) G protein (sG) bears resemblance to the chemokine fractalkine (CX₃CL1). Both RSV sG and CX₃CL1 possess a mucin-like domain and a CX₃C motif, exist in membrane-associated and soluble forms, and bind to the CX₃CR1 receptor expressed on immune and epithelial cells. To explore the biological significance of RSV sG and CX₃CR1 interaction, we produced wild type (WT) and CX₃C motif-deficient (CX₃C^Mut) RSV sG proteins and determined their effects on CX₃CR1 signaling in monocytic cells. Both CX₃C^Mut- and WT RSV sG failed to activate CX₃CR1 signaling directly. However, WT sG competed with CX₃CL1 for CX₃CR1 binding and reduced CX₃CL1-induced CX₃CR1-activation, monocyt

SUBMITTER: Meineke R 

PROVIDER: S-EPMC11721137 | biostudies-literature | 2024 Dec

REPOSITORIES: biostudies-literature