Abstract
The human cytomegalovirus (HCMV)-encoded chemokine receptor US28 contributes to various aspects of the viral life cycle and promotes immune evasion by scavenging chemokines from the microenvironment of HCMV-infected cells.In contrast to the plasma membrane localization of most human chemokinereceptors, US28 has a predominant intracellular localization. In this study, weused immunofluorescence and electron microscopy to determine thelocalization of US28 upon exogenous expression, as well as in HCMV-infectedcells. We observed that US28 localizes to late endosomal compartmentscalled multivesicular bodies (MVBs), where it is sorted in intraluminal vesicles. Live-cell total internal reflection fluorescence (TIRF) microscopy revealed that US28-containing MVBs can fuse with the plasma membrane, resulting inthe secretion of US28 on exosomes. Exosomal US28 binds thechemokines CX3CL1 and CCL5, and US28-containing exosomes inhibited theCX3CL1-CX3CR1 signaling axis. These findings suggest that exosomal releaseof US28contributes to chemokine scavenging and immune evasion by HCMV.
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