Junctional adhesion molecule A and tumor cell surface sialic acids (JAM-A/Sialic acid)

Junctional adhesion molecule A (JAM-A) and tumor cell surface sialic acids function as a dual-receptor system exploited by certain therapeutic agents, most notably oncolytic reoviruses like Pelareorep. Sialic acids, which are frequently overexpressed on the surface of malignant cells (hypersialylation), serve as the initial low-affinity attachment sites for the virus (Reiter et al., 2011). Following this initial tethering, the virus binds with high affinity to JAM-A, a member of the immunoglobulin superfamily typically found in tight junctions but often upregulated and mislocalized in various cancers (Barton et al., 2001). This dual-binding mechanism facilitates viral entry and subsequent selective replication within cancer cells, leading to direct oncolysis and the stimulation of a systemic anti-tumor immune response. Targeting this combination allows for enhanced selectivity toward neoplastic tissues while sparing normal cells that lack the necessary density or accessibility of these surface markers (Oncolytics Biotech).

Other names

F11 receptorF11RJAM-1CD321PAM-1Sialic acid-JAM-A receptor complex

Oncolytic viral entry via sequential binding to sialic acid (attachment) and JAM-A (internalization).