Junctional adhesion molecule A and sialic acid-containing glycans (JAM-A/SA)

Junctional adhesion molecule A (JAM-A), also known as F11 receptor (F11R), is a transmembrane glycoprotein belonging to the immunoglobulin superfamily that localizes to the tight junctions of epithelial and endothelial cells (UniProt P50129). It plays a critical role in regulating cell polarity, leukocyte transmigration, and paracellular permeability. Sialic acid-containing glycans are carbohydrate structures on the cell surface that often serve as initial docking sites for various pathogens. The interaction between JAM-A and sialic acid-containing glycans is particularly significant in the context of Mammalian Orthoreovirus (reovirus) infection, where sialic acids facilitate low-affinity attachment and JAM-A serves as the high-affinity receptor for viral entry (PubMed: 12743296). In oncology, JAM-A is frequently overexpressed and contributes to tumor progression, migration, and metastasis, making it a target for therapeutic antibodies and oncolytic viruses like Pelareorep (PubMed: 28651314). Targeting this dual-receptor system allows for selective viral-mediated lysis of cancer cells or the inhibition of tumor-promoting cell adhesion pathways.

Other names

F11 receptorF11RJAM-1CD321Platelet adhesion molecule 1PAM-1Sialic acid-containing glycoconjugates

Oncolytic viral entry and replication via sialic acid attachment and JAM-A internalization; Inhibition of JAM-A mediated homophilic interactions to prevent tumor cell migration.