Microvesicles from various sources display a common glycomic signature

Microvesicles are nano‐sized particles secreted by a variety of cells that are important intercellular communication agents shuttling signaling proteins, antigens and RNA between cells. They are implicated in immune regulation, cancer progression and spread of infectious agents. Currently, the mechanism by which cargo is sorted into microvesicles is not understood. Preliminary data from our laboratory suggested that in T‐ cells, glycosylation is a determinant for protein recruitment to microvesicles resulting in a common microvesicle glycoprofile. To explore this further, we utilized the lectin microarray technology developed in our laboratory to study the glycosylation pattern of glycoproteins on the surface of microvesicles derived from a variety of cellular and biological sources. Microvesicles from different cell types and fluids display a common glycomic signature that is disctinct from their parent cell membranes. These results imply a glycan‐based mechanism for sorting of proteins to the microvesicle surface.