Membrane binding, endocytic trafficking and intracellular fate of high-affinity antibodies to gangliosides GD1a and GM1

RUGGIERO F.M.; VILCAES A.; YUKI N.; DANIOTTI J.L.

BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES

ELSEVIER SCIENCE BV

Lugar: Amsterdam; Año: 2017 vol. 1859 p. 80 - 80

0005-2736

angliosides are glycolipids embedded in the outer leaflets of the plasma membrane. Antibodies against GM1 and GD1a gangliosides are associated with selective dysfunction of motor axons in peripheral neuropathies, and differential endocytic processing of antibodies to gangliosides represent a critical modulator of site-specific injury in Guillain-Barré syndrome. In addition, antibodies to glycolipids have emerged as an attractive tool fortherapeutic interventions in cancer. In thiswork, we have investigated the binding, endocytosis and intracellular fate of high-affinity antibodies to gangliosides GD1a and GM1 both in epithelial and neuronal-like cells. Live cellimaging and fluorometric analysis showed that, after specific plasma membrane binding, a fraction of antibody to GD1a was slightly but rapidly internalized by a dynamin 2-independent pathway and then accumulated in the endocytic recycling compartment. We also show that internalization of antibody to GD1a is regulated by ADPribo