Anti-idiotipic antibodies mimicking a T antigen specific lectin inhibits human epithelial tumor cell proliferation

SENDRA VG; ZLOKOWSKI N; NORES GA; IRAZOQUI FJ

NATURE PUBLISHING GROUP

Año: 2010 vol. 88 p. 787 - 787

p class="MsoNormal" style="MARGIN: 0cm 0cm 0pt; LINE-HEIGHT: normal; TEXT-ALIGN: justify; mso-layout-grid-align: none">Cancer-associated mucins show frequent alterations of oligosaccharide chain profile. Terminal structures may be deleted, thereby exposing normally ‘cryptic’ structures such as Tn (GalNAcá-O-Ser/Thr) and T antigen (Galâ1-3GalNAcá-O-Ser/Thr). Overexpression of these commonly hidden glycoforms, and reduced level of naturally occurring anti-T or anti-Tn antibodies, is associated with epithelial tumor progression and aggressiveness. The lectin from the common edible mushroom Agaricus bisporus (ABL) shows high affinity binding to T antigen,