Thursday, July 25, 2013
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Crystal structure of variable
lymphocyte receptor (VLR) VLRB.aGPA.23
with a tumor-associated glycan antigen
The crystal structure of
VLR bound to a tumor-associated glycan antigen could be useful for designing
tumor-targeting VLRs for therapeutic and diagnostic applications. VLRs are
adaptive immunity proteins from jawless vertebrates that bind glycans with
selectivity comparable to that of antibodies. Crystal structure and
thermodynamic studies showed that VLRB.aGPA.23 binds the tumor-associated Thomsen-Friedenreich
with four tryptophan residues that create a hydrophobic cage around the
target disaccharide. Next steps include developing VLRB.aGPA.23 as a
diagnostic reagent and determining its targets for therapeutic applications.
Published online July 25, 2013
Patents issued and pending
covering VLR composition of matter and methods for making and using the VLRs;
available for licensing
Luo, M. et al. J. Biol.
published online June 19, 2013;
Contact: Roy A. Mariuzza, Institute for Bioscience and
Biotechnology Research at the University of Maryland, Rockville, Md.
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