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TitleStructural characterization of a Vatairea macrocarpa lectin in complex with a tumor-associated antigen: A new tool for cancer research.
Journal, issue, pagesInt J Biochem Cell Biol, Vol. 72, Page 27-39, Year 2016
Publish dateJan 2, 2016
AuthorsBruno L Sousa / José C Silva-Filho / Prashant Kumar / Melissa A Graewert / Ronniery I Pereira / Rodrigo M S Cunha / Kyria S Nascimento / Gustavo A Bezerra / Plínio Delatorre / Kristina Djinovic-Carugo / Celso S Nagano / Karl Gruber / Benildo S Cavada /
PubMed AbstractLegume lectins are the most thoroughly studied group of lectins and have been widely linked to many pathological processes. Their use as immunohistochemistry markers for cell profiling and cancer ...Legume lectins are the most thoroughly studied group of lectins and have been widely linked to many pathological processes. Their use as immunohistochemistry markers for cell profiling and cancer diagnosis have made these molecules important tools for immunological studies and have stimulated the prospection and characterization of new lectins. The crystal structures of a recombinant seed lectin from Vatairea macrocarpa (rVML) and its complexes with GalNAcα1-O-Ser, GalNAc and α-lactose, have been determined at 1.90, 1.97, 2.70 and 1.83Å resolution, respectively. Small angle X-ray scattering and calorimetry assays have confirmed the same pH stable oligomerization pattern and binding profiles proposed for its wild-type counterpart. In silico analyzes have explored the potential of this recombinant lectin as new tool for cancer research through a comparative profile with other legume lectins widely used for cancer diagnosis and prognosis. The results suggest the recognition of specific epitopes exhibited on different cancer cells as a process that relies on the disposition of hydrophobic clusters and charged regions around the lectin carbohydrate-binding site, favouring the anchorage of different groups in the antigen boundaries, highlighting the different potential of each analyzed lectin. In conclusion, the experimental results and comparative analysis show that rVML is as a promising tool for cancer research, able to bind with high affinity specific tumor-associated antigens, highly stable and easily produced.
External linksInt J Biochem Cell Biol / PubMed:26751394
MethodsSAS (X-ray synchrotron) / X-ray diffraction
Resolution1.83 Å
Structure data

SASDBS2:
Recombinant Tn antigen-binding lectin from Vatairea macrocarpa
Method: SAXS/SANS

PDB-4wv8:
Crystal structure of a recombinant Vatairea macrocarpa seed lectin complexed with lactose
Method: X-RAY DIFFRACTION / Resolution: 1.83 Å

Chemicals

ChemComp-CA:
Unknown entry

ChemComp-MN:
Unknown entry

ChemComp-HOH:
WATER

Source
  • vatairea macrocarpa (plant)
KeywordsSUGAR BINDING PROTEIN / Recombinant / Lectin / Legume / Dalbergieae

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