Computational design of a symmetrical β-trefoil lectin with cancer cell binding activity.

Posted on Posted in AMRC Research

Date: 26 Jul 2017


Computational protein design has advanced very rapidly over the last decade, but there remain few examples of artificial proteins with direct medical applications. This study describes a new artificial β-trefoil lectin that recognises Burkitt’s lymphoma cells, and which was designed with the intention of finding a basis for novel cancer treatments or diagnostics. The new protein, called “Mitsuba”, is based on the structure of the natural shellfish lectin MytiLec-1, a member of a small lectin family that uses unique sequence motifs to bind α-D-galactose. The three subdomains of MytiLec-1 each carry one galactose binding site, and the 149-residue protein forms a tight dimer in solution. Mitsuba (meaning “three-leaf” in Japanese) was created by symmetry constraining the structure of a MytiLec-1 subunit, resulting in a 150-residue sequence that contains three identical tandem repeats. Mitsuba-1 was expressed and crystallised to confirm the X-ray structure matches the predicted model. Mitsuba-1 recognises cancer cells that express globotriose (Galα(1,4)Galβ(1,4)Glc) on the surface, but the cytotoxicity is abolished.


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For inquiries regarding this press release

Jeremy R. H. TAME

E-mail:   Phone: +81 45 508 7228


Professor, Drug Design Laboratory,
Yokohama City University, Graduate School of Medical Life Science
1-7-29 Suehiro-cho, Tsurumi-ku, Yokohama 230-0045 JAPAN


Yasuhiro OZEKI

E-mail:   Phone: +81 45 787 2221


Professor, Laboratory of Glycobiology and Marine Biochemistry,
Yokohama City University, Graduate School of Nanobioscience
22-2 Seto, Kanazawa-ku, Yokohama 236-0027 JAPAN