A novel lectin structure was found for a 17-kDa α-
d-galactose-binding lectin (termed “MytiLec”) isolated from the Mediterranean mussel,
Mytilus galloprovincialis. The complete primary structure of the lectin was determined by Edman degradation
and mass spectrometric analysis. MytiLec was found to consist of 149 amino acids with
a total molecular mass of 16,812.59 Da by Fourier transform-ion cyclotron resonance
mass spectrometry, in good agreement with the calculated value of 16,823.22 Da. MytiLec
had an N terminus of acetylthreonine and a primary structure that was highly novel
in comparison with those of all known lectins in the structure database. The polypeptide
structure consisted of three tandem-repeat domains of ∼50 amino acids each having
45–52% homology with each other. Frontal affinity chromatography technology indicated
that MytiLec bound specifically to globotriose (Gb3; Galα1–4Galβ1–4Glc), the epitope
of globotriaosylceramide. MytiLec showed a dose-dependent cytotoxic effect on human
Burkitt lymphoma Raji cells (which have high surface expression of Gb3) but had no
such effect on erythroleukemia K562 cells (which do not express Gb3). The cytotoxic
effect of MytiLec was specifically blocked by the co-presence of an α-galactoside.
MytiLec treatment of Raji cells caused increased binding of anti-annexin V antibody
and incorporation of propidium iodide, which are indicators of cell membrane inversion
and perforation. MytiLec is the first reported lectin having a primary structure with
the highly novel triple tandem-repeat domain and showing transduction of apoptotic
signaling against Burkitt lymphoma cells by interaction with a glycosphingolipid-enriched
microdomain containing Gb3.
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Article Info
Publication History
Received in revised form:
October 21,
2012
Received:
September 14,
2012
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© 2012 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.
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