Structure and specificity of lectin from bacterium Burkholderia pseudomallei
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| Year of publication | 2015 |
| Type | Conference abstract |
| MU Faculty or unit | |
| Citation | |
| Description | A new lectin from B. pseudomallei was identified, which did not show any significant sequence similarity to the known proteins. The gene coding the lectin was cloned and protein expression and purification were successfully optimized. Surface plasmon resonance (SPR) and titration microcalorimetry (ITC) were used to characterize the interactions between the lectin and saccharides. Both methods revealed the lectin ability to bind D-mannose and mannosylated derivatives. The structure of the protein was solved using X-ray diffraction and showed a novel fold of bacterial lectins. The lectin is present as a monomer in solution as determined using analytical ultracentrifugation, which was also confirmed in the crystal structure. According to its structure and sequence, the protein belongs to a not yet described family of lectins. |
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