Publication details

A point mutation led to overturn in sugar-binding specificity of lectin RS-IIL from PA-IIL lectin superfamily

Authors

MRÁZKOVÁ Jana MALINOVSKÁ Lenka WIMMEROVÁ Michaela

Year of publication 2015
Type Conference abstract
MU Faculty or unit

Faculty of Science

Citation
Description The so-called “PA-IIL lectin superfamily” includes several lectins from human opportunistic pathogens: PA-IIL (from Pseudomonas aeruginosa), CV-IIL (from Chromobacterium violaceum), BC2L-A and C-terminal domain from BC2L-C (from Burkholderia cenocepacia). Also, it includes one lectin from important plant pathogen: RS-IIL (from Ralstonia solanacearum). All these lectins are homologues with significant sequential and structural similarities but they differ in sugar-binding specificity. This fact is caused by differences in three amino acids which are arranged in the so-called “specificity binding loop” (amino acids at positions 22-23-24). The previous study, which was focused on investigation of fine specificity of PA-IIL, confirmed that amino acid at position 22 is mainly responsible for sugar binding specificity. Specific amino acid substitution in this position led to change of sugar preference of PA-IIL to the RS-IIL one. In this work, we prepared a mutant of the RS-IIL lectin with substitution of amino acid at position 22 to the one present in PA-IIL “specificity loop” to test possibility of changing of sugar preference to the PA IIL one.
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