Abstract
Lectins are carbohydrate-interacting proteins that play a pivotal role in multiple physiological and developmental aspects of all organisms. They can specifically interact with different bacterial and viral pathogens through carbohydrate-recognition domains (CRD). In addition, lectins are also of biotechnological interest because of their potential use as biosensors for capturing and identifying bacterial species. In this work, three C-type lectins from the Lepidoptera Spodoptera exigua were produced as recombinant proteins and their bacterial agglutination properties were characterized. The lowest protein concentration producing bacterial agglutination against a panel of different Gram+ and Gram− as well as their carbohydrate binding specificities was determined for the three lectins. One of these lectins, BLL2, was able to agglutinate cells from a broad range of bacterial species at an extremely low concentration, becoming a very interesting protein to be used as a biosensor or for other biotechnological applications involving bacterial capture.
Highlights
Lectins are carbohydrate-interacting proteins that play a pivotal role in multiple physiological and developmental aspects of all organisms
We have previously reported that the bracoviral-derived C-type lectin BLL2 from the Lepidoptera
One common property of the C-type lectins is their ability to bind to the cell surface, generally inducing agglutination of the cells
Summary
Lectins are carbohydrate-interacting proteins that play a pivotal role in multiple physiological and developmental aspects of all organisms. In the case of the immune defense, lectins are mainly involved in two important processes: the recognition of the pathogen, and the cellular interactions that lead to pathogen neutralization [1] Based on their functions, their structural characteristics, and their carbohydrate specificity, lectins can be grouped into several families [2]. Each CRD forms a double-loop structure stabilized by two highly conserved disulfide bridges, located at the base of the loops [4], which mediate the specific binding to sugars [1]. These proteins often act in an oligomeric form, which increases their avidity for multivalent ligands [3]. In the case of C-type lectin, the bacterial agglutination requires the presence of Calcium ions (Ca2+ ) [2]
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