Lectin microarrays and lectin-based methods continue to be important for developing biomarkers from Exosomes

A group from Department of Life Technologies, Division of Biotechnology, University of Turku, Finland, etc. has repoprted that lectins, lectin microarrays, and lectin-based methods continue to be important for screening, targeting, separation, and identification of improved biomarkers from the surface of Extracellular Vesicles (EVs).
https://pubmed.ncbi.nlm.nih.gov/37773167/

The EVs field has grown rapidly in the last decade. Although significant progress has been made in EV-based cancer biomarker discovery, translating these findings into clinical practice (including therapeutics) faces several challenges. These include the technical challenges of EV separation and detection and the need for more insights into molecular mechanisms governing EV release and EV uptake by target cells.
In each of these areas, it is thought that glycosylation holds a key to progress and that lectin-based approaches will unlock doors with their specificity and ease of implementation.

Some lectins have overlapping binding affinities and specificities towards multiple glycan structures which lead to difficulties in precisely identifying the glycan structures of interest. These ambiguities influence the assay results which lead to false-positive or false-negative results. Despite this kind od limitation, lectins, lectin microaerrays, and lectin-based methods definitely remain valuable tools in glycan research. To overcome some of these challenges, combination with other techniques such as MS and HPLC will be useful for a better understanding of detailed glycan structures and their applications. Moreover, glycan microarray technology will be complementaly to study glycan interactions and their functions in a systematic way.

To ensure accurate and reliable results from lectins and their glycan interaction, it is essential to verify this interaction through competitive inhibition, through modification of the glycan structures or by comparison with lectins which have been modified to show different binding specificities. This combination approach helps to avoid false positive or negative results and provides concrete evidence for glycan-mediated binding.