@article{open2063,
          volume = {491},
          number = {3},
          author = {Sonal Mahajan and Aasawari Khairnar and Ritika Bishnoi and T.N.C. Ramya},
            note = {Copyright of this article belongs to Elsevier.},
           title = {Microbial F-type lectin domains with affinity for blood group antigens},
       publisher = {Elsevier},
            year = {2017},
         journal = {Biochemical and Biophysical Research Communications},
           pages = {708--713},
        keywords = {Blood group antigens; Cyanobium sp. FLD; F-type lectin domain; Fucose; Leucothrix mucor FLD; Myxococcus hansupus FLD},
             url = {http://crdd.osdd.net/open/2063/},
        abstract = {F-type lectins are fucose binding lectins with characteristic fucose binding and calcium binding motifs. Although they occur with a selective distribution in viruses, prokaryotes and eukaryotes, most biochemical studies have focused on vertebrate F-type lectins. Recently, using sensitive bioinformatics search techniques on the non-redundant database, we had identified many microbial F-type lectin domains with diverse domain organizations. We report here the biochemical characterization of F-type lectin domains from Cyanobium sp. PCC 7001, Myxococcus hansupus and Leucothrix mucor. We demonstrate that while all these three microbial F-type lectin domains bind to the blood group H antigen epitope on fucosylated glycans, there are fine differences in their glycan binding specificity. Cyanobium sp. PCC 7001 F-type lectin domain binds exclusively to extended H type-2 motif, Myxococcus hansupus F-type lectin domain binds to B, H type-1 and Lewisb motifs, and Leucothrix mucor F-type lectin domain binds to a wide range of fucosylated glycans, including A, B, H and Lewis antigens. We believe that these microbial lectins will be useful additions to the glycobiologist's toolbox for labeling, isolating and visualizing glycans.}
}