Structural highlights
Function
[PA1L_PSEAE] D-galactose specific lectin. Binds in decreasing order of affinity: melibiose, methyl-alpha-D-galactoside, D-galactose, methyl-beta-D-galactoside, N-acetyl-D-galactosamine. Similar to plant lectins in its selective (carbohydrate-specific) hemagglutinating activity.
Publication Abstract from PubMed
Biofilm formation by pathogenic bacteria is a hallmark of chronic infections. In many cases, lectins play key roles in establishing biofilms. The pathogen Pseudomonas aeruginosa often exhibiting various drug resistances employs its lectins LecA and LecB as virulence factors and biofilm building blocks. Therefore, inhibition of the function of these proteins is thought to have potential in developing 'pathoblockers' preventing biofilm formation and virulence. Here, we describe for the first time a covalent lectin inhibitor specific to a carbohydrate binding site. In addition we report its application in the LecA-specific in vitro imaging of biofilms formed by P. aeruginosa.
Covalent lectin inhibition and application in bacterial biofilm imaging.,Wagner S, Hauck D, Hoffmann M, Sommer R, Joachim I, Muller R, Imberty A, Varrot A, Titz A Angew Chem Int Ed Engl. 2017 Sep 28. doi: 10.1002/anie.201709368. PMID:28960731[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wagner S, Hauck D, Hoffmann M, Sommer R, Joachim I, Muller R, Imberty A, Varrot A, Titz A. Covalent lectin inhibition and application in bacterial biofilm imaging. Angew Chem Int Ed Engl. 2017 Sep 28. doi: 10.1002/anie.201709368. PMID:28960731 doi:http://dx.doi.org/10.1002/anie.201709368
