Heparin, on the other hand, shows

more extensive sulfation and uronic acid epimerization (Figure 6). Taken together, these data indicate that the regiochemistry of the sulfation is crucial for STI571 in vivo affinity of the binding as evidenced by the difference between the CS sulfated at C-4 or C-6, or the significant difference between the oversulfated heparin and the HS. Furthermore, the epimerization of the uronic acid seems also to be crucial, based on the difference in behavior CH5183284 induced by IdoA-rich species, such as heparin and, particularly, CS B. Figure 6 Disaccharide units of GAGs: CS A is sulfated at C4 of GalNAc (pointed by an arrow). CS C is sulfated at C6 of GalNAc (pointed by an arrow). In CS B (DS) GlcA is epimerized to IdoA, and can be sulfated at C4 or C6 of GalNAc and C2 of IdoA. HS includes GlcA and IdoA residues and can be sulfated at C2 of the uronic acid residue and at N, C6 and C3 of GlcN; heparin

is basically constituted of IdoA-GlcN oversulfated disaccharides. The high affinity of particular bacteria for HS and heparin has been observed with several pathogens. For instance, both molecules bind strongly to Pneumococci, Penicillium, Enterococci and Listeria[25, 51–53]. Ro 61-8048 supplier Conversely, heparin displays greater affinity for Chlamydia[54] while HS does so for Pseudomonas[55]. The CSs are high affinity receptors for Pneumococci[53] or Spirochetes[56] although they do not bind to Chlamydia, Penicillium, Pseudomonas or Listeria[51, 52, 54, 55]. Interestingly, DS usually shows a different behavior compared to other molecular forms of galactosaminoglycans, acting as receptor in Chlamydia, Penicillium or Leptospira[52, 54, 57], although, to our knowledge, this is the first communication on an increase of bacterial binding in the presence of this molecule in solution. The GAGs obtained

from different cell types have different effect on adherence The fine structure of the GAGs differs according not only to their nature, but also to the developmental phase Phosphoribosylglycinamide formyltransferase and the physiological and pathological conditions as well as to the cellular type. This is especially noticeable for HS, but also for CS/DS [50, 58, 59]. GAGs isolated from HeLa and HT-29 cells notably increased the inhibition of binding in comparison to the commercial forms, which were isolated from bovine kidney (HS), bovine trachea (CS A), shark cartilage (CS C) and porcine mucosa (CS B). OppA protein is an adhesin involved in Lv 72 adhesion to HeLa cells Once the nature of the main eukaryotic cell receptors was known, identification of bacterial adhesins became easier because the prior could be employed as affinity ligands for the latter. In this way, using heparin as ligand, we identified OppA, which strongly interfered with HeLa – L. salivarius attachment in a concentration dependent manner.