Disease relevance of L-Guluronic acid

• Alginate, a co-polymer of O-acetylated beta-1,4-linked D-mannuronic acid and L-guluronic acid, has been reported to function in the virulence of Pseudomonas syringae, although genetic studies to test this hypothesis have not been undertaken previously [1].
• The L-guluronic acid residues in the Azotobacter vinelandii polysaccharide alginate originate from a post-polymerization reaction catalysed by the enzyme mannuronan C-5-epimerase (ME) [2].

High impact information on L-Guluronic acid

• G-blocks, alpha 1-4-linked L-guluronic acid polymers that did not induce cytokine production from monocytes, reduced the cytokine production induced by the beta 1-4-linked polyuronic acids and LPS [3].
• Alginate, a copolymer of D-mannuronic acid and L-guluronic acid, is produced by a variety of pseudomonads, including Pseudomonas syringae [4].
• Immunochemical examination of the Pseudomonas aeruginosa glycocalyx: a monoclonal antibody which recognizes L-guluronic acid residues of alginic acid [5].
• Competitive binding studies with various alginates and monosaccharides suggest that the C6 carboxyl group of uronic acids are recognized by the antibody and that the antigen-binding site is fairly large and may recognize a particular sequence or epitope of alginic acid which is rich in L-guluronic acid [5].
• The relative viscosity is not correlated with the ratio of D-mannuronic acid to L-guluronic acid residues, or the degree of acetylation [6].

Anatomical context of L-Guluronic acid

• Alginate, an acetylated polymer of D-mannuronic and L-guluronic acid obtained from a mucoid strain of Pseudomonas aeruginosa was shown to inhibit the binding of an isogenic non-mucoid revertant to mouse peritoneal and pulmonary macrophages [7].

References