Conjugation of a phenanthrene‐imidazole fluorophore with the chondroitin sulfate generated from Escherichia coli K4 polysaccharide

2021 ◽  
Vol 138 (48) ◽  
pp. 51538
Author(s):  
Shuqin Xu ◽  
Huimin Xiang ◽  
Zhuqun Wang ◽  
Xiaoli Tang ◽  
Yan Zhang ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Chondroitin Sulfate ◽  
Escherichia Coli K4

Production of capsular polysaccharide from Escherichia coli K4

2010 ◽  
Vol 150 ◽  
pp. 82-82
Author(s):  
D. Cimini ◽  
E. Carlino ◽  
O.F. Restaino ◽  
R. De Mattia ◽  
M. De Rosa ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Capsular Polysaccharide ◽  
Escherichia Coli K4

Production of capsular polysaccharide from Escherichia coli K4 for biotechnological applications

2009 ◽  
Vol 85 (6) ◽  
pp. 1779-1787 ◽  
Author(s):  
Donatella Cimini ◽  
Odile Francesca Restaino ◽  
Angela Catapano ◽  
Mario De Rosa ◽  
Chiara Schiraldi
Keyword(s):  
Escherichia Coli ◽  
Capsular Polysaccharide ◽  
Biotechnological Applications ◽  
Escherichia Coli K4

scholarly journals Biosynthesis of dermatan sulphate. Defructosylated Escherichia coli K4 capsular polysaccharide as a substrate for the d-glucuronyl C-5 epimerase, and an indication of a two-base reaction mechanism

1996 ◽  
Vol 313 (2) ◽  
pp. 589-596 ◽  
Author(s):  
Helgi H. HANNESSON ◽  
Åsa HAGNER-McWHIRTER ◽  
Kerstin TIEDEMANN ◽  
Ulf LINDAHL ◽  
Anders MALMSTRÖM
Keyword(s):  
Escherichia Coli ◽  
Reaction Mechanism ◽  
Acid Hydrolysis ◽  
Capsular Polysaccharide ◽  
Glucuronic Acid ◽  
Microsomal Enzyme ◽  
Dermatan Sulphate ◽  
Mild Acid Hydrolysis ◽  
Mild Acid ◽  
Escherichia Coli K4

The capsular polysaccharide from Escherichia coli K4 consists of a chondroitin {[GlcA(β1→3)GalNAc(β1→4)]n} backbone, to which β-fructofuranose units are linked to C-3 of D-glucuronic acid (GlcA) residues. Removal of the fructose units by mild acid hydrolysis provided a substrate for the GlcA C-5 epimerase, which is involved in the generation of L-iduronic acid (IdoA) units during dermatan sulphate biosynthesis. Incubation of this substrate with solubilized fibroblast microsomal enzyme in the presence of 3H2O resulted in the incorporation of tritium at C-5 of hexuronyl units. A Km of 67×10-6 M hexuronic acid (equivalent to disaccharide units) was determined, which is similar to that (80×10-6 M) obtained for dermatan (desulphated dermatan sulphate). Vmax. was about 4 times higher with dermatan than with the K4 substrate. A defructosylated K4 polysaccharide isolated after incubation of bacteria with D-[5-3H]glucose released 3H2O on reaction with the epimerase, and thus could be used to assay the enzyme. Incubation of a K4 substrate with solubilized microsomal epimerase for 6 h in the presence of 3H2O resulted in the formation of about 5% IdoA and approximately equal amounts of 3H in GlcA and IdoA. A corresponding incubation of dermatan yielded approx. 22% GlcA, which contained virtually all the 3H label. These results are tentatively explained in terms of a two-base reaction mechanism, involving a monoprotic L-ido-specific base and a polyprotic D-gluco-specific base. Most of the IdoA residues generated by the enzyme occurred singly, although some formation of two or three consecutive IdoA-containing disaccharide units was observed.

scholarly journals Antibodies to Escherichia coli-Expressed C-Terminal Domains of Plasmodium falciparum Variant Surface Antigen 2-Chondroitin Sulfate A (VAR2CSA) Inhibit Binding of CSA-Adherent Parasites to Placental Tissue

2013 ◽  
Vol 81 (4) ◽  
pp. 1031-1039 ◽  
Author(s):  
Tracy Saveria ◽  
Andrew V. Oleinikov ◽  
Kathryn Wiliamson ◽  
Richa Chaturvedi ◽  
Joe Lograsso ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Plasmodium Falciparum ◽  
Chondroitin Sulfate ◽  
Surface Antigen ◽  
Transmembrane Protein ◽  
Placental Malaria ◽  
Placental Tissue ◽  
Content Type ◽  
Variant Surface Antigen ◽  
Chondroitin Sulfate A

ABSTRACTPlacental malaria (PM) is characterized by infected erythrocytes (IEs) that selectively bind to chondroitin sulfate A (CSA) and sequester in placental tissue. Variant surface antigen 2-CSA (VAR2CSA), aPlasmodium falciparumerythrocyte membrane protein 1 (PfEMP1) protein family member, is expressed on the surface of placental IEs and mediates adherence to CSA on the surface of syncytiotrophoblasts. This transmembrane protein contains 6 Duffy binding-like (DBL) domains which might contribute to the specific adhesive properties of IEs. Here, we use laboratory isolate 3D7 VAR2CSA DBL domains expressed inEscherichia colito generate antibodies specific for this protein. Flow cytometry results showed that antibodies generated against DBL4ε, DBL5ε, DBL6ε, and tandem double domains of DBL4-DBL5 and DBL5-DBL6 all bind to placental parasite isolates and to lab strains selected for CSA binding but do not bind to children's parasites. Antisera to DBL4ε and to DBL5ε inhibit maternal IE binding to placental tissue in a manner comparable to that for plasma collected from multigravid women. These antibodies also inhibit binding to CSA of several field isolates derived from pregnant women, while antibodies to double domains do not enhance the functional immune response. These data support DBL4ε and DBL5ε as vaccine candidates for pregnancy malaria and demonstrate thatE. coliis a feasible tool for the large-scale manufacture of a vaccine based on these VAR2CSA domains.

scholarly journals Isolation and Expression in Escherichia coli ofcslA and cslB, Genes Coding for the Chondroitin Sulfate-Degrading Enzymes Chondroitinase AC and Chondroitinase B, Respectively, from Flavobacterium heparinum

2000 ◽  
Vol 66 (1) ◽  
pp. 29-35 ◽  
Author(s):  
Ana Lydia Tkalec ◽  
Dominique Fink ◽  
Françoise Blain ◽  
Guiyi Zhang-Sun ◽  
Maryse Laliberte ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Chondroitin Sulfate ◽  
Dna Sequences ◽  
Dermatan Sulfate ◽  
Signal Sequence ◽  
Open Reading Frames ◽  
Amino Acid Residues ◽  
Chondroitin Ac Lyase ◽  
Flavobacterium Heparinum

ABSTRACT In medium supplemented with chondroitin sulfate,Flavobacterium heparinum synthesizes and exports two chondroitinases, chondroitinase AC (chondroitin AC lyase; EC 4.2.2.5 ) and chondroitinase B (chondroitin B lyase; no EC number), into its periplasmic space. Chondroitinase AC preferentially depolymerizes chondroitin sulfates A and C, whereas chondroitinase B degrades only dermatan sulfate (chondroitin sulfate B). The genes coding for both enzymes were isolated from F. heparinum and designated cslA (chondroitinase AC) and cslB(chondroitinase B). They were found to be separated by 5.5 kb on the chromosome of F. heparinum, transcribed in the same orientation, but not linked to any of the heparinase genes. In addition, the synthesis of both enzymes appeared to be coregulated. The cslA and cslB DNA sequences revealed open reading frames of 2,103 and 1,521 bp coding for peptides of 700 and 506 amino acid residues, respectively. Chondroitinase AC has a signal sequence of 22 residues, while chondroitinase B is composed of 25 residues. The mature forms of chondroitinases AC and B are comprised of 678 and 481 amino acid residues and have calculated molecular masses of 77,169 and 53,563 Da, respectively. TruncatedcslA and cslB genes have been used to produce active, mature chondroitinases in the cytoplasm of Escherichia coli. Partially purified recombinant chondroitinases AC and B exhibit specific activities similar to those of chondroitinases AC and B from F. heparinum.

scholarly journals High cell density cultivation of Escherichia coli K4 in a microfiltration bioreactor: a step towards improvement of chondroitin precursor production

2011 ◽  
Vol 10 (1) ◽  
pp. 10 ◽  
Author(s):  
Odile Restaino ◽  
Donatella Cimini ◽  
Mario De Rosa ◽  
Angela Catapano ◽  
Mario De Rosa ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Cell Density ◽  
High Cell Density ◽  
High Cell ◽  
High Cell Density Cultivation ◽  
Escherichia Coli K4
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