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Capsular polysaccharide biosynthesis protein ..

capD - Capsular polysaccharide biosynthesis protein …

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Required for the biosynthesis of type 1 capsular polysaccharide.

Diffusion of antibiotics can take place through the matrix of the biofilm. Diffusion or penetration of antibiotics to deeper layers of biofilm is affected by exopolysaccharide acting as a physical barrier. When molecules direct interact with this matrix, their movement to the interior of the biofilm is slow down, resulting antibiotic resistance. This may also acts as a hindrance for high molecular weight molecules such as complement system proteins and lysozyme, and in liquid culture bacterial cells are readily exposed to antibiotics as compare to compact structure biofilm. Bacteria escape from biofilm that do not produce polysaccharide and are easily attack by immune system cells. Inactivation of antibiotic takes place when bind to biofilm matrix. P. aeruginosa have alginate exopolysaccharide, which is anionic in nature. Presence of this matrix explains slow penetration of fluoroquinolones and aminoglycosides [,,]. Low penetration of antibiotic is not sufficient to explain the biofilm resistance, other mechanisms have been assumed that must be involved. This is also suggested recently that slow diffusion of antibiotics permit plenty of time to establish a protective response to stress [].

cpsA capsular polysaccharide biosynthesis protein …

Characterization of a novel acyl carrier protein, RkpF, encoded by an operon involved in capsular polysaccharide biosynthesis in Sinorhizobium meliloti

negatively regulates capsular polysaccharide biosynthesis in ..

This domain is found in diverse bacterial polysaccharide biosynthesis proteins including the CapD protein from Staphylococcus aureus [], the WalL protein, mannosyl-transferase [], and several putative epimerases. The CapD protein is required for biosynthesis of type 1 capsular polysaccharide.

cps14B to cps14H products are similar to other proteins involved in bacterial polysaccharide biosynthesis in both Gram-negative and -positive bacteria [].

in capsular polysaccharide (CPS) biosynthesis ..

Capsular (CPSs) are protective structures on the surfaces of many Gram-negative bacteria. The principal CPS of the human pathogen and Tier 1 select agent consists of a linear repeat of –­3)-­2--acetyl-6-deoxy----heptopyranose-(1–. This CPS is critical to the virulence of this emerging pathogen and represents a key target for the development of novel therapeutics. is one of several genes in the CPS biosynthetic cluster whose deletion leads to significant attenuation of the pathogen; unlike most others, it has no homologues of known function and no detectable sequence similarity to any protein with an extant structure. Here, the of WcbI bound to its proposed product, coenzyme A, is reported at 1.38 Å resolution, solved using the halide-soak method with multiple This structure reveals that WcbI incorporates a previously described 100-amino-acid subdomain into a novel, principally helical fold (310 amino acids). This fold adopts a cradle-like structure, with a deep binding pocket for CoA in the loop-rich cradle. Structural analysis and biophysical assays suggest that WcbI functions as an acetyltransferase enzyme, whilst biochemical tests suggest that another functional module might be required to assist its activity in forming the mature capsule.

" Characterization of a novel acyl carrier protein, RkpF, encoded by an operon involved in capsular polysaccharide biosynthesis in Sinorhizobium meliloti "

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  • rmpA reduced K2 capsular polysaccharide (CPS) biosynthesis, ..

    13/02/2017 · RmpA regulation of capsular polysaccharide biosynthesis in Klebsiella ..

  • capsular polysaccharide (CPS) biosynthesis ..

    The polysaccharide biosynthesis protein, ..

  • Biosynthesis and Assembly of Capsular Polysaccharides …

    Biosynthesis and Assembly of Capsular Polysaccharides in Escherichia ..

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capsular polysaccharide biosynthesis

AB - Background. In V. cholerae, the biogenesis of capsule polysaccharide is poorly understood. The elucidation of capsule structure and biogenesis is critical to understanding the evolution of surface polysaccharide and the internal relationship between the capsule and LPS in this species. V. cholerae serogroup O31 NRT36S, a human pathogen that produces a heat-stable enterotoxin (NAG-ST), is encapsulated. Here, we report the covalent structure and studies of the biogenesis of the capsule in V. cholerae NRT36S. Results. The structure of the capsular (CPS) polysaccharide was determined by high resolution NMR spectroscopy and shown to be a complex structure with four residues in the repeating subunit. The gene cluster of capsule biogenesis was identified by transposon mutagenesis combined with whole genome sequencing data (GenBank accession DQ915177). The capsule gene cluster shared the same genetic locus as that of the O-antigen of lipopolysaccharide (LPS) biogenesis gene cluster. Other than V. cholerae O139, this is the first V. cholerae CPS for which a structure has been fully elucidated and the genetic locus responsible for biosynthesis identified. Conclusion. The co-location of CPS and LPS biosynthesis genes was unexpected, and would provide a mechanism for simultaneous emergence of new O and K antigens in a single strain. This, in turn, may be a key element for V. cholerae to evolve new strains that can escape immunologic detection by host populations.

Capsular polysaccharide synthesis, CpsB/CapC (IPR016667) ..

Capsular polysaccharide A (CPSA) is a four-sugar repeating unit polymer found on the surface of the gut symbiont that has therapeutic potential in animal models of autoimmune disorders. This therapeutic potential has been credited to its zwitterionic character derived from a positively charged N-acetyl-4-aminogalactosamine (AADGal) and a negatively charged 4,6-O-pyruvylated galactose (PyrGal). In this report, using a fluorescent polyisoprenoid chemical probe, the complete enzymatic assembly of the CPSA tetrasaccharide repeat unit is achieved. The proposed pyruvyltransferase, WcfO; galactopyranose mutase, WcfM; and glycosyltransferases, WcfP and WcfN, encoded by the CPSA biosynthesis gene cluster were heterologously expressed and functionally characterized. Pyruvate modification, catalyzed by WcfO, was found to occur on galactose of the polyisoprenoid-linked disaccharide (AADGal-Gal), and did not occur on galactose linked to uridine diphosphate (UDP) or a set of nitrophenyl-galactose analogues. This pyruvate modification was also found to be required for the incorporation of the next sugar in the pathway N-acetylgalactosamine (GalNAc) by the glycosyltransferase WcfP. The pyruvate acetal modification of a galactose has not been previously explored in the context of a polysaccharide biosynthesis pathway, and this work demonstrates the importance of this modification to repeat unit assembly. Upon production of the polyisoprenoid-linked AADGal-PyrGal-GalNAc, the proteins WcfM and WcfN were found to work in concert to form the final tetrasaccharide, where WcfM formed UDP-galactofuranose (Gal) and WcfN transfers Gal to the AADGal-PyrGal-GalNAc. This work demonstrates the first enzymatic assembly of the tetrasaccharide repeat unit of CPSA in a sequential single pot reaction.

capsular-polysaccharide biosynthesis ..

Capsular polysaccharide A (CPSA) is a four-sugar repeating unit polymer found on the surface of the gut symbiont that has therapeutic potential in animal models of autoimmune disorders. This therapeutic potential has been credited to its zwitterionic character derived from a positively charged N-acetyl-4-aminogalactosamine (AADGal) and a negatively charged 4,6-O-pyruvylated galactose (PyrGal). In this report, using a fluorescent polyisoprenoid chemical probe, the complete enzymatic assembly of the CPSA tetrasaccharide repeat unit is achieved. The proposed pyruvyltransferase, WcfO; galactopyranose mutase, WcfM; and glycosyltransferases, WcfP and WcfN, encoded by the CPSA biosynthesis gene cluster were heterologously expressed and functionally characterized. Pyruvate modification, catalyzed by WcfO, was found to occur on galactose of the polyisoprenoid-linked disaccharide (AADGal-Gal), and did not occur on galactose linked to uridine diphosphate (UDP) or a set of nitrophenyl-galactose analogues. This pyruvate modification was also found to be required for the incorporation of the next sugar in the pathway N-acetylgalactosamine (GalNAc) by the glycosyltransferase WcfP. The pyruvate acetal modification of a galactose has not been previously explored in the context of a polysaccharide biosynthesis pathway, and this work demonstrates the importance of this modification to repeat unit assembly. Upon production of the polyisoprenoid-linked AADGal-PyrGal-GalNAc, the proteins WcfM and WcfN were found to work in concert to form the final tetrasaccharide, where WcfM formed UDP-galactofuranose (Gal) and WcfN transfers Gal to the AADGal-PyrGal-GalNAc. This work demonstrates the first enzymatic assembly of the tetrasaccharide repeat unit of CPSA in a sequential single pot reaction.

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