Structural and Genetic Characterization of Enterohemorrhagic
            <i>Escherichia coli</i>
            O145 O Antigen and Development of an O145 Serogroup-Specific PCR Assay

Feng, Lu; Senchenkova, Sof’ya N.; Jiang, Tao; Shashkov, Alexander S.; Liu, Bin; Shevelev, Sergei D.; Reeves, Peter R.; Xu, Jianguo; Knirel, Yuriy A.; Wang, Lei

doi:10.1128/jb.187.2.758-764.2005

Cited by 62 publications

(47 citation statements)

References 66 publications

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“…NeuA* offers a mechanism to regulate the degree of acetylation by controlling the concentration of O-acetylated sialic acids available for surface modification. In contrast, no O acetylation of sialic acid was reported for the E. coli O145 serotype (14), suggesting that there may be differences in the relative activity of NeuA* or activity of NeuD in some strains. In GBS the relative concentration of O-acetylated monomeric sialic acids is low unless the neuA orthologue is inactivated (24).…”

Section: Discussionmentioning

confidence: 81%

Separate Pathways for O Acetylation of Polymeric and Monomeric Sialic Acids and Identification of Sialyl O -Acetyl Esterase in Escherichia coli K1

et al. 2006

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O acetylation at carbon positions 7 or 9 of the sialic acid residues in the polysialic acid capsule of Escherichia coli K1 is catalyzed by a phase-variable contingency locus, neuO, carried by the K1-specific prophage, CUS-3. Here we describe a novel method for analyzing polymeric sialic acid O acetylation that involves the release of surface sialic acids by endo-N-acetylneuraminidase digestion, followed by fluorescent labeling and detection of quinoxalinone derivatives by chromatography. The results indicated that NeuO is responsible for the majority of capsule modification that takes place in vivo. However, a minor neuO-independent O acetylation pathway was detected that is dependent on the bifunctional polypeptide encoded by neuD. This pathway involves O acetylation of monomeric sialic acid and is regulated by another bifunctional enzyme, NeuA, which includes N-terminal synthetase and C-terminal sialyl O-esterase domains. A homologue of the NeuA C-terminal domain (Pm1710) in Pasteurella multocida was also shown to be an esterase, suggesting that it functions in the catabolism of acetylated environmental sialic acids. Our combined results indicate a previously unexpected complexity in the synthesis and catabolism of microbial sialic and polysialic acids. These findings are key to understanding the biological functions of modified sialic acids in E. coli K1 and other species and may provide new targets for drug or vaccine development.Escherichia coli K1 is a versatile human and animal facultative pathogen that causes a variety of extraintestinal diseases including sepsis, meningitis, cystitis, pyelonephritis, cellulitis, pneumonia, and postoperative infections. The ability of E. coli K1 to invade and traverse the mammalian epithelial cell barrier also may contribute to inflammatory bowel syndromes such as Crohn's disease. A primary virulence determinant in these diseases is the polysialic acid capsule or K1 antigen, a homopolymer of 2-keto-3-deoxy-5-acetamido-7,8,9-D-glycero-D-galacto-nonulosonic, or N-acetylneuraminic acid (Neu5Ac, the most common sialic acid), residues connected by ␣2,8-glycoketosidic linkages (36). The kps and neu genes needed for polysialic acid synthesis and export map to a 17-kb accretion domain inserted near pheV (7). Mutation of neu (biosynthetic) genes generally results in no capsular polysaccharide produced while kps mutations usually result in intracellular accumulation of unexported polysaccharides (46, 47). Polysialic acid is also found on the mammalian neural cell adhesion molecule and comprises the group B meningococcal, Pasteurella haemolytica A2, and Moraxella nonliquefaciens capsular polysaccharides (41). Mammalian polysialic acid regulates cell migration, axon pathfinding and targeting, and plasticity in the embryonic and adult nervous system (6). Molecular mimicry of this antigen by the bacterial capsules is thought to account for the relatively low immunogenicity of microbial polysialic acid, which has limited the attempts to produce safe and effective capsulebased vaccines ...

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Section: Discussionmentioning

confidence: 81%

Separate Pathways for O Acetylation of Polymeric and Monomeric Sialic Acids and Identification of Sialyl O -Acetyl Esterase in Escherichia coli K1

et al. 2006

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“…Further fragmentation products were observed, matching the loss of amino acids or sugar residues. The glycan can be predicted to be composed of N-acetylhexosamine (HexNAc), 2-acetimidoylamino-2,6-dideoxygalactose (FucNAm), and sialic acid (Neu5Ac), matching the O145 O-antigen structure (31). The spectrum is shown with full peptide (MϩH; M refers to peptide, and MϩH is peptide without glycan), and fragmentation derivatives (M ϩ glycan) or glycan fragments ( Fig.…”

Section: Resultsmentioning

confidence: 99%

Serogroup-Specific Bacterial Engineered Glycoproteins as Novel Antigenic Targets for Diagnosis of Shiga Toxin-Producing-Escherichia coli-Associated Hemolytic-Uremic Syndrome

et al. 2015

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Human infection with Shiga toxin-producing Escherichia coli (STEC) is a major cause of postdiarrheal hemolytic-uremic syndrome (HUS), a life-threatening condition characterized by hemolytic anemia, thrombocytopenia, and acute renal failure. E. coli O157:H7 is the dominant STEC serotype associated with HUS worldwide, although non-O157 STEC serogroups can cause a similar disease. The detection of anti-O157 E. coli lipopolysaccharide (LPS) antibodies in combination with stool culture and detection of free fecal Shiga toxin considerably improves the diagnosis of STEC infections. In the present study, we exploited a bacterial glycoengineering technology to develop recombinant glycoproteins consisting of the O157, O145, or O121 polysaccharide attached to a carrier protein as serogroup-specific antigens for the serological diagnosis of STEC-associated HUS. Our results demonstrate that using these antigens in indirect ELISAs (glyco-iELISAs), it is possible to clearly discriminate between STEC O157-, O145-, and O121-infected patients and healthy children, as well as to confirm the diagnosis in HUS patients for whom the classical diagnostic procedures failed. Interestingly, a specific IgM response was detected in almost all the analyzed samples, indicating that it is possible to detect the infection in the early stages of the disease. Additionally, in all the culture-positive HUS patients, the serotype identified by glyco-iELISAs was in accordance with the serotype of the isolated strain, indicating that these antigens are valuable not only for diagnosing HUS caused by the O157, O145, and O121 serogroups but also for serotyping and guiding the subsequent steps to confirm diagnosis. Shiga toxin-producing Escherichia coli (STEC) is an important food-borne pathogen associated with sporadic cases and outbreaks of diarrhea, bloody diarrhea (BD), and hemolytic-uremic syndrome (HUS), a life-threatening condition characterized by microangiopathic hemolytic anemia, thrombocytopenia, and acute renal failure (1). Postdiarrheal HUS is caused by particular serotypes of STEC or, in regions, such as South Asia, by Shigella dysenteriae serotype 1 (2). STEC strains are characterized by the production of Shiga toxin 1 (Stx1) and/or Shiga toxin 2 (Stx2), and the production of these toxins is central in the pathogenesis of BD and HUS (3). E. coli O157:H7 is the dominant STEC serotype associated with sporadic cases and outbreaks of BD and HUS in different parts of the world (4); however, a subset of non-O157:H7 STEC serotypes (O26:H11, O103:H2, O111:NM, O121:H19, O145:NM, and O45:H2, among others) can cause a similar disease (5, 6).STEC-associated HUS is the most common cause of acute renal failure in children worldwide and constitutes 90% of all HUS cases in this population. Five to 10 percent of children with STEC infection develop HUS, for which the only treatment is supportive care. The incidence rate of postdiarrheal HUS varies according to country, and Argentina shows the highest HUS incidence worldwide, with 12 to 14 cases per 100,000 ...

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“…In the first cluster of M. maripaludis N-glycosylation genes, immediately adjacent to aglA, yet transcribed from the opposite strand, is an operon comprising three genes, mmp1081-mmp1083, subsequently renamed aglXYZ (125). These three genes show high sequence similarity to wbuXYZ, E. coli genes implicated in the biosynthesis of 2,6-dideoxy-2-acetamidino-L-galactose, found in the O-antigen (126). In the bacterial system, the three gene products are thought to act in concert, with the glutaminidase WbuY generating ammonia that is delivered to the amidotransferase WbuX via an ammonia tunnel formed by WbuZ.…”

Section: Pathway Of N-linked Glycosylation In Methanogensmentioning

confidence: 99%

N-Linked Glycosylation in Archaea: a Structural, Functional, and Genetic Analysis

Jarrell

Ding

Meyer

et al. 2014

Microbiol Mol Biol Rev

180

214

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SUMMARY N-glycosylation of proteins is one of the most prevalent posttranslational modifications in nature. Accordingly, a pathway with shared commonalities is found in all three domains of life. While excellent model systems have been developed for studying N-glycosylation in both Eukarya and Bacteria , an understanding of this process in Archaea was hampered until recently by a lack of effective molecular tools. However, within the last decade, impressive advances in the study of the archaeal version of this important pathway have been made for halophiles, methanogens, and thermoacidophiles, combining glycan structural information obtained by mass spectrometry with bioinformatic, genetic, biochemical, and enzymatic data. These studies reveal both features shared with the eukaryal and bacterial domains and novel archaeon-specific aspects. Unique features of N-glycosylation in Archaea include the presence of unusual dolichol lipid carriers, the use of a variety of linking sugars that connect the glycan to proteins, the presence of novel sugars as glycan constituents, the presence of two very different N-linked glycans attached to the same protein, and the ability to vary the N-glycan composition under different growth conditions. These advances are the focus of this review, with an emphasis on N-glycosylation pathways in Haloferax , Methanococcus , and Sulfolobus .

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Structural and Genetic Characterization of Enterohemorrhagic Escherichia coli O145 O Antigen and Development of an O145 Serogroup-Specific PCR Assay

Cited by 62 publications

References 66 publications

Separate Pathways for O Acetylation of Polymeric and Monomeric Sialic Acids and Identification of Sialyl O -Acetyl Esterase in Escherichia coli K1

Separate Pathways for O Acetylation of Polymeric and Monomeric Sialic Acids and Identification of Sialyl O -Acetyl Esterase in Escherichia coli K1

Serogroup-Specific Bacterial Engineered Glycoproteins as Novel Antigenic Targets for Diagnosis of Shiga Toxin-Producing-Escherichia coli-Associated Hemolytic-Uremic Syndrome

N-Linked Glycosylation in Archaea: a Structural, Functional, and Genetic Analysis

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