Structural studies of the O-antigenic polysaccharide of Escherichia coli O86, which possesses blood-group B activity

Andersson, Mats; Carlin, Nils; Leontein, Karin; Lindquist, Ulf; Slettengren, Kerstin

doi:10.1016/0008-6215(89)80036-9

Cited by 64 publications

(32 citation statements)

References 17 publications

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“…14 The complete structure of the O-polysaccharide from serogroup O86:H2 was elucidated and confirmed the presence of blood group B antigen epitope in O-repeating unit. 15 In this work, we report a new O-polysaccharide structure obtained from E. coli O86:K62:B7 (abbreviated as B7), which is different from the published structure. Interestingly, comparison of these two structures showed that they are derived from the same O-repeating unit via different polymerization sites on different sugar residues (Fig.…”

Section: Introductionmentioning

confidence: 79%

“…Then, 2% polyvinylpyrrolidone (PVP) in PBS buffer was used to block nonspecific binding for 3 h. The anti-B antibody described above was used in series dilution. ELISA end-point titers were determined as described, 15 employing a secondary antibody goat anti-mouse IgM conjugated to HRP (1:1000) (Sigma). The peroxidase substrate (3,3 0 ,5,5 0 -tetramethylbenzidine, Sigma) was used to develop the signal, which was monitored at 405 nm.…”

Section: Elisa Of Lps With Anti-b Antibodymentioning

confidence: 99%

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Two different O-polysaccharides from Escherichia coli O86 are produced by different polymerization of the same O-repeating unit

Yi¹,

Bystrický²,

Yao³

et al. 2006

Carbohydrate Research

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Section: Introductionmentioning

confidence: 79%

Section: Elisa Of Lps With Anti-b Antibodymentioning

confidence: 99%

Two different O-polysaccharides from Escherichia coli O86 are produced by different polymerization of the same O-repeating unit

Yi¹,

Bystrický²,

Yao³

et al. 2006

Carbohydrate Research

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“…Bacteria could be an important target for such an Ab (eg, see Muschel 35 ). Indeed, the presence of carbohydrate substances on bacteria 36,37 or other antigenic carriers entering the gut is after all the main suspected reason for the initial development in neonates of ABO Ab, as well as Ab against Gal␣1-3Gal. 19,20 In addition, severe viral diseases have been implicated in this regard (eg, small pox).…”

Section: Discussionmentioning

confidence: 99%

Expression of ABO or related antigenic carbohydrates on viral envelopes leads to neutralization in the presence of serum containing specific natural antibodies and complement

Preece

Strahan

Devitt

et al. 2002

Blood

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No definitive biologic function has been associated with the human ABO histoblood group polymorphism, or any other terminal carbohydrate differences within or between closely related species. We have experimentally addressed the question of whether viral particles can become glycosylated as determined by the glycosylation (eg, ABO) status of the producer cell and as a result be affected by human serum containing specific natural antibodies (NAbs). Measles virus was produced in cells transfected with cDNA encoding, either human A-transferase, B-transferase, an inactive "O-transferase," or a pig ␣1-3galactosyltransferase (␣1-3GT) synthesizing the Gal␣1-3Gal structure. The viruses were shown to carry the same ABO structures as the cells; that is, A but not B if produced in A-type cells, and B but not A if produced in B-type cells. Only O was detected on the virus produced from O-type cells, whereas reduced amounts of O appeared on the Aand B-type viral particles. In addition, the Gal␣1-3Gal structure was transferred onto measles only when grown in human cells expressing this structure. When subjected to human preimmune sera, the A-type, the B-type, and the Gal␣1-3Gal viral particles were partially neutralized in a complement-dependent manner. However, the O-type or the Gal␣1-3Gal-negative viral particles were not neutralized. The neutralization appeared to be mediated by specific NAb, as judged by specific inhibition using synthetic A and IntroductionThe ABO (or ABH) histo-blood group system is characterized by the expression of polymorphic carbohydrate termini on several cell types. The genetic basis for this polymorphism in humans is explained by the existence of allelic forms of a single gene encoding glycosyltransferases with specificity for different monosaccharides. 1 They appear to be evolutionarily old, being present on glycosylated structures in different eukaryotic as well as prokaryotic organisms, and established their present day polymorphic form in humans at the latest during early primate evolution (for a review, see Blancher et al 2 ). Hence, it would be surprising if the ABO structures did not serve an important purpose. No definitive biologic function has, however, as yet been identified, 3 although suggestions have often centered on immunologic explanations. [4][5][6][7] Another very similar terminal carbohydrate structure, the Gal␣1-3Gal␤1-4GlcNAc-R (referred to as Gal␣1-3Gal) is present in other mammals but not in humans and other Old World primates. 8 Bacteria mimicking vertebrate terminal carbohydrates may have given rise to selection pressures favoring polymorphic glycans. 9 In addition, many pathogens and their toxins bind to specific terminal carbohydrate structures and may consequently produce selection pressures affecting the evolution of terminal carbohydrate structures. 7,10 It has also been previously suggested that viruses may carry ABO structures as part of their envelope 11,12 and consequently serve as potential selective forces influencing ABO genotype frequencies in a population....

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“…LPS consists of a hydrophobic domain known as lipid A anchored in the membrane, a polysaccharide (O-antigen) made of repetitive subunits of one to eight sugars and a "core" oligosaccharide at the junction between the two other regions [111]. The Oantigens, being at the outermost cell surface, are at the interface between the bacterium and its environment, and are important virulence factors and antigens for many pathogenic bacteria [112]. Many bacteria are subclassified by the O-antigen on their surface [113].…”

Section: Lectin-based Biosensors For Detecting Carbohydratesmentioning

confidence: 99%

Carbohydrate–protein interactions and their biosensing applications

Zeng

Andrade²,

Oliveira³

et al. 2011

Anal Bioanal Chem

105

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Carbohydrate recognition is clearly present throughout nature, playing a major role in the initial attachment of one biological entity to another. The important question is whether these prevalent interactions could provide a real suitable alternative to the use of antibodies or nucleic acid for detection and identification. Currently, examples of carbohydrates being employed in biological detection systems are limited. The challenges of using carbohydrate recognition for detection mainly come from the weak affinity of carbohydrate-protein interactions, the lack of versatile carbohydrate scaffolds with well-defined structures, and the less developed high-information-content, real-time, and label-free assay technology. In this review, we focus on discussing the characteristics of carbohydrate-protein interactions in nature and the methods for carbohydrate immobilization based on surface coupling chemistry in terms of their general applicability for developing carbohydrate- and lectin-based label-free sensors. Furthermore, examples of innovative design of multivalent carbohydrate-protein interactions for sensor applications are given. We limit our review to show the feasibility of carbohydrate and lectin as recognition elements for label-free sensor development in several representative cases to formulate a flexible platform for their use as recognition elements for real-world biosensor applications.

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Structural studies of the O-antigenic polysaccharide of Escherichia coli O86, which possesses blood-group B activity

Cited by 64 publications

References 17 publications

Two different O-polysaccharides from Escherichia coli O86 are produced by different polymerization of the same O-repeating unit

Two different O-polysaccharides from Escherichia coli O86 are produced by different polymerization of the same O-repeating unit

Expression of ABO or related antigenic carbohydrates on viral envelopes leads to neutralization in the presence of serum containing specific natural antibodies and complement

Carbohydrate–protein interactions and their biosensing applications

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