Structure and serologic properties of O-specific polysaccharide from Citrobacter freundii possessing cross-reactivity with Escherichia coli O157:H7

Nishiuchi, Yukiko

doi:10.1016/s0928-8244(00)00149-8

Cited by 5 publications

(6 citation statements)

References 22 publications

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“…Different studies (3,28,38) showed that 12 to 14% of the serum samples obtained from the rural population were positive for reactivity to the O157 LPS. These results suggest the production of an immune response against the O157 LPS induced by contact with common epitopes shared by these bacteria (22,24,33).…”

Section: Discussionmentioning

confidence: 77%

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Antibody Responses to Escherichia coli O157 and Other Lipopolysaccharides in Healthy Children and Adults

Navarro¹,

Eslava²,

Hernández³

et al. 2003

Clin Vaccine Immunol

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In Mexico, diarrheal disease due to different serotypes of Escherichia coli is highly prevalent, with only sporadic isolation of O157 non-H7 strains. This could be due to exposure to the O157 or related E. coli lipopolysaccharide (LPS), such as O7 or O116, at an early age. By using enzyme-linked immunosorbent assay (ELISA) and Western blotting, the present study analyzed 605 serum samples from Mexican adults and infants without clinical symptoms of disease for the presence of antibodies to these three E. coli LPSs. The bactericidal activities of homologous and heterologous rabbit and human serum samples against O7, O116, and O157 E. coli LPSs were also determined. By using a cutoff point of 0.7, it was found by the ELISAs that 28 of 562 (5%) of the serum samples from adolescents and adults and 2 of 43 (5%) of the serum samples from infants less than 1 year of age reacted with the O157 LPS. By using cutoff points between 0.4 and 0.699, the proportion of serum samples from both age groups that reacted with the O157 LPS increased to 20%. Western blotting analysis of selected serum samples that showed an intermediate response against the O157 LPS by the ELISAs showed that 61 of 88 (69%) reacted with the same LPS. A similar result was observed for maternal milk samples. The bactericidal activities of rabbit serum samples against the O7, O116, and O157 LPSs showed that they were positive for both homologous and heterologous antigens. Similar results were observed with the human serum samples. O157 non-H7 strains were identified in only 10% of the E. coli strains isolated from 263 Mexican children with and without diarrhea over the past 15 years. This absence of O157:H7 strains in Mexico may be associated with the presence of antibodies against O157 or related E. coli LPSs.Enterohemorrhagic Escherichia coli O157:H7 is of great clinical and epidemiological importance as a cause of hemorrhagic colitis (HC) and hemolytic-uremic syndrome (HUS) in developed countries (2, 21, 35). The incidence of these bacteria in Mexico and other developing countries is low, although it has been reported that these bacteria are present in Chile, Brazil, Argentina, and Colombia (12,17,19,20).The presence of antibodies in sera from patients with HUS against the lipopolysaccharide (LPS) of E. coli O157 was reported initially by Notenboom et al. (23). Subsequent studies designed to characterize the immune responses of patients infected with E. coli O157 have reported the presence of immunoglobulin M (IgM) (8), IgG (16), and both IgM and IgG (1) antibodies to O157 LPS in patients with HUS. IgA antibodies have also been reported in the serum and feces of patients with HUS (6, 30). A study carried out by Reymond et al. (28) showed the presence of antibodies to O157 LPS in 12% of the population living in rural areas where O157 strains are endemic, whereas they were found in only 4.7% of the population living in urban areas. Similar results were observed by Belongia et al. (3) in a rural Wisconsin population.Cross-reactivities between the LPS of...

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Section: Discussionmentioning

confidence: 77%

“…It has been proposed that the 4-amino-4,6-dideoxy-␣-D-mannopyranosyl polysaccharide present in the repeated units of the LPS side chain could be an antigenic determinant related to the immune response (22,26).…”

Section: Discussionmentioning

confidence: 99%

Antibody Responses to Escherichia coli O157 and Other Lipopolysaccharides in Healthy Children and Adults

Navarro¹,

Eslava²,

Hernández³

et al. 2003

Clin Vaccine Immunol

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“…Several isolates of C. freundii E9750 displayed cross-reactivity in agglutination tests with the anti-O serum of S. senftenberg 74210, which suggests changes in the conformation of the epitopes that may be associated with the addition of glucosyl groups or residues derived from N-acetyl [46]. The isolates of C. freundii E9750 that display variability suggest heterogeneity in the composition or conformation of the epitopes of the O antigen.…”

Section: Intra-species Variability In the Composition Of The O Antigenmentioning

confidence: 99%

Mechanisms of O-Antigen Structural Variation of Bacterial Lipopolysaccharide (LPS)

Reyes¹,

González²,

Jiménez³

et al. 2012

The Complex World of Polysaccharides

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“…This decreased adherence of rough strains or blocking of adherence using the free lipooligosaccharide (LOS)/ lipopolysaccharide (LPS) in both cell-based and animal infection models has been noted in a range of Gram-negative bacteria including Campylobacter jejuni, Haemophilus influenzae, Salmonella typhi, Salmonella enterica serovar Typhimurium, E. coli, Shigella flexneri, Pseudomonas aeruginosa, and Serratia marcescens (10,(12)(13)(14)(15)(16)(17)(18)(19)(20). Blocking of surface glycans with antibodies has also been shown to inhibit adherence and invasion of cell layers in a range of bacteria, including S. flexneri (21)(22)(23). The cellular receptors for adherence via these bacterial surface glycans have not been identified.…”

mentioning

confidence: 99%

Glycan:glycan interactions: High affinity biomolecular interactions that can mediate binding of pathogenic bacteria to host cells

Day

Tran

Semchenko

et al. 2015

Proc. Natl. Acad. Sci. U.S.A.

100

104

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Cells from all domains of life express glycan structures attached to lipids and proteins on their surface, called glycoconjugates. Cell-tocell contact mediated by glycan:glycan interactions have been considered to be low-affinity interactions that precede highaffinity protein-glycan or protein-protein interactions. In several pathogenic bacteria, truncation of surface glycans, lipooligosaccharide (LOS), or lipopolysaccharide (LPS) have been reported to significantly reduce bacterial adherence to host cells. Here, we show that the saccharide component of LOS/LPS have direct, high-affinity interactions with host glycans. Glycan microarrays reveal that LOS/LPS of four distinct bacterial pathogens bind to numerous host glycan structures. Surface plasmon resonance was used to determine the affinity of these interactions and revealed 66 high-affinity host-glycan:bacterial-glycan pairs with equilibrium dissociation constants (K D ) ranging between 100 nM and 50 μM. These glycan:glycan affinity values are similar to those reported for lectins or antibodies with glycans. Cell assays demonstrated that glycan:glycan interaction-mediated bacterial adherence could be competitively inhibited by either host cell or bacterial glycans. This is the first report to our knowledge of high affinity glycan:glycan interactions between bacterial pathogens and the host. The discovery of large numbers of glycan:glycan interactions between a diverse range of structures suggests that these interactions may be important in all biological systems.H ost surface glycosylation is ubiquitous and is targeted by pathogenic bacteria, viruses, fungi and parasites for adherence and toxin binding and by glycosidases (1). Escherichia coli type 1 fimbriae, FimH, is one of the most widely studied glycanrecognizing protein adhesins, with specificity for monomannose to oligomannose structures with the variability of the mannose structure bound leading to different tissue tropism (2). Other glycan-recognizing adhesins expressed by bacteria include the following: Pseudomonas aeruginosa lectins 1 and 2 (PA-IL and PA-IIL) that have specificity for galactose and fucose, respectively (3); Helicobacter pylori SabA, specific for sialic acid containing glycoconjugates including sialyLewis X; and BabAspecific for fucosylated glycoconjugates including Lewis B (4, 5). Although there are numerous known glycan binding adhesins, the adhesins of some bacteria that interact with host surface glycans remain unknown.Direct interactions between surface glycans (glycan:glycan interactions) have been reported in sea sponges as heterogenous glycan interactions, and in mouse embryo development and cancer where homodimers of Lewis X (LeX) or ganglioside structures play a role in cell adhesion and growth factor receptor interactions (6, 7). Outside of these reports, glycan:glycan interactions, when noted, have generally been considered to be low-affinity, weak interactions (8) that precede high-affinity protein:glycan or protein:protein interactions (1, 2, 5, 9).Interestingly, there...

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Structure and serologic properties of O-specific polysaccharide from Citrobacter freundii possessing cross-reactivity with Escherichia coli O157:H7

Cited by 5 publications

References 22 publications

Antibody Responses to Escherichia coli O157 and Other Lipopolysaccharides in Healthy Children and Adults

Antibody Responses to Escherichia coli O157 and Other Lipopolysaccharides in Healthy Children and Adults

Mechanisms of O-Antigen Structural Variation of Bacterial Lipopolysaccharide (LPS)

Glycan:glycan interactions: High affinity biomolecular interactions that can mediate binding of pathogenic bacteria to host cells

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