Escherichia Coli Serotypes and Renal Involvement in Urinary-Tract Infection

Mabeck, Carl Erik; Ørskov, Frits; Ørskov, Ida

doi:10.1016/s0140-6736(71)91884-8

Cited by 86 publications

(44 citation statements)

References 7 publications

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“…As we know that 0 16: K 1 strains can be found in Denmark (data not published), we can only guess if this difference is based on an unexplained different prevalence in the intestine of the general population or if the US 016: K1 serotypes carry special virulence factors. When discussing serotype distribution in different geographical locations, one could mention that Mabeck, 0rskov & 0rskov (1971 a), who examined UTI strains in a certain area, found unexplained changes in the prevalence of the serotype 02: K 1: H4 over a three year period.…”

Section: Bacteraemiamentioning

confidence: 99%

Escherichia coliin extra-intestinal infections

Ørskov

1985

J. Hyg.

220

161

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When Theodor Escherich (1885a, b) first describedEscherichia colihe looked on it as a saprophytic organism. Soon several investigators found that colibacteria could be isolated from intestinal infections and from many infections outside the intestine, like urinary tract infections (UTI), cholecystitis, wound infections, meningitis, septicaemia, pulmonary infections, and many more. Uhlenhuth (1897) showed that coli strains from pathological processes were more pathogenic in animal experiments than strains isolated from the normal intestine. Smith (1927), who examined strains from white scours in calves, showed that spontaneous acapsular mutants could be obtained from certain colibacteria, and that such mutants were less virulent when injected intra-peritoneally into guinea-pigs.

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Section: Bacteraemiamentioning

confidence: 99%

Escherichia coliin extra-intestinal infections

Ørskov

1985

J. Hyg.

220

161

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“…The fljB gene is in a fifth gene cluster, not known to occur in E. coli, that contains only fljB and fljA (32). fljB and fljA are coexpressed, with fljA encoding a repressor of fliC, thus ensuring that only one flagellin gene is expressed at any time (35,36).The single H antigen of E. coli K-12 is encoded at the fliC locus, and until recently this was thought to apply to all 53 forms (16,17,27). However, Ratiner (27) showed that some H-antigen genes are at loci other than fliC, although none have yet been found at fljB.…”

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Species-Wide Variation in the Escherichia coli Flagellin (H-Antigen) Gene

et al. 2003

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Escherichia coli is a clonal species. The best-understood components of its clonal variation are the flagellar (H) and polysaccharide (O) antigens, both well documented since the mid-1930s because of their use in serotyping. Flagellin is the protein subunit of the flagellum that carries H-antigen specificity. We show that 43 of the 54 H-antigen specificities of E. coli map to the flagellin gene at fliC and sequenced all 43 forms and confirmed specificity of each by cloning and expression. This is, to our knowledge, the first time that all known forms of such a highly polymorphic gene have been fully sequenced and characterized for any species. The established distinction between a highly variable central region and more conserved flanking regions is upheld. The sequences fall into two groups, one of which may be derived from the fliC gene of the E. coli/Salmonella enterica common ancestor, the other perhaps obtained by lateral transfer since species divergence. Comparison of sequences revealed that both horizontal DNA transfer and fixation of mutations under diversifying selection pressure contributed to polymorphism in this locus.The O polysaccharide and flagellin are the two major antigens of gram-negative bacteria, also known respectivly as the O and H antigens. Both are highly polymorphic, and Escherichia coli, if one includes the Shigella strains, has 187 O and 53 H forms defined by serology (4,6,15,21). In this study, we show that 43 of the 53 H forms map to the fliC locus and have sequenced all 43 alleles. In some strains the H-antigen phenotype maps to alternative loci, so we cloned, sequenced, and expressed the fliC gene from type strains to relate definitively H-antigen specificity and sequence. These data supplement the genome sequence data of E. coli K-12 and O157:H7 to give more comprehensive genetic information on the species and, in conjunction with the recently published structure (31) of one flagellin form, will allow analysis of the structural basis of the antigenic variation and development of a molecular typing scheme for the H antigen.The bacterial flagellum projects well beyond the surface of the cell and is rotated to provide motive power. The flagellar filament is composed of a single protein, flagellin. The flagellin proteins of E. coli and several other species are conserved in their terminal regions, while the central region is variable and carries H-serotype-specific epitopes (9,17,22,39,40). The structure of the Salmonella enterica LT2 flagellum is known from electron microscopy, X-ray fiber diffraction, and X-ray crystallography. Three domains are recognized (Fig. 1). The conserved terminal segments form the D1 domain located in the center of the flagellum, while the central region of the protein forms two domains (D2 and D3) exposed on the surface (31). The boundaries between D1 and D2 correspond quite well to the boundaries between the central and terminal regions of the protein as determined by alignment of sequences of different forms. However, because we are dealing mostly with...

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“…E. coli isolated from the urine of patients with pyelonephritis contain especially large amounts of capsular antigen (6)(7)(8), and certain capsular serotypes, most notably Kl, predominate in these patients and in infants with E. coli meningitis (6,(9)(10)(11).…”

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Influence of the Escherichia coli capsule on complement fixation and on phagocytosis and killing by human phagocytes.

Horwitz¹,

Silverstein²

1980

J. Clin. Invest.

248

146

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A B S T R A C T To define mechanisms by which polysaccharide capsules confer enhanced virulence on gram-negative bacteria, we examined the effect of the Escherichia coli capsule on complement fixation to the bacterial surface and on phagocytosis and killing of these bacteria by mouse macrophages and human polymorphonuclear leukocytes (PMN) 82IgG, PMN and monocytes required complement to effectively phagocytose and kill the E. coli. We conclude that (a) attachment by itself results in ingestion of unencapsulated but not encapsulated E. coli; (b) under physiologic conditions, E. coli are not phagocytosed or killed effectively by PMN or monocytes unless complement is fixed to their surface; (c) in the absence of antibody, the E. coli capsule blocks complement fixation to the bacterial surface probably by masking surface components, such as lipopolysaccharide, capable of activating the complement pathway; (d) the E. coli capsule imposes a requirement for specific antibacterial antibody for complement fixation; and (e) the complement receptor of human PMN and monocytes mediates phagocytosis of complement-coated encapsulated bacteria and is the primary mediator of phagocytosis and killing of these bacteria.

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Escherichia Coli Serotypes and Renal Involvement in Urinary-Tract Infection

Cited by 86 publications

References 7 publications

Escherichia coliin extra-intestinal infections

Escherichia coliin extra-intestinal infections

Species-Wide Variation in the Escherichia coli Flagellin (H-Antigen) Gene

Influence of the Escherichia coli capsule on complement fixation and on phagocytosis and killing by human phagocytes.

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