Membrane glycoproteins of human polymorphonuclear leukocytes that act as receptors for mannose-specific Escherichia coli (original) (raw)
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Acta pathologica, microbiologica, et immunologica Scandinavica. Section B, Microbiology, 1985
The influence of culture period on mannose-specific and hydrophobic properties of the bacterial surface and on bacteria/polymorphonuclear leukocyte (PMNL) interaction was studied. Four E. coli strains, PN7 (01:K1), ABU2 (ON:K14), CU9 (06:K14) and CU13 (08:KN) and two Salmonella typhimurium strains 395 MR10 and 395 MS, well characterized according to physicochemical surface properties, presence of type 1 fimbriae and interaction with PMNL, were used in the study. The results show that with prolonged culture period, the liability to hydrophobic interaction increases, the agglutination-strength of mannose-specific maltobionamide liposomes increases, while the agglutination-titer with guinea-pig erythrocytes remains constant. Furthermore, the mannose-specific association with and metabolic activation of PMNL is augmented, while the ingestion is unchanged. In addition, our results demonstrate differences in sensitivity between the methods used to detect exposure of mannose-specific struc...
Infection and Immunity, 1980
Recently, it was suggested that a mannose-specific lectin on the bacterial cell surface is responsible for the recognition by phagocytic cells of certain nonopsonized Escherichia coli strains. In this study we assessed the interaction of two strains of E. coli at different phases of growth with a monolayer of mouse peritoneal macrophages and developed a direct method with [ 14 C]mannan to quantitate the bacterial mannose-binding activity. Normal-sized bacteria were obtained from logarithmic and stationary phases of growth. Nonseptated filamentous cells were formed by growing the organisms in the presence of cephalexin or at a restrictive temperature. Attachment to macrophages of all bacterial forms was inhibited by methyl α- d -mannoside and mannan but not by other sugars tested. The attachment of stationary phase and filamentous bacteria to macrophages, as well as their mannose-binding activity, was similar, whereas in the exponential-phase bacteria they were markedly reduced. The ...
Infection and Immunity, 1991
Attachment of bacteria to phagocytic cells may be mediated by lectin-carbohydrate interactions, resulting in lectinophagocytosis. The best-studied system is the interaction of type 1-fimbriated (mannose-specific) Escherichia coli with human phagocytic cells. Here we demonstrate that the leukocyte integrins CD11 and CD18 (CD11/CD18) constitute the major receptors for type 1-fimbriated E. coli. Bacteria were bound in a dose-dependent and saturable manner to CD11/CD18, which was immobilized to microwells, whereas nonfimbriated E. coli cells failed to bind. The binding was efficiently inhibited (82 to 85%) by methyl-alpha-mannoside but not by galactose, and it was reduced by treatment of the immobilized CD11/CD18 with sodium metaperiodate, endoglycosidase H, or a mixture of endoglycosidase F and N-glycosidase. The fimbriated bacteria also bound to CD11a,b,c and CD18 separated by polyacrylamide gel electrophoresis with sodium dodecyl sulfate and blotted onto nitrocellulose paper. This bi...
Infection and Immunity, 1983
In the present study, we assayed protein iodination in human granulocytes after interaction of the cells with mannose-specific (MS) type 1 fimbriated (MS+) and nonfimbriated (MS-) phenotypes of Escherichia coli pretreated with various amounts of anti-E. coli and antifimbrial antibodies. The MS+ phenotype stimulated protein iodination in granulocytes and possessed potent MS activity as measured by yeast aggregometry. In contrast, the MS- phenotype lacked all these activities. MS+ pretreated with moderate concentrations of antibodies, however, showed up to a 15-fold increase in granulocyte stimulation as compared to granulocyte stimulation induced by the non-antibody-treated MS+ phenotype or by the antibody-treated MS- phenotype. This marked antibody-mediated increase in stimulation of granulocytes was (i) dependent on the antibody concentrations, (ii) markedly reduced by methyl-alpha-D-mannoside, (iii) caused by immunoglobulin G as well as by F(ab')2, (iv) caused only by antifimb...
Journal of Biological Chemistry, 2002
The in vitro binding of the macrophage mannose receptor to a range of different bacterial polysaccharides was investigated. The receptor was shown to bind to purified capsular polysaccharides from Streptococcus pneumoniae and to the lipopolysaccharides, but not capsular polysaccharides, from Klebsiella pneumoniae. Binding was Ca 2؉-dependent and inhibitable with D-mannose. A fusion protein of the mannose receptor containing carbohydrate recognition domains 4-7 and a full-length soluble form of the mannose receptor containing all domains external to the transmembrane region both displayed very similar binding specificities toward bacterial polysaccharides, suggesting that domains 4-7 are sufficient for recognition of these structures. Surprisingly, no direct correlation could be made between polysaccharide structure and binding to the mannose receptor, suggesting that polysaccharide conformation may play an important role in recognition. The full-length soluble form of the mannose receptor was able to bind simultaneously both polysaccharide via the carbohydrate recognition domains and sulfated oligosaccharide via the cysteine-rich domain. The possible involvement of the mannose receptor, either cell surface or soluble, in the innate and adaptive immune responses to bacterial polysaccharides is discussed.
Infection and Immunity, 1988
Uropathogenic strains of Escherichia coli bearing mannose-sensitive (type 1) fimbriae promote a unique pattern of degranulation from human polymorphonuclear leukocytes (PMN). Significant quantities of the primary (1 degree) and tertiary (3 degree) granule markers, neutral protease-myeloperoxidase and N-acetyl-beta-D-glucosaminidase, respectively, were released by PMN in a dose- and time-dependent manner when stimulated by these defined bacterial strains. Organisms bearing mannose-resistant (P) fimbriae promoted release of only the secondary (2 degree) granule marker, vitamin B12-binding protein. When this pattern of degranulation was compared to that produced by PMN in response to a variety of soluble and particulate stimuli, only the calcium ionophore A23187 similarly triggered 1 degree and 3 degree granule marker release. All the other stimuli tested--zymosan, serum-treated and unopsonized; n-formylmethionyl-leucyl-phenylalanine; and phorbol myristate acetate--promoted release of ...
Mannose Binding and Epithelial Cell Adherence of Escherichia coli
Infection and Immunity, 1978
The mannose-binding activity of several isolates of Escherichia coli was monitored by aggregometry with mannan-containing yeast cells. The velocity of yeast cell aggregation was found to correlate with the ability of the organisms to adhere to human epithelial cells. Mannose or its derivatives specifically inhibited or reversed epithelial cell adherence and yeast cell aggregation. Most of the adherent bacteria could be displaced within 30 min from the epithelial cells with methyl α- d -mannopyranoside, but not with other sugars tested. Cultures of E. coli were fractionated into nonadherent and adherent populations by adsorption with epithelial cells followed by elution of the adherent bacteria with methyl α- d -mannopyranoside. When the methyl α- d -mannopyranoside-displaced organisms were washed free of the sugar, they exhibited a high degree of mannose-binding activity and were heavily piliated. In contrast, the nonadherent fraction of organisms lacked detectable mannose-binding a...
European Journal of Biochemistry, 1994
Rat monoclonal antibody MASC1-MR9 (MR9) binds to a mannan of Candida species and the O-antigenic polysaccharides of Salmonella bacteria of serogroups C1 (CO) and E (EO). Mannan and glycoconjugates comprising BSA and O-antigen polysaccharides, decasaccharide-BSA (CO-BSA) or trisaccharide-BSA (EO-BSA), inhibited each other's reactivity with MR9. The saccharides beta-D-Manp-(1-->6)-alpha-D-Manp-1-OMe, beta-D-Manp(1-->3)-alpha-D-Manp-1-OMe, beta-D-Manp(1-->2)-alpha-D-Manp-1-OMe (corresponds to the terminal non-reducing end of Salmonella serogroup C1 O-antigen) and beta-D-Manp(1-->4)-alpha-L-Rhap(1-->3)-alpha-D-Galp-1-O-p-++ +trifluoroacetamido aniline (corresponds to the backbone of Salmonella serogroup E O-antigen) inhibited the binding of MR9 to these antigens whereas alpha-D-Manp(1-->3)-alpha-D-Manp-1-OMe and alpha-D-Manp(1-->4)-alpha-L- Rhap-1-O-p-nitrophenyl did not. Saccharides (3-10 residues) of mammalian origin with terminal and internal Manp alpha-1-->2, Manp alpha-1-->3 and Manp alpha-1-->6 residues also failed to inhibit at any concentration. None of the saccharides with internal beta-mannosyl residue was able to inhibit the MR9 antibody. Monosaccharides D-mannose, beta-D-Manp-1-OMe and 1,5 anhydro-D-mannitol inhibited the MR9 monoclonal antibody whereas alpha-D-Manp-1-OMe, beta-D-Glcp-1-OMe, and beta-D-Galp-1-OMe did not. In addition a Klebsiella K24 capsular polysaccharide containing a beta-D-Manp(1-->4)-alpha-D- GlcA (GlcA, glucuronic acid) as a structural element possessed an inhibitory activity. MR9 therefore recognizes an epitope within beta-mannose monosaccharide residues at the terminal non-reducing ends of carbohydrate chains in mannan, and polysaccharides in Salmonella serogroups CO and EO and Klebsiella K24.