A new locus, pilE, required for the binding of type 1 piliated Escherichia coli to erhythrocytes

Maurer, Lisa M.

doi:10.1016/0378-1097(85)90365-9

Cited by 36 publications

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“…Bacterial agglutination in the presence of antiserum raised against purified type 1 pili and hemagglutination of guinea pig erythrocytes were accomplished as previously described (12). The PilE-phenotype is defined by the failure of mutants to agglutinate guinea pig erythrocytes while maintaining the ability to agglutinate in antipilus antiserum (8).…”

Section: Orn115mentioning

confidence: 99%

“…Recently, it has become evident that while type 1 pili are required for receptor binding, their presence is not sufficient for binding (8). This fact is indicated by the existence of fully piliated mutants that fail to agglutinate guinea pig erythrocytes (8).…”

mentioning

confidence: 99%

“…The receptor-binding function requires, in addition to polymerized pili, the product of the pilE gene (8). The pilE gene product is distinct from pilin (the pilA gene product), which makes up the pilus fiber.…”

mentioning

confidence: 99%

“…For the purpose of experimentation, it is assumed either that the pilE gene product acts as the true adhesive component (adhesin), requiring the pilus only for proper presentation, or that the * Corresponding author. pilE gene product acts indirectly, for example, conferring receptor-binding capacity on the pilin monomer (8,10).…”

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confidence: 99%

“…The pilE locus has been mapped and shown to act in trans (8). However, the gene product has not been observed.…”

mentioning

confidence: 99%

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Identification and characterization of genes determining receptor binding and pilus length of Escherichia coli type 1 pili

Maurer¹,

Orndorff²

1987

J Bacteriol

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121

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We describe the identification and characterization of two genes and their gene products responsible for determining receptor binding and pilus length in type 1-piliated Escherichia coli. One gene, pilE, conferred the ability of piliated cells to agglutinate guinea pig erythrocytes. The other gene, pilF, determined pilus length, in that mutants having lesions in pilF had very long pili. The two genes were detected after TnS mutagenesis of a cloned segment of DNA that normally complemented a pilE lesion in the chromosome. Thus, lesions in pilE or pilF on the cloned segment resulted in mutants having the PilE-phenotype (piliated but unable to agglutinate erythrocytes). Introduction of the plasmid-encoded mutant alleles of pilE and pilF into the chromosome followed by electron microscopic examination of the mutants showed that only lesions in pilF conferred the striking increase in pilus length. Mutations in pilF could be complemented in trans by the original cloned segment to produce cells with parental-length pili. Minicell transcription and translation of the cloned pilE and pilF genes having representative TnS insertion mutations showed that the pilE gene product was a protein of ca. 31 kilodaltons and that the pilF gene product was a protein of ca. 18 kilodaltons. We believe that the pilF gene product may act as a competititve inhibitor of pilus polymerization. Thus, pilus length may be controlled by the ratio of pilin to pilF gene product present within the cell.Type 1 pili of Escherichia coli provide a convenient model for studying the control and assembly of supramolecular extracellular structures. Also, they provide a model for cell-cell interaction, since type 1 pili are required to mediate attachment of E. coli to a variety of eucaryotic cells through a mannose-sensitive interaction with a receptor on the eucaryotic cell (4).One interesting facet of the assembly of type 1 pili concerns how the cell monitors the number of pili it has and how long those pili are. These two considerations would seem to be important for the cell to conserve energy. However, since pili are on the outside of the cell, it is unclear how the cell would keep track of these two parameters. It is apparent from recent work that at least one mechanism exists for controlling the number of pili per cell. This fact is indicated by the existence of hyperpiliated mutants (13). Since hyperpiliated mutants also have longer pili (13), one might infer that the cell has a way to monitor pilus length also. However, no such pilus length mutants have been isolated.Another interesting feature of type 1 pili concerns their involvement in receptor-ligand interactions. Recently, it has become evident that while type 1 pili are required for receptor binding, their presence is not sufficient for binding (8). This fact is indicated by the existence of fully piliated mutants that fail to agglutinate guinea pig erythrocytes (8).

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Section: Orn115mentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

“…The pilE locus has been mapped and shown to act in trans (8). However, the gene product has not been observed.…”

mentioning

confidence: 99%

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Identification and characterization of genes determining receptor binding and pilus length of Escherichia coli type 1 pili

Maurer¹,

Orndorff²

1987

J Bacteriol

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121

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Functional analysis of the minor subunits of S fimbrial adhesin (SfaI) in pathogenic Escherichia coli

et al. 2000

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S fimbrial adhesins I and II (SfaI and II), produced by extraintestinal Escherichia coli pathogens that cause urinary tract infections (UTI) and newborn meningitis (NBM), respectively, mediate bacterial adherence to sialic acid-containing glycoprotein receptors present on host epithelial cells and extracellular matrix. The S fimbrial adhesin complexes consist of four proteins: SfaI-A, the major subunit protein and the minor subunit proteins SfaI-G, SfaI-S and SfaI-H. Sialic acid-specific binding is mediated by the minor subunit protein SfaI-S. In order to determine whether the minor subunit proteins SfaI-G, -S and -H play a role in the modulation of adherence and the degree of fimbriation, a trans-complementation system was developed. A non-adhesive E. coli K-12 derivative, harbouring the sfaI-A gene but lacking sfaI-G, -S and -H, was transformed with sfaI-G, -S or -H. Only SfaI-S was able to increase the degree of fimbriation and to confer adhesion properties on the recombinant E. coli K-12 strains. Amino acid residues in SfaI-S that are involved in modulation of fimbriation as well as in receptor recognition were localized by random and site-directed mutagenesis.

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Bacterial lectins, cell‐cell recognition and infectious disease

1987

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Numerous bacterial strains produce surface lectins, commonly in the form of fimbriae that are filamentous assemblies of protein subunits. Among the best characterized of these are the type 1 (mannose specific) fimbrial lectins of Escherichia coli that consist almost exclusively of one class of subunit with a molecular mass of 17 kDa. They possess an extended combining site corresponding to a trisaccharide and preferentially bind carbohydrate units of oligomannose or hybrid type. Type 1 fimbriae also possess a hydrophobic region close to the carbohydrate-binding site, since aromatic a-mannosides inhibit strongly (up to lOOO-times more than methyl a-mannoside) the agglutination of yeasts by the bacteria and the adherence of the latter to pig ileal epithelial cells. The combining sites of type 1 fimbriae of the salmonellae and of other enteric bacteria are different from those of E. coli in that they are smaller and do not possess a hydrophobic region. The various bacterial surface lectins appear to function primarily in the initiation of infection by mediating bacterial adherence to epithelial cells, e.g. in the urinary and gastrointestinal tracts. The mannose specific lectins also act as recognition molecules in lectinophagocytosis (i.e. phagocytosis of the bacteria in the absence of opsonins) by mouse, rat and human peritoneal macrophages, and human polymorphonuclear leukocytes. Affinity chromatography of membrane lysates from human polymorphonuclear leukocytes on immobilized type 1 fimbrial lectin, using methyl u-mannoside as eluent, showed that glycoproteins with apparent molecular masses of 7&80, 100 and 150 kDa act as receptors for the bacteria. Inhibition experiments with monoclonal antibodies suggest that the glycoprotein bands of 100 and 150 kDa may be identical with the a and /l subunits of leukocyte complement receptors and adhesion glycoproteins involved in complement-mediated opsonophagocytosis. The systems described serve as a fine illustration for the biological role of lectin-carbohydrate interactions. Further studies of these systems will lead to a deeper understanding of the molecular basis of infectious diseases, and perhaps also to new approaches for their prevention.

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A new locus, pilE, required for the binding of type 1 piliated Escherichia coli to erhythrocytes

Cited by 36 publications

References 0 publications

Identification and characterization of genes determining receptor binding and pilus length of Escherichia coli type 1 pili

Identification and characterization of genes determining receptor binding and pilus length of Escherichia coli type 1 pili

Functional analysis of the minor subunits of S fimbrial adhesin (SfaI) in pathogenic Escherichia coli

Bacterial lectins, cell‐cell recognition and infectious disease

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