P-fimbriae of Escherichia coli: immuno- and protein-chemical characterization of fimbriae from two pyelonephritogenic strains [PDF]
FEMS Microbiology Letters, 1983 Many types of fimbriae have been described on pathogenic Escherichia coli strains. K88, K99, C F A / I and C F A / I I are fimbrial antigens on enterotoxigenic E. coli strains. The K88 antigens are found on strains causing diarrhoea in piglets [1], whereas strains with the K99 antigen cause diarrhoea in calves and lambs [2].
Mikael Rhen +5 more
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Protein interaction studies of curli fimbriae in Escherichia coli biofilms [PDF]
Bioinformation, 2019 Catheter-associated urinary tract infections (CAUTIs) caused by biofilms on indwelling medical devices are the most common type of nosocomial infections, a major health concern due to complications and frequent recurrence. The infections are most often caused by Escherichia coli.
Iyer, Maithreyi Suresh +2 more
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Microorganisms, 2021 Background. Urinary tract infections (UTIs) are a public health problem in Mexico, and uropathogenic Escherichia coli (UPEC) is one of the main etiological agents. Flagella, type I fimbriae, and curli promote the ability of these bacteria to successfully
Rubí Vega-Hernández +9 more
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Porphyromonas gingivalis fimbriae induce a 68-kilodalton phosphorylated protein in macrophages [PDF]
Infection and Immunity, 1994 The present study was performed to examine whether Porphyromonas gingivalis fimbriae induce specifically a protein kinase-mediated phosphorylated protein that is involved in the mechanism of signal transduction. The fimbriae induced a 68-kDa phosphorylated protein (pp68) in a dose-dependent manner in mouse peritoneal macrophages. A marked appearance of
Y, Murakami +6 more
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Fimbria-associated proteins of Bacteroides loescheii PK1295 mediate intergeneric coaggregations [PDF]
Journal of Bacteriology, 1987 Bacteroides loescheii PK1295 serves as a coaggregation bridge between Streptococcus sanguis 34 and Actinomyces israelii PK14, two gram-positive oral bacteria that are otherwise unable to coaggregate. Whereas coaggregation with S. sanguis 34 is inhibited by lactose, no simple sugar was found that inhibited coaggregation with A.
E I, Weiss +4 more
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Identification of major and minor chaperone proteins involved in the export of 987P fimbriae [PDF]
Journal of Bacteriology, 1996 The 987P fimbriae of Escherichia coli consist mainly of the major subunit, FasA, and two minor subunits, FasF and FasG. In addition to the previously characterized outer membrane or usher protein FasD, the FasB, FasC, and FasE proteins are required for fimbriation.
R A, Edwards, J, Cao, D M, Schifferli
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Isolation and characterization of Bacteroides nodosus fimbriae: structural subunit and basal protein antigens [PDF]
Journal of Bacteriology, 1984 We examined the isolation of fimbriae from Bacteroides nodosus. It was found that the best preparations were obtained from the supernatant of washed cells cultured on solid medium, from which fimbriae could be recovered in high yield and purity by a simple one-step procedure.
J S, Mattick +3 more
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Histone H1 Proteins Act As Receptors for the 987P Fimbriae of Enterotoxigenic Escherichia coli [PDF]
Journal of Biological Chemistry, 2005 The tip adhesin FasG of the 987P fimbriae of enterotoxigenic Escherichia coli mediates two distinct adhesive interactions with brush border molecules of the intestinal epithelial cells of neonatal piglets. First, FasG attaches strongly to sulfatide with hydroxylated fatty acyl chains.
Guoqiang, Zhu +4 more
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Interactions of Streptococcus mutans Fimbria-Associated Surface Proteins with Salivary Components [PDF]
Clinical Diagnostic Laboratory Immunology, 1999 ABSTRACT Streptococcus mutans has been implicated as the major causative agent of human dental caries. S. mutans binds to saliva-coated tooth surfaces, and previous studies suggested that fimbriae may play a role in the initial bacterial adherence to salivary components.
C A, Ray +3 more
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Active sites of salivary proline-rich protein for binding to Porphyromonas gingivalis fimbriae [PDF]
Infection and Immunity, 1997 Porphyromonas gingivalis fimbriae specifically bind salivary acidic proline-rich protein 1 (PRP1) through protein-protein interactions. The binding domains of fimbrillin (a subunit of fimbriae) for PRP1 were analyzed previously (A. Amano, A. Sharma, J.-Y. Lee, H. T. Sojar, P. A. Raj, and R. J. Genco, Infect. Immun. 64:1631-1637, 1996).
K, Kataoka +5 more
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