Characterization of a Salmonella choleraesuis mutant that cannot multiply within epithelial cells

1991 ◽  
Vol 37 (7) ◽  
pp. 568-572 ◽  
Author(s):  
B. Brett Finlay ◽  
Steve Chatfield ◽  
Ka Yin Leung ◽  
Gordon Dougan ◽  
Stanley Falkow
Keyword(s):  
Epithelial Cell ◽  
Epithelial Cells ◽  
Anaerobic Growth ◽  
Eukaryotic Cells ◽  
Perinuclear Region ◽  
Salmonella Choleraesuis ◽  
Membrane Bound ◽  
Intracellular Multiplication ◽  
Minimal Media

A mutant of Salmonella choleraesuis was identified that could invade (enter) and penetrate through polarized monolayers of Caco-2 and MDCK epithelial cells at normal levels but was defective for intracellular multiplication within these cells. It was also able to survive inside cultured J774 macrophage cells. These bacteria remained inside membrane-bound vacuoles, which coalesced at later times in the perinuclear region of the epithelial cell. This mutant exhibited slightly slower growth rates in rich or minimal media than the parental strain but was normal for iron usage, phosphate usage, and anaerobic growth and was a prototroph. The mutant was completely avirulent when administered orally or intravenously to susceptible mice. These results suggest that the ability to multiply within eukaryotic cells may contribute to S. choleraesuis virulence. Key words: Salmonella choleraesuis, virulence, pathogenesis, intracellular, multiplication.

Intranuclear Crystals in Regenerating Canine Kidneys

1973 ◽  
Vol 31 ◽  
pp. 412-413
Author(s):  
D.G. Osborne ◽  
L.J. McCormack ◽  
M.O. Magnusson ◽  
W.S. Kiser
Keyword(s):  
Epithelial Cell ◽  
Epithelial Cells ◽  
Tubular Epithelial Cell ◽  
Tubular Epithelial Cells ◽  
Cell Nuclei ◽  
Crystalline Structures ◽  
Small Crystals ◽  
Membrane Bound

During a project in which regenerative changes were studied in autotransplanted canine kidneys, intranuclear crystals were seen in a small number of tubular epithelial cells. These crystalline structures were seen in the control specimens and also in regenerating specimens; the main differences being in size and number of them. The control specimens showed a few tubular epithelial cell nuclei almost completely occupied by large crystals that were not membrane bound. Subsequent follow-up biopsies of the same kidneys contained similar intranuclear crystals but of a much smaller size. Some of these nuclei contained several small crystals. The small crystals occurred at one week following transplantation and were seen even four weeks following transplantation. As time passed, the small crystals appeared to fuse to form larger crystals.

scholarly journals Interaction of an Outer Membrane Protein of Enterotoxigenic Escherichia coli with Cell Surface Heparan Sulfate Proteoglycans

2002 ◽  
Vol 70 (3) ◽  
pp. 1530-1537 ◽  
Author(s):  
James M. Fleckenstein ◽  
James T. Holland ◽  
David L. Hasty
Keyword(s):  
Escherichia Coli ◽  
Epithelial Cell ◽  
Epithelial Cells ◽  
Cell Surface ◽  
Heparan Sulfate ◽  
Heparan Sulfate Proteoglycans ◽  
Eukaryotic Cells ◽  
Heparin Binding ◽  
Wild Type ◽  
E Coli

ABSTRACT We have previously shown that enterotoxigenic invasion protein A (Tia), a 25-kDa outer membrane protein encoded on an apparent pathogenicity island of enterotoxigenic Escherichia coli (ETEC) strain H10407, mediates attachment to and invasion into cultured human gastrointestinal epithelial cells. The epithelial cell receptor(s) for Tia has not been identified. Here we show that Tia interacts with cell surface heparan sulfate proteoglycans. Recombinant E. coli expressing Tia mediated invasion into wild-type epithelial cell lines but not invasion into proteoglycan-deficient cells. Furthermore, wild-type eukaryotic cells, but not proteoglycan-deficient eukaryotic cells, attached to immobilized polyhistidine-tagged recombinant Tia (rTia). Binding of epithelial cells to immobilized rTia was inhibited by exogenous heparan sulfate glycosaminoglycans but not by hyaluronic acid, dermatan sulfate, or chondroitin sulfate. Similarly, pretreatment of eukaryotic cells with heparinase I, but not pretreatment of eukaryotic cells with chrondroitinase ABC, inhibited attachment to rTia. In addition, we also observed heparin binding to both immobilized rTia and recombinant E. coli expressing Tia. Heparin binding was inhibited by a synthetic peptide representing a surface loop of Tia, as well as by antibodies directed against this peptide. Additional studies indicated that Tia, as a prokaryotic heparin binding protein, may also interact via sulfated proteoglycan molecular bridges with a number of mammalian heparan sulfate binding proteins. These findings suggest that the binding of Tia to host epithelial cells is mediated at least in part through heparan sulfate proteoglycans and that ETEC belongs on the growing list of pathogens that utilize these ubiquitous cell surface molecules as receptors.

scholarly journals BgaA acts as an adhesin to mediate attachment of some pneumococcal strains to human epithelial cells

Microbiology ◽  
2011 ◽  
Vol 157 (8) ◽  
pp. 2369-2381 ◽  
Author(s):  
Dominique H. Limoli ◽  
Julie A. Sladek ◽  
Lindsey A. Fuller ◽  
Anirudh K. Singh ◽  
Samantha J. King
Keyword(s):  
Epithelial Cell ◽  
Epithelial Cells ◽  
Cell Receptor ◽  
Host Cells ◽  
Bacterial Binding ◽  
Human Epithelial Cells ◽  
Adherence Mechanism ◽  
Epithelial Cell Surface

Streptococcus pneumoniae colonization of the respiratory tract is an essential precursor for pneumococcal disease. To colonize efficiently, bacteria must adhere to the epithelial-cell surface. S. pneumoniae possesses surface-associated exoglycosidases that are capable of sequentially deglycosylating human glycans. Two exoglycosidases, neuraminidase (NanA) and β-galactosidase (BgaA), have previously been shown to contribute to S. pneumoniae adherence to human epithelial cells, as deletion of either of these genes results in reduced adherence. It has been suggested that these enzymes may modulate adherence by cleaving sugars to reveal a receptor on host cells. Pretreatment of epithelial cells with exogenous neuraminidase restores the adherence of a nanA mutant, whereas pretreatment with β-galactosidase does not restore the adherence of a bgaA mutant. These data suggest that BgaA may not function to reveal a receptor, and implicate an alternative role for BgaA in adherence. Here we demonstrate that β-galactosidase activity is not required for BgaA-mediated adherence. Addition of recombinant BgaA (rBgaA) to adherence assays and pretreatment of epithelial cells with rBgaA both significantly reduced the level of adherence of the parental strain, but not the BgaA mutant. One possible explanation of these data is that BgaA is acting as an adhesin and that rBgaA is binding to the receptor, preventing bacterial binding. A bead-binding assay demonstrated that BgaA can bind directly to human epithelial cells, supporting the hypothesis that BgaA is an adhesin. Preliminary characterization of the epithelial-cell receptor suggests that it is a glycan in the context of a glycosphingolipid. To further establish the relevance of this adherence mechanism, we demonstrated that BgaA-mediated adherence contributed to adherence of a recent clinical isolate to primary human epithelial cells. Together, these data suggest a novel role for BgaA as an adhesin and suggest that this mechanism could contribute to adherence of at least some pneumococcal strains in vivo.

scholarly journals Menaquinone (Vitamin K2) Biosynthesis: Localization and Characterization of the menA Gene fromEscherichia coli

1998 ◽  
Vol 180 (10) ◽  
pp. 2782-2787 ◽  
Author(s):  
K. Suvarna ◽  
D. Stevenson ◽  
R. Meganathan ◽  
M. E. S. Hudspeth
Keyword(s):  
High Performance ◽  
Promoter Sequence ◽  
Anaerobic Growth ◽  
Gene Encoding ◽  
Reading Frame ◽  
Chromatography Analysis ◽  
Naphthoic Acid ◽  
Membrane Bound ◽  
Carbon Side Chain

ABSTRACT A key reaction in the biosynthesis of menaquinone involves the conversion of the soluble bicyclic naphthalenoid compound 1,4-dihydroxy-2-naphthoic acid (DHNA) to the membrane-bound demethylmenaquinone. The enzyme catalyzing this reaction, DHNA-octaprenyltransferase, attaches a 40-carbon side chain to DHNA. The menA gene encoding this enzyme has been cloned and localized to a 2.0-kb region of the Escherichia coli genome between cytR and glpK. DNA sequence analysis of the cloned insert revealed a 308-codon open reading frame (ORF), which by deletion analyses was shown to restore anaerobic growth of amenA mutant. Reverse-phase high-performance liquid chromatography analysis of quinones extracted from theorf-complemented cells independently confirmed the restoration of menaquinone biosynthesis, and similarly, analyses of isolated cell membranes for DHNA octaprenyltransferase activity confirmed the introduction of the menA product into theorf-complemented menA mutant. The validity of an ORF-associated putative promoter sequence was confirmed by primer extension analyses.

scholarly journals The Characterization of Haemaglutinin Protein of Vili Vibrio alginolyticus as Adhesion Molecule on Epithelial Cells Receptor of Humpback Grouper (Cromileptes altivelis)

2007 ◽  
Vol 2 (1) ◽  
Author(s):  
Uun Yanuhar
Keyword(s):  
Epithelial Cell ◽  
Epithelial Cells ◽  
Adhesion Molecule ◽  
Vibrio Alginolyticus ◽  
Crucial Problem ◽  
Adhesion Pattern ◽  
Attachment Process

Vibriosis was a crucial problem and a primer infection causing mortality of humpback grouper.Virulence factor of vibrio, such as vili, is an adhesion molecule protein based on haemaglutination test toblood serum of humpback grouper. This research was aimed to characterize an adhesion molecule of viliprotein of V. alginolyticus on epithelial cells of Humpback grouper as haemaglutinin protein. Themethods are laboratory exploration by isolate epithelial cells of Humpback grouper, characterize a receptorand test vili protein to adhesion molecule that is epithelial cell of Humpback grouper. The result of proteinhaemaglutinin test to vili V. alginolyticus show that an adhesion molecule with a molecule weight of38.98 kDa is an adhesin vili V. alginolyticus and a haemaglutinin. The adhesion pattern of V.alginolyticus on epithelial cells of Humpback grouper exposed to protein haemaglutinin of vili show bothdiffuse and localize pattern. Research conclusion was the haemaglutinin protein of vili V. alginolyticuswas an adhesin having a role to both virulence process of bacteria and attachment process to receptor ofepithelial cells of Humpback grouper.Keywords: adhesion molecule, epithelial cell, vili, V. alginolyticus, C. altivelis

Enrichment and characterization of clonogenic epithelial cells from adult rat liver and initiation of epithelial cell strains

1987 ◽  
Vol 23 (5) ◽  
pp. 339-348 ◽  
Author(s):  
Kazunori Furukawa ◽  
Tomiko Shimada ◽  
Patricia England ◽  
Yohichi Mochizuki ◽  
Gary M. Williams
Keyword(s):  
Epithelial Cell ◽  
Epithelial Cells ◽  
Rat Liver ◽  
Adult Rat ◽  
Cell Strains

Electron Microscopic Study of the Epithelium of the Seminal Vesicle of Aging Rats

1974 ◽  
Vol 32 ◽  
pp. 138-139
Author(s):  
V. F. Allison ◽  
G. C. Fink ◽  
G. W. Cearley
Keyword(s):  
Cell Growth ◽  
Epithelial Cell ◽  
Epithelial Cells ◽  
Seminal Vesicle ◽  
Seminal Vesicles ◽  
Epithelial Layer ◽  
Epithelial Hyperplasia ◽  
Electron Microscopic ◽  
Aging Rats ◽  
Pseudostratified Epithelium

It is well known that epithelial hyperplasia (benign hypertrophy) is common in the aging prostate of dogs and man. In contrast, little evidence is available for abnormal epithelial cell growth in seminal vesicles of aging animals. Recently, enlarged seminal vesicles were reported in senescent mice, however, that enlargement resulted from increased storage of secretion in the lumen and occurred concomitant to epithelial hypoplasia in that species.The present study is concerned with electron microscopic observations of changes occurring in the pseudostratified epithelium of the seminal vescles of aging rats. Special attention is given to certain non-epithelial cells which have entered the epithelial layer.

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