Subgingival Curettage Versus Surgical Elimination of Periodontal Pockets

Peer Reviewedhttps://deepblue.lib.umich.edu/bitstream/2027.42/142057/1/jper0167.pd

Short Term Results of Three Modalities of Periodontal Treatment

Peer Reviewedhttps://deepblue.lib.umich.edu/bitstream/2027.42/141914/1/jper0131.pd

Longitudinal Study of Periodontal Therapy

Peer Reviewedhttps://deepblue.lib.umich.edu/bitstream/2027.42/142010/1/jper0066.pd

Results Following Three Modalities of Periodontal Therapy

Peer Reviewedhttps://deepblue.lib.umich.edu/bitstream/2027.42/141627/1/jper0522.pd

Results of Periodontal Treatment Related to Pocket Depth and Attachment Level. Eight Years

Peer Reviewedhttps://deepblue.lib.umich.edu/bitstream/2027.42/141007/1/jper0225.pd

Radiographs in Clinical Periodontal Trials

Peer Reviewedhttps://deepblue.lib.umich.edu/bitstream/2027.42/141530/1/jper0381.pd

Oral Hygiene and Maintenance of Periodontal Support

Peer Reviewedhttps://deepblue.lib.umich.edu/bitstream/2027.42/142220/1/jper0026.pd

Four modalities of periodontal treatment compared over five years

Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/65517/1/j.1600-0765.1987.tb01573.x.pd

Identification and Characterization of Microcin S, a New Antibacterial Peptide Produced by Probiotic Escherichia coli G3/10

Escherichia coli G3/10 is a component of the probiotic drug Symbioflor 2. In an in vitro assay with human intestinal epithelial cells, E. coli G3/10 is capable of suppressing adherence of enteropathogenic E. coli E2348/69. In this study, we demonstrate that a completely novel class II microcin, produced by probiotic E. coli G3/10, is responsible for this behavior. We named this antibacterial peptide microcin S (MccS). Microcin S is coded on a 50.6 kb megaplasmid of E. coli G3/10, which we have completely sequenced and annotated. The microcin S operon is about 4.7 kb in size and is comprised of four genes. Subcloning of the genes and gene fragments followed by gene expression experiments enabled us to functionally characterize all members of this operon, and to clearly identify the nucleotide sequences encoding the microcin itself (mcsS), its transport apparatus and the gene mcsI conferring self immunity against microcin S. Overexpression of cloned mcsI antagonizes MccS activity, thus protecting indicator strain E. coli E2348/69 in the in vitro adherence assay. Moreover, growth of E. coli transformed with a plasmid containing mcsS under control of an araC PBAD activator-promoter is inhibited upon mcsS induction. Our data provide further mechanistic insight into the probiotic behavior of E. coli G3/10

The host response to the probiotic Escherichia coli strain Nissle 1917: Specific up-regulation of the proinflammatory chemokine MCP-1

BACKGROUND: The use of live microorganisms to influence positively the course of intestinal disorders such as infectious diarrhea or chronic inflammatory conditions has recently gained increasing interest as a therapeutic alternative. In vitro and in vivo investigations have demonstrated that probiotic-host eukaryotic cell interactions evoke a large number of responses potentially responsible for the effects of probiotics. The aim of this study was to improve our understanding of the E. coli Nissle 1917-host interaction by analyzing the gene expression pattern initiated by this probiotic in human intestinal epithelial cells. METHODS: Gene expression profiles of Caco-2 cells treated with E. coli Nissle 1917 were analyzed with microarrays. A second human intestinal cell line and also pieces of small intestine from BALB/c mice were used to confirm regulatory data of selected genes by real-time RT-PCR and cytometric bead array (CBA) to detect secretion of corresponding proteins. RESULTS: Whole genome expression analysis revealed 126 genes specifically regulated after treatment of confluent Caco-2 cells with E. coli Nissle 1917. Among others, expression of genes encoding the proinflammatory molecules monocyte chemoattractant protein-1 ligand 2 (MCP-1), macrophage inflammatory protein-2 alpha (MIP-2α) and macrophage inflammatory protein-2 beta (MIP-2β) was increased up to 10 fold. Caco-2 cells cocultured with E. coli Nissle 1917 also secreted high amounts of MCP-1 protein. Elevated levels of MCP-1 and MIP-2α mRNA could be confirmed with Lovo cells. MCP-1 gene expression was also up-regulated in mouse intestinal tissue. CONCLUSION: Thus, probiotic E. coli Nissle 1917 specifically upregulates expression of proinflammatory genes and proteins in human and mouse intestinal epithelial cells