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Query: UMLS:C0001511 (Adhesion)
 5,955 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The following findings were obtained from histomorphological examination of 45 piglets with coli-bacillosis (with serotypical Escherichia coli detected) and ten piglets with coli-diarrhoea (with non-serotypical E. coli detected): Diarrhoea accompanying either disease was not attributable to catarrhal or haemorrhagic gastro-enteritis. The mucous membrane of the gastro-insestinal tract remained histomorphologically intact in either disease. No change was recorded particularly from villous or surface epithelia and glandular epithelium, and the villous structure was not basically altered. Different degrees of hyper aemia of the gastro-intestinal mucous membrane and moderate oedematisation of the villous stroma were irregular findings. Adhesion of enteropathogenic E. coli to mucous membrane surface was observed but rarely and did not exhibit any visible relationship with the incidence in E. coli of L-antigen K88. In coli-bacillosis and coli-diarrhoea both the diarrhoea and morphological situation of the gastro-bacillosis tract were in conformity with the cholera-type "intestinal noninflammatory secretory diarrhoea" as caused by enterotoxins. Other issues relating to pathology and diagnosis are also discussed.
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PMID:[Pathology and pathogenesis of coli dysentery and coli diarrhea in suckling piglets. 1. Studies on the pathomorphology of the gastrointestinal tract in coli dysentery as well as coli diarrhea in the suckling piglet]. 79 39

Adhesion of Campylobacter jejuni and C. coli to epithelial cells is thought to be a decisive step in enteritis. In this work, we tried to determine which bacterial components are responsible for this phenomenon. Outer membrane (OM) extracts were prepared from strains of C. jejuni (3 strains) and C. coli (2 strains). These strains had been isolated from stools of febrile patients with diarrhoea and were able to adhere to HeLa cells in culture. After incubation of bacterial OM extracts with HeLa cells in culture, bacterial adherent material was recovered, subjected to electrophoresis and immunoblotted. Bacterial adherent antigens were revealed by a rabbit antiserum raised against whole bacterial cells. Antigenic fractions, ranging from 26 to 30 kDa, were found to preferentially bind to HeLa cells (cell-binding fractions; CBF). These antigens were proteins and were distinct from flagellin and lipopolysaccharide. Bacteria incubated with a rabbit antiserum raised against homologous CBF, were unable to bind to HeLa cells. Moreover, the inhibitory effect decreased when the antiserum was diluted. Under the same conditions, a rabbit antiserum raised against a non-adherent OM fraction of 92 kDa did not prevent bacteria from binding to HeLa cells.
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PMID:Adhesion to HeLa cells of Campylobacter jejuni and C. coli outer membrane components. 261 91

Vibrio parahaemolyticus is an emerging bacterial pathogen which colonizes the gastrointestinal tract and can cause severe enteritis and bacteraemia. During infection, V. parahaemolyticus primarily attaches to the small intestine, where it causes extensive tissue damage and compromises epithelial barrier integrity. We have previously described that Multivalent Adhesion Molecule (MAM) 7 contributes to initial attachment of V. parahaemolyticus to epithelial cells. Here we show that the bacterial adhesin, through multivalent interactions between surface-induced adhesin clusters and phosphatidic acid lipids in the host cell membrane, induces activation of the small GTPase RhoA and actin rearrangements in host cells. In infection studies with V. parahaemolyticus we further demonstrate that adhesin-triggered activation of the ROCK/LIMK signaling axis is sufficient to redistribute tight junction proteins, leading to a loss of epithelial barrier function. Taken together, these findings show an unprecedented mechanism by which an adhesin acts as assembly platform for a host cellular signaling pathway, which ultimately facilitates breaching of the epithelial barrier by a bacterial pathogen.
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PMID:Multivalent adhesion molecule 7 clusters act as signaling platform for host cellular GTPase activation and facilitate epithelial barrier dysfunction. 2525 50