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Fibrinogen-binding and platelet-aggregation activities of a Lactobacillus salivarius septicaemia isolate are mediated by a novel fibrinogen-binding protein.

Mol. Microbiol.. 2012; 
Collins James,van Pijkeren Jan-Peter,Svensson Lisbeth,Claesson Marcus J,Sturme Mark,Li Yin,Cooney Jakki C,van Sinderen Douwe,Walker Alan W,Parkhill Julian,Shannon Oonagh,O'Toole Pa
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Peptide Synthesis Unbound CCUG_2371 was removed with six washes and bound CCUG_2371 probed with affinity-purified rabbit anti-CCUG_2371 antibody (200 ng ml-1), raised against a synthetic peptide based upon residues 173–187 (with sequence IYVKDDSTYQDLLG) of the CCUG_2371 protein (GenScript), followed by goat anti- rabbit IgG horseradish peroxidase-coupled immunoglobulin (1:5000 dilution) (Sigma). Get A Quote

摘要

The marketplace for probiotic foods is burgeoning, measured in billions of euro per annum. It is imperative, however, that all bacterial strains are fully assessed for human safety. The ability to bind fibrinogen is considered a potential pathogenicity trait that can lead to platelet aggregation, serious medical complications, and in some instances, death. Here we examined strains from species frequently used as probiotics for their ability to bind human fibrinogen. Only one strain (CCUG 47825), a Lactobacillus salivarius isolate from a case of septicaemia, was found to strongly adhere to fibrinogen. Furthermore, this strain was found to aggregate human platelets at a level comparable to the h... More

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