NR AYCG
AU Lipscomb,I.P.; Herve,R.; Harris,K.; Pinchin,H.; Collin,R.; Keevil,C.W.
TI Amyloid-specific fluorophores for the rapid, sensitive in situ detection of prion contamination on surgical instruments
QU Journal of General Virology 2007 Sep; 88(9): 2619-26
PT journal article; research support, non-u.s. gov't
AB Prion diseases or transmissible spongiform encephalopathies (TSEs) are a group of rare, transmissible and fatal neurodegenerative diseases associated with the protein agent (PrPsc). As such, the sensitive and rapid detection of prion PrPsc amyloid on the surface of suspect surgical instruments is of great importance and may even allow remedial action to be taken prior to any further operative intervention and possible iatrogenic transmission. However, conventional PrPsc detection methodologies tend to rely on the inefficient and unreliable removal of suspect material from a surface using swabs or wipes prior to antibody analysis. Here we show how the combination of an advanced light microscope technique, episcopic differential interference contrast/epifluorescence (EDIC/EF) microscopy, and the application of beta-amyloid fluorescent thiazole markers (thioflavin T, thioflavin S) can be used to detect, in situ, submicron (attomole) levels of prion protein amyloid contamination in brain and spleen sections, smears and homogenate on surgical stainless steel surfaces and surgical instruments. This technique, although not specific to an amyloid type, can be used to verify that surgical instruments are substantially free from prion amyloid protein soiling and hence reduce the risk of iatrogenic transmission.
MH Brain/*pathology; *Equipment Contamination; Fluorescent Dyes; Humans; Indicators and Reagents; PrPsc Proteins/analysis; Prions/*isolation & purification; Sensitivity and Specificity; Stainless Steel; Surgical Instruments/*standards
AD Environmental Healthcare Unit, School of Biological Sciences, University of Southampton, Bassett Crescent East, Southampton SO16 7PX, UK.
SP englisch
PO England