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Antigens of abnormal isoform of prion protein characterized.
2004 JUN 2 - (NewsRx.com & NewsRx.net) -- Researchers characterized the antigens of an abnormal isoform of prion protein using a new diverse panel of monoclonal antibodies.
"We established a panel of monoclonal antibodies (mAbs) against prion protein (PrP) by immunizing PrP gene-ablated mice with the pathogenic isoform of prion protein (PrP[superscript]Sc) or recombinant prion protein (rPrP). The mAbs could be divided into at least 10 groups by fine epitope analyses using mutant rPrPs and pepspot analysis. Seven linear epitopes, lying within residues 56-90, 119-127, 137-143, 143-149, 147-151, 163-169, and 219-229, were defined by seven groups of mAbs, although the remaining three groups of mAbs recognized discontinuous epitopes," scientists in Japan report.
"We attempted to examine whether any of these epitopes are located on the accessible surface of PrP[superscript]Sc," said Chan-Lan Kim and collaborators at Obihiro University of Agriculture and Veterinary Medicine and at Fujirebio Inc. "However, no mAbs reacted with protease-treated PrP[superscript]Sc purified from scrapie-affected mice, even when PrP[superscript]Sc was dispersed into a detergent-lipid protein complex, to reduce the size of PrP[superscript]Sc aggregates. In contrast, denaturation of PrP[superscript]Sc by guanidine hydrochloride efficiently exposed all of the epitopes. This suggests that any epitope recognized by this panel of mAbs is buried within the PrP[superscript]Sc aggregates."
"Alternatively, if the ...
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Source: HighBeam Research, Antigens of abnormal isoform of prion protein characterized.