NDLI: Demonstration of a protein with enhanced resistance to proteinase K in transmissible cytopathic condition elicited by cell-free lysate of free-living ameba Naegleria gruberi : Are microbial proteins capable of converting mammalian proteins into prion-like pathogens? A probable pathomechanism for some postinfectious degenerative sequelae and for natural prion disease in sheep, goat and cervids

Content Provider	Springer Nature Link
Author	Füzi, Miklos Pászti, Judit Gyuris, Ágnes Orosz, Erika Minárovits, Jás Szénási, Zsuzsa
Copyright Year	2008
Abstract	The cell-free lysate of free-living amebae Naegleria gruberi and Naegleria fowleri were reported to elicit cytopathic effect in various cell lines that could be indefinitely transmitted by the culture media. The causative agent showed sensitivity to treatments detrimental to proteins while resisted exposures damaging to nucleic acids. Here we demonstrate that subsequent to exposure to N. gruberi lysate mild digestion with proteinase K reveals the presence of a protein band in HeLa cells absent from control cell lines. Though the small quantity of this protein with enhanced resistance to proteinase K relative to the total protein content of the sample has proved to date insufficient for its purification, we suppose that it is a human cellular protein that assumed altered conformation in a prion-like fashion. The conformational conversion could have been trigerred by an ameba protein in the lysate. In addition, we showed that HeLa cells treated with N. gruberi lysate display elevated cathepsin B activity which is assumed to be a secondary response to the accumulation of the proteinase K-resistant protein. We propose that a number of degenerative sequelae following previous microbial infections in mammals could have a similar pathomechanism. Moreover, epidemiological data strongly suggest that natural prion disease in sheep, goat and cervids may also have an etiology linked to prior infection/colonization with a microbe, as it had already been proposed by one of us.
Starting Page	203
Ending Page	208
Page Count	6
File Format	PDF
ISSN	10400400
Journal	Structural Chemistry
Volume Number	19
Issue Number	2
e-ISSN	15729001
Language	English
Publisher	Springer US
Publisher Date	2008-01-19
Publisher Place	Boston
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Prion Ameba Postinfectious Transmission Proteinase K resistant Cathepsin B Autoimmune Rheumatic fever Theoretical and Computational Chemistry Physical Chemistry Computer Applications in Chemistry
Content Type	Text
Resource Type	Article
Subject	Physical and Theoretical Chemistry Condensed Matter Physics

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Naegleria fowleri Lysate Induces Strong Cytopathic Effects and Pro-inflammatory Cytokine Release

in the Differentiation of Naegleria gruberi

Some aspects of the enflagellation index of naegleria gruberi.

Basal bodies, but not centrioles, in Naegleria (1971)

Synthesis and assembly of the cytoskeleton of naegleria gruberi flagellates. Z cell biol (1984).

Synthesis and assembly of the cytoskeleton of Naegleria gruberi flagellates (1984)

New Poly(A)+RNAs Appear Coordinately during the Differentiation of Naegleria gruberi

New Poly(A)+RNAs Appear Coordinately during the Differentiation of Naegleria gruberi

Purification and characterization of cathepsin L-like proteinase from goat brain

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Basal bodies, but not centrioles, in Naegleria (1971)

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