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Pilot study to determine the feasibility of producing protease-resistant prion protein fragments by random PCR mutagenesis.

Abstract：

:We report the results of a pilot study to determine the feasibility of using PCR random mutagenesis and in vitro transcription/translation to produce protease resistant full-length or truncated ovine prion proteins (PrP). Using this approach, we show the novel production of protease resistant recombinant ovine prion protein fragments isolated from a panel of seventy randomly mutated ovine PrP protein molecules. Protease resistance of the proteinase K (PK) digested fragments was present de novo within physiological conditions without the need for template-assisted conversion to protease resistance or the requirement of reductants, denaturants or acid pH reported to date. Four of the mutant proteins were truncated at their C-termini and all of these gave rise to digestion products which were protease resistant at significant PK concentrations and exposure times. All other mutant proteins translated as full length molecules and gave rise to PK-resistant products which showed a variability in their proteinase digestion profiles. We discuss the relevance of these finding to current research.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Dear DV,Fitzmaurice TJ,Garton S,Richards SJ

doi

10.1006/bbrc.2001.4450

subject

Has Abstract

pub_date

2001-03-09 00:00:00

pages

929-35

issue

4

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(01)94450-X

journal_volume

281

pub_type

杂志文章

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