The saga of prion: to cut or not to cut

Sy, Man Sun

doi:10.1038/cr.2009.102

Cell Res

2009

DOI: 10.1038/cr.2009.102

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The saga of prion: to cut or not to cut

Man Sun Sy

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2010

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“…Fifth, the 3F4 epitope is the endoproteolytic cleavage site for generation of the normal metabolic product of human PrP called C1 (15). Finally, it has been recently demonstrated that PrP C -associated signal transduction is modulated by the primary sequence around the C1 cleavage site (16,17). Therefore, the 3F4 epitope appears to be the central area within which these physiological and pathophysiological molecular events occur.…”

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confidence: 99%

PrP Conformational Transitions Alter Species Preference of a PrP-specific Antibody

Zou

Langeveld²,

Xiao

et al. 2010

Journal of Biological Chemistry

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The epitope of the 3F4 antibody most commonly used in human prion disease diagnosis is believed to consist of residues Met-LysHis-Met (MKHM) corresponding to human PrP-(109 -112). This assumption is based mainly on the observation that 3F4 reacts with human and hamster PrP but not with PrP from mouse, sheep, and cervids, in which Met at residue 112 is replaced by Val. Here we report that, by brain histoblotting, 3F4 did not react with PrP of uninfected transgenic mice expressing elk PrP; however, it did show distinct immunoreactivity in transgenic mice infected with chronic wasting disease. Compared with human PrP, the 3F4 reactivity with the recombinant elk PrP was 2 orders of magnitude weaker, as indicated by both Western blotting and surface plasmon resonance. To investigate the molecular basis of these species-and conformer-dependent preferences of 3F4, the epitope was probed by peptide membrane array and antigen competition experiments. Remarkably, the 3F4 antibody did not react with MKHM but reacted strongly with KTNMK (corresponding to human PrP-(106 -110)), a sequence that is also present in cervids, sheep, and cattle. 3F4 also reacted with elk PrP peptides containing KTNMKHV. We concluded that the minimal sequence for the 3F4 epitope consists of residues KTNMK, and the speciesand conformer-dependent preferences of 3F4 arise largely from the interactions between Met 112 (human PrP) or Val 115 (cervid PrP) and adjacent residues.

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mentioning

confidence: 99%

PrP Conformational Transitions Alter Species Preference of a PrP-specific Antibody

Zou

Langeveld²,

Xiao

et al. 2010

Journal of Biological Chemistry

Self Cite

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The saga of prion: to cut or not to cut

Cited by 1 publication

References 14 publications

PrP Conformational Transitions Alter Species Preference of a PrP-specific Antibody

PrP Conformational Transitions Alter Species Preference of a PrP-specific Antibody

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