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• W2186649364 abstract "Results: Prion conversion was reduced by non-aromatic amino acids at PrP position 169 in the 2-2 loop. Conclusion: The conserved tyrosine side chain at PrP position 169 promotes efficient prion formation. Significance: These findings are consistent with a zipper model of prion conversion. The transmission of infectious prions into different host spe- cies requires compatible prion protein (PrP) primary structures, and even one heterologous residue at a pivotal position can block prion infection. Mapping the key amino acid positions that govern cross-species prion conversion has not yet been pos- sible, although certain residue positions have been identified as restrictive, including residues in the 2-2 loop region of PrP. To further define how 2-2 residues impact conversion, we investigated residue substitutions in PrP C using an in vitro prion conversion assay. Within the 2-2 loop, a tyrosine residue at position 169 is strictly conserved among mammals, and trans- genic mice expressing mouse PrP having the Y169G, S170N, and N174T substitutions resist prion infection. To better under- stand the structural requirements of specific residues for con- version initiated by mouse prions, we substituted a diverse array of amino acids at position 169 of PrP. We found that the substi- tution of glycine, leucine, or glutamine at position 169 reduced conversion by 75%. In contrast, replacing tyrosine 169 with either of the bulky, aromatic residues, phenylalanine or trypto- phan, supported efficient prion conversion. We propose a model based on a requirement for tightly interdigitating com- plementary amino acid side chains within specific domains of adjacent PrP molecules, known as steric zippers, to explain these results. Collectively, these studies suggest that an aromatic residue at position 169 supports efficient prion conversion." @default.
• W2186649364 created "2016-06-24" @default.
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• W2186649364 date "2014-01-01" @default.
• W2186649364 modified "2023-10-01" @default.
• W2186649364 title "A Proposed Mechanism for the Promotion of Prion Conversion Involving a Strictly Conserved Tyrosine" @default.
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