PRNP sequences of wild animals from the Qinghai-Tibet Plateau

Timothy Hill
Prion disease: PRNP sequences of wild animals from the Qinghai-Tibet Plateau
RT-QuIC assays of rSheepPrP25-234, rpikaPrP23-230, and rHaPrP23-231 to four various rodent-adapted scrapie strains. (A) Hamster-tailored strain 263K. (B) Mouse-tailored strain 139A. (C) Mouse-tailored pressure ME7. (D) Mouse-adapted pressure S15. The dilutions of scrapie strains are demonstrated in the top rated of each and every graph. Neg Ctrl: damaging regulate of 10-5 diluted mind homogenate of regular hamster. Blank Ctrl: blank management of PBS. Numerous recombinant PrP proteins are indicated on the ideal. Credit: Zoonoses (2023). DOI: 10.15212/ZOONOSES-2022-0036

Tibetan antelope (Rhinopithecus), blue sheep (Pseudois nayauris), and plateau pika (Ochotona curzoniae) are wild animals dwelling on the Qinghai-Tibet Plateau. There have been no experiences of in a natural way developing transmissible spongioform encephalopathies (TSEs) involving these animals. Furthermore, the PRNP genes have not been described in the literature.

For a analyze released in Zoonoses, the PRNP genes from 21 Tibetan antelopes, 4 blue sheep, and 3 plateau pikas were being attained and sequenced. The recombinant proteins had been then organized. Employing scrapie strains (263K, 139A, ME7, and S15) as the seeds, the reactivity of the PrP proteins from sheep (rSheepPrP25-234) and pika (rPikaPrP23-230) had been tested making use of real-time quaking-induced conversion (RT-QuIC). Protein misfolding cyclic amplification (PMCA) checks of the mind homogenates from domestic sheep and rabbits ended up performed with the seeds of strains 263K and ME7.

The PRNP genes of bovids had been 771 bp long and encoded 256 amino acids (aa), demonstrating 100% homology with the wild-form sheep prion protein (PrP) aa sequence. The PRNP gene of pika was 759 bp very long and encoded 252 amino acids, exhibiting 92.1% homology with the aa sequence of domestic rabbits. The sheep and pika proteins exposed positive reactions in 10-5 diluted seeds. Only rPikaPrP23-230 made beneficial curves in 10-7 diluted seeds. The PMCA assessments failed to generate proteinase K (PK)-resistant PrP (PrPres).

This is the to start with description of PRNP genes and PrP aa sequences of Tibetan antelope, blue sheep, and plateau pike from the Qinghai-Tibet Plateau. In the existence of rodent prions, the PrPs of sheep and pika successfully induce fibrillation in RT-QuIC, but do not produce PrPres in PMCA. Our final results reveal that pika, as a single of the crucial links in the Qinghai-Tibet Plateau organic chain, could enjoy an essential position in the prion circulation. Pika PrP warrants additional evaluation for its opportunity software value in assays for human prion illness.

Extra data:
Yue-Zhang Wu et al, PRNP Sequences of Tibetan Antelope, Blue Sheep, and Plateau Pika from the Qinghai-Tibet Plateau and Reactivity of PrP Proteins to Rodent-Tailored Scrapie Strains in RT-QuIC and PMCA, Zoonoses (2023). DOI: 10.15212/ZOONOSES-2022-0036

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Prion disease: PRNP sequences of wild animals from the Qinghai-Tibet Plateau (2023, January 24)
retrieved 25 January 2023

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