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Single nucleotide polymorphisms of the prion protein gene ( PRNP ) in Chinese pig breeds
Author(s) -
Meng Liping,
Zhao Deming,
Liu Hongxiang,
Yang Jianmin,
Ning Zhangyong
Publication year - 2005
Publication title -
xenotransplantation
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.052
H-Index - 61
eISSN - 1399-3089
pISSN - 0908-665X
DOI - 10.1111/j.1399-3089.2005.00229.x
Subject(s) - prnp , biology , gene , virology , genetics , scrapie , single nucleotide polymorphism , open reading frame , bovine spongiform encephalopathy , genotype , disease , peptide sequence , prion protein , medicine , pathology
Prion diseases (transmissible spongiform encephalopathies, TSE), as a group of fatal neurodegenerative diseases, have affected humans and a variety of other mammals. Although no natural TSE have been documented in pigs, appropriate precautions need to be taken to prevent the iatrogenic spread of prion disease through pig‐to‐human xenotransplantation. Polymorphisms within the open reading frame (ORF) of the single‐copy gene of prion protein (PRNP) are associated with susceptibility to scrapie in sheep and variant Creutzfeldt‐Jacob disease in humans. We screened polymorphisms in the PRNP gene of 64 China Experimental Minipigs and Beijing Large White pigs. Our findings suggest that the porcine PRNP gene is highly homogenous. The amino acid sequences of the mature prion protein of all samples tested were identical. Four single nucleotide polymorphisms (G11A, G615C, G684A, T726G) in the ORF of the porcine PRNP gene were found, and the G→C nucleotide substitution resulted in a serine to asparaginate amino acid substitution at codon 4. We conclude that pigs raised under specific pathogen‐free conditions, with the exclusion of rendered mammalian material for at least two generations, will have little risk of being infected with a TSE, and even less possibility of transmitting prion disease to humans through xenotransplantation.