■哺乳动物中的朊病毒疾病是由天然朊病毒蛋白(PrPC)向致病性同工型的结构转化引起的,朊病毒蛋白(PrPSc)的瘙痒病形式。\“几项研究报道,朊病毒蛋白(Sho)的阴影,由pr病毒蛋白基因(SPRN)的影子编码,通过加速PrPC到PrPSc的构象转化参与朊病毒疾病的发展。直到现在,尚未在野鸡中研究SPRN基因的遗传多态性和与pr病毒疾病脆弱性相关的Sho蛋白结构,这是一种家禽。
■这里,我们通过聚合酶链反应(PCR)鉴定了SPRN基因序列,并比较了SPRN基因和Sho蛋白序列,以使用ClustalOmega鉴定野鸡Sho的独特遗传特征。此外,我们调查了山鸡SPRN基因的遗传多态性,并分析了基因型,等位基因,和单倍型频率,以及遗传多态性之间的连锁不平衡。此外,我们在silico程序中使用,即Mutpred2、MUpro和AMYCO,研究非同义单核苷酸多态性(SNP)的影响。最后,通过Alphafold2分析了来自各种物种的Sho蛋白的预测二级和三级结构。
■在本研究中,我们首次报道了山鸡SPRN基因序列,共鉴定出14个新的SNPs,包括7个非同义SNP和4个同义SNP。此外,鸡Sho蛋白序列与鸡Sho蛋白序列具有100%的同一性。此外,预测氨基酸取代会影响山鸡Sho蛋白3D结构中的氢键分布。
■据我们所知,这是山鸡SPRN基因的遗传和结构特征的首次报道。
UNASSIGNED: Prion diseases in mammals are caused by the structural conversion of the natural prion protein (PrPC) to a pathogenic isoform, the \"scrapie form of prion protein (PrPSc).\" Several studies reported that the shadow of prion protein (Sho), encoded by the shadow of prion protein gene (SPRN), is involved in prion disease development by accelerating the conformational conversion of PrPC to PrPSc. Until now, genetic polymorphisms of the SPRN gene and the protein structure of Sho related to fragility to prion disease have not been investigated in
pheasants, which are a species of poultry.
UNASSIGNED: Here, we identified the SPRN gene sequence by polymerase chain reaction (PCR) and compared the SPRN gene and Sho protein sequences among various prion disease-susceptible and -resistant species to identify the distinctive genetic features of pheasant Sho using Clustal Omega. In addition, we investigated genetic polymorphisms of the SPRN gene in
pheasants and analyzed genotype, allele, and haplotype frequencies, as well as linkage disequilibrium among the genetic polymorphisms. Furthermore, we used in silico programs, namely Mutpred2, MUpro and AMYCO, to investigate the effect of non-synonymous single nucleotide polymorphisms (SNPs). Finally, the predicted secondary and tertiary structures of Sho proteins from various species were analyzed by Alphafold2.
UNASSIGNED: In the present study, we reported pheasant SPRN gene sequences for the first time and identified a total of 14 novel SNPs, including 7 non-synonymous and 4 synonymous SNPs. In addition, the pheasant Sho protein sequence showed 100% identity with the chicken Sho protein sequence. Furthermore, amino acid substitutions were predicted to affect the hydrogen bond distribution in the 3D structure of the pheasant Sho protein.
UNASSIGNED: To the best of our knowledge, this is the first report of the genetic and structural features of the pheasant SPRN gene.