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北京鸭中该基因的首次遗传特征分析()。

The First Genetic Characterization of the Gene in Pekin Ducks ().

作者信息

Nguyen Thi-Thuy-Duong, Zayed Mohammed, Kim Yong-Chan, Jeong Byung-Hoon

机构信息

Korea Zoonosis Research Institute, Jeonbuk National University, 820-120, Hana-ro, Iksan 54531, Republic of Korea.

Department of Bioactive Material Sciences, Institute for Molecular Biology and Genetics, Jeonbuk National University, Jeonju 54896, Republic of Korea.

出版信息

Animals (Basel). 2024 May 27;14(11):1588. doi: 10.3390/ani14111588.

DOI:10.3390/ani14111588
PMID:38891635
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC11171214/
Abstract

Prion diseases are fatal neurodegenerative disorders characterized by an accumulation of misfolded prion protein (PrP) in brain tissues. The shadow of prion protein (Sho) encoded by the shadow of prion protein gene () is involved in prion disease progress. The interaction between Sho and PrP accelerates the PrP conversion rate while the gene polymorphisms have been associated with prion disease susceptibility in several species. Until now, the gene has not been investigated in ducks. We identified the duck gene sequence and investigated the genetic polymorphisms of 184 Pekin ducks. We compared the duck nucleotide sequence and the duck Sho protein amino acid sequence with those of several other species. Finally, we predicted the duck Sho protein structure and the effects of non-synonymous single nucleotide polymorphisms (SNPs) using computational programs. We were the first to report the Pekin duck gene sequence. The duck Sho protein sequence showed 100% identity compared with the chicken Sho protein sequence. We found 27 novel SNPs in the duck gene. Four amino acid substitutions were predicted to affect the hydrogen bond distribution in the duck Sho protein structure. Although MutPred2 and SNPs&GO predicted that all non-synonymous polymorphisms were neutral or benign, SIFT predicted that four variants, A22T, G49D, A68T, and M105I, were deleterious. To the best of our knowledge, this is the first report about the genetic and structural characteristics of the duck gene.

摘要

朊病毒病是致命的神经退行性疾病,其特征是脑组织中错误折叠的朊病毒蛋白(PrP)积累。朊病毒蛋白基因()的影子所编码的朊病毒蛋白影子(Sho)参与朊病毒病的进展。Sho与PrP之间的相互作用加速了PrP的转化率,而该基因多态性与多个物种的朊病毒病易感性相关。到目前为止,尚未在鸭中对该基因进行研究。我们鉴定了鸭的基因序列,并研究了184只北京鸭的基因多态性。我们将鸭的核苷酸序列和鸭Sho蛋白氨基酸序列与其他几个物种的进行了比较。最后,我们使用计算程序预测了鸭Sho蛋白结构以及非同义单核苷酸多态性(SNP)的影响。我们首次报道了北京鸭的基因序列。鸭Sho蛋白序列与鸡Sho蛋白序列显示出100%的同一性。我们在鸭基因中发现了27个新的SNP。预测四个氨基酸替换会影响鸭Sho蛋白结构中的氢键分布。尽管MutPred2和SNPs&GO预测所有非同义多态性都是中性或良性的,但SIFT预测四个变体A22T、G49D、A68T和M105I是有害的。据我们所知,这是关于鸭基因的遗传和结构特征的首次报道。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8eb6/11171214/8d0de8bf603a/animals-14-01588-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8eb6/11171214/20fca04fad2f/animals-14-01588-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8eb6/11171214/5d0448d6cfa1/animals-14-01588-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8eb6/11171214/c7037a80cece/animals-14-01588-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8eb6/11171214/8c9abda6ed69/animals-14-01588-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8eb6/11171214/a6d73e56d89c/animals-14-01588-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8eb6/11171214/8d0de8bf603a/animals-14-01588-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8eb6/11171214/20fca04fad2f/animals-14-01588-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8eb6/11171214/5d0448d6cfa1/animals-14-01588-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8eb6/11171214/c7037a80cece/animals-14-01588-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8eb6/11171214/8c9abda6ed69/animals-14-01588-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8eb6/11171214/a6d73e56d89c/animals-14-01588-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8eb6/11171214/8d0de8bf603a/animals-14-01588-g006.jpg

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