Novel Polymorphisms and Genetic Characteristics of the Shadow of Prion Protein Gene ( SPRN ) in Cats, Hosts of Feline Spongiform Encephalopathy
Prion diseases are transmissible spongiform encephalopathies (TSEs) caused by pathogenic prion protein (PrP ) originating from normal prion protein (PrP ) and have been reported in several types of livestock and pets. Recent studies have reported that the shadow of prion protein (Sho) encoded by the...
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Published in | Viruses Vol. 14; no. 5; p. 981 |
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Language | English |
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Abstract | Prion diseases are transmissible spongiform encephalopathies (TSEs) caused by pathogenic prion protein (PrP
) originating from normal prion protein (PrP
) and have been reported in several types of livestock and pets. Recent studies have reported that the shadow of prion protein (Sho) encoded by the shadow of prion protein gene (
) interacts with prion protein (PrP) and accelerates prion diseases. In addition, genetic polymorphisms in the
gene are related to susceptibility to prion diseases. However, genetic polymorphisms in the feline
gene and structural characteristics of the Sho have not been investigated in cats, a major host of feline spongiform encephalopathy (FSE). We performed amplicon sequencing to identify feline
polymorphisms in the 623 bp encompassing the open reading frame (ORF) and a small part of the 3' untranslated region (UTR) of the
gene. We analyzed the impact of feline
polymorphisms on the secondary structure of
mRNA using RNAsnp. In addition, to find feline-specific amino acids, we carried out multiple sequence alignments using ClustalW. Furthermore, we analyzed the N-terminal signal peptide and glycosylphosphatidylinositol (GPI)-anchor using SignalP and PredGPI, respectively. We identified three novel SNPs in the feline
gene and did not find strong linkage disequilibrium (LD) among the three SNPs. We found four major haplotypes of the
polymorphisms. Strong LD was not observed between
and
polymorphisms. In addition, we found alterations in the secondary structure and minimum free energy of the mRNA according to the haplotypes in the
polymorphisms. Furthermore, we found four feline-specific amino acids in the feline Sho using multiple sequence alignments among several species. Lastly, the N-terminal signal sequence and cutting site of the Sho protein of cats showed similarity with those of other species. However, the feline Sho protein exhibited the shortest signal sequence and a unique amino acid in the omega-site of the GPI anchor. To the best of our knowledge, this is the first report on genetic polymorphisms of the feline
gene. |
---|---|
AbstractList | Prion diseases are transmissible spongiform encephalopathies (TSEs) caused by pathogenic prion protein (PrPSc) originating from normal prion protein (PrPC) and have been reported in several types of livestock and pets. Recent studies have reported that the shadow of prion protein (Sho) encoded by the shadow of prion protein gene (SPRN) interacts with prion protein (PrP) and accelerates prion diseases. In addition, genetic polymorphisms in the SPRN gene are related to susceptibility to prion diseases. However, genetic polymorphisms in the feline SPRN gene and structural characteristics of the Sho have not been investigated in cats, a major host of feline spongiform encephalopathy (FSE). We performed amplicon sequencing to identify feline SPRN polymorphisms in the 623 bp encompassing the open reading frame (ORF) and a small part of the 3′ untranslated region (UTR) of the SPRN gene. We analyzed the impact of feline SPRN polymorphisms on the secondary structure of SPRN mRNA using RNAsnp. In addition, to find feline-specific amino acids, we carried out multiple sequence alignments using ClustalW. Furthermore, we analyzed the N-terminal signal peptide and glycosylphosphatidylinositol (GPI)-anchor using SignalP and PredGPI, respectively. We identified three novel SNPs in the feline SPRN gene and did not find strong linkage disequilibrium (LD) among the three SNPs. We found four major haplotypes of the SPRN polymorphisms. Strong LD was not observed between PRNP and SPRN polymorphisms. In addition, we found alterations in the secondary structure and minimum free energy of the mRNA according to the haplotypes in the SPRN polymorphisms. Furthermore, we found four feline-specific amino acids in the feline Sho using multiple sequence alignments among several species. Lastly, the N-terminal signal sequence and cutting site of the Sho protein of cats showed similarity with those of other species. However, the feline Sho protein exhibited the shortest signal sequence and a unique amino acid in the omega-site of the GPI anchor. To the best of our knowledge, this is the first report on genetic polymorphisms of the feline SPRN gene. Prion diseases are transmissible spongiform encephalopathies (TSEs) caused by pathogenic prion protein (PrP ) originating from normal prion protein (PrP ) and have been reported in several types of livestock and pets. Recent studies have reported that the shadow of prion protein (Sho) encoded by the shadow of prion protein gene ( ) interacts with prion protein (PrP) and accelerates prion diseases. In addition, genetic polymorphisms in the gene are related to susceptibility to prion diseases. However, genetic polymorphisms in the feline gene and structural characteristics of the Sho have not been investigated in cats, a major host of feline spongiform encephalopathy (FSE). We performed amplicon sequencing to identify feline polymorphisms in the 623 bp encompassing the open reading frame (ORF) and a small part of the 3' untranslated region (UTR) of the gene. We analyzed the impact of feline polymorphisms on the secondary structure of mRNA using RNAsnp. In addition, to find feline-specific amino acids, we carried out multiple sequence alignments using ClustalW. Furthermore, we analyzed the N-terminal signal peptide and glycosylphosphatidylinositol (GPI)-anchor using SignalP and PredGPI, respectively. We identified three novel SNPs in the feline gene and did not find strong linkage disequilibrium (LD) among the three SNPs. We found four major haplotypes of the polymorphisms. Strong LD was not observed between and polymorphisms. In addition, we found alterations in the secondary structure and minimum free energy of the mRNA according to the haplotypes in the polymorphisms. Furthermore, we found four feline-specific amino acids in the feline Sho using multiple sequence alignments among several species. Lastly, the N-terminal signal sequence and cutting site of the Sho protein of cats showed similarity with those of other species. However, the feline Sho protein exhibited the shortest signal sequence and a unique amino acid in the omega-site of the GPI anchor. To the best of our knowledge, this is the first report on genetic polymorphisms of the feline gene. Prion diseases are transmissible spongiform encephalopathies (TSEs) caused by pathogenic prion protein (PrP Sc ) originating from normal prion protein (PrP C ) and have been reported in several types of livestock and pets. Recent studies have reported that the shadow of prion protein (Sho) encoded by the shadow of prion protein gene ( SPRN ) interacts with prion protein (PrP) and accelerates prion diseases. In addition, genetic polymorphisms in the SPRN gene are related to susceptibility to prion diseases. However, genetic polymorphisms in the feline SPRN gene and structural characteristics of the Sho have not been investigated in cats, a major host of feline spongiform encephalopathy (FSE). We performed amplicon sequencing to identify feline SPRN polymorphisms in the 623 bp encompassing the open reading frame (ORF) and a small part of the 3′ untranslated region (UTR) of the SPRN gene. We analyzed the impact of feline SPRN polymorphisms on the secondary structure of SPRN mRNA using RNAsnp. In addition, to find feline-specific amino acids, we carried out multiple sequence alignments using ClustalW. Furthermore, we analyzed the N-terminal signal peptide and glycosylphosphatidylinositol (GPI)-anchor using SignalP and PredGPI, respectively. We identified three novel SNPs in the feline SPRN gene and did not find strong linkage disequilibrium (LD) among the three SNPs. We found four major haplotypes of the SPRN polymorphisms. Strong LD was not observed between PRNP and SPRN polymorphisms. In addition, we found alterations in the secondary structure and minimum free energy of the mRNA according to the haplotypes in the SPRN polymorphisms. Furthermore, we found four feline-specific amino acids in the feline Sho using multiple sequence alignments among several species. Lastly, the N-terminal signal sequence and cutting site of the Sho protein of cats showed similarity with those of other species. However, the feline Sho protein exhibited the shortest signal sequence and a unique amino acid in the omega-site of the GPI anchor. To the best of our knowledge, this is the first report on genetic polymorphisms of the feline SPRN gene. |
Author | Kim, Kiwon Kim, Hyeon-Ho Kim, An-Dang Kim, Yong-Chan Jeong, Byung-Hoon |
AuthorAffiliation | 4 Cool-Pet Animal Hospital, Anyang 14066, Gyeonggi, Korea; kad7582@hanmail.net 3 Haemalken Animal Hospital, Yangju 11492, Gyeonggi, Korea; kkw0075@hanmail.net 2 Department of Bioactive Material Sciences and Institute for Molecular Biology and Genetics, Jeonbuk National University, Jeonju 54896, Jeonbuk, Korea 1 Korea Zoonosis Research Institute, Jeonbuk National University, Iksan 54531, Jeonbuk, Korea; kych@jbnu.ac.kr (Y.-C.K.); khh7051@jbnu.ac.kr (H.-H.K.) |
AuthorAffiliation_xml | – name: 1 Korea Zoonosis Research Institute, Jeonbuk National University, Iksan 54531, Jeonbuk, Korea; kych@jbnu.ac.kr (Y.-C.K.); khh7051@jbnu.ac.kr (H.-H.K.) – name: 3 Haemalken Animal Hospital, Yangju 11492, Gyeonggi, Korea; kkw0075@hanmail.net – name: 4 Cool-Pet Animal Hospital, Anyang 14066, Gyeonggi, Korea; kad7582@hanmail.net – name: 2 Department of Bioactive Material Sciences and Institute for Molecular Biology and Genetics, Jeonbuk National University, Jeonju 54896, Jeonbuk, Korea |
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Cites_doi | 10.1038/s41423-021-00747-z 10.1073/pnas.1204498109 10.3389/fvets.2021.804325 10.3390/membranes11120978 10.1111/j.1750-3639.1998.tb00171.x 10.1007/s13353-012-0102-4 10.2741/3681 10.1371/journal.ppat.1000666 10.1038/s41598-020-63805-y 10.1371/journal.pone.0018067 10.3389/fcell.2015.00005 10.4161/pri.19640 10.1111/bpa.12696 10.3390/genes12010013 10.1038/s41587-021-01156-3 10.1186/s13567-021-00975-1 10.1002/0471250953.bi0313s48 10.2741/3801 10.1093/bioinformatics/bth457 10.1038/sj.emboj.7601830 10.2139/ssrn.3825525 10.1099/vir.0.041400-0 10.1093/nar/gkt291 10.1186/1471-2105-9-392 10.1128/JVI.03429-14 10.1261/rna.1082708 10.1055/s-0039-1687841 10.1136/jmg.2008.061804 |
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Snippet | Prion diseases are transmissible spongiform encephalopathies (TSEs) caused by pathogenic prion protein (PrP
) originating from normal prion protein (PrP
) and... Prion diseases are transmissible spongiform encephalopathies (TSEs) caused by pathogenic prion protein (PrPSc) originating from normal prion protein (PrPC) and... Prion diseases are transmissible spongiform encephalopathies (TSEs) caused by pathogenic prion protein (PrP Sc ) originating from normal prion protein (PrP C )... |
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StartPage | 981 |
SubjectTerms | 3' Untranslated regions Amino acid sequence Cats Encephalopathy feline Free energy Gene polymorphism Glycosylphosphatidylinositol Haplotypes Linkage disequilibrium Livestock mRNA Open reading frames Peptides Pets prion Prion protein PRNP Protein structure Proteins Secondary structure Single-nucleotide polymorphism SNP Spongiform encephalopathy SPRN Transmissible spongiform encephalopathy |
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Title | Novel Polymorphisms and Genetic Characteristics of the Shadow of Prion Protein Gene ( SPRN ) in Cats, Hosts of Feline Spongiform Encephalopathy |
URI | https://www.ncbi.nlm.nih.gov/pubmed/35632724 https://www.proquest.com/docview/2670486937/abstract/ https://search.proquest.com/docview/2671270499 https://pubmed.ncbi.nlm.nih.gov/PMC9148082 https://doaj.org/article/f08e82f66de9465bbf38507f7630f5d0 |
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