Single nucleotide polymorphism scanning and expression analysis of ACSL1 from different duck breeds

2021 ◽  
Author(s):  
Qianqian Song ◽  
Zhixiu Wang ◽  
Hongliang Zhang ◽  
Xiangxiang Li ◽  
Yang Zhang ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Protein Expression ◽  
Meat Quality ◽  
Liver Tissue ◽  
Phylogenetic Analyses ◽  
Abdominal Fat ◽  
Breast Muscle ◽  
Pekin Duck ◽  
Lipid Deposition

Accumulating studies have indicated that the long-chain fatty acyl-CoA1 (ACSL1) gene is related to fat deposition and meat quality in mammals. However, few studies have investigated the relationship between ACSL1 and lipid deposition in ducks. To examine this, we assessed the physicochemical property, homologous alignment and phylogenetic analyses of the ACSL1 amino acid sequence using bioinformatics tools. The analysis indicated that the ACSL1 amino acid sequence varies in animals, and the duck ACSL1 protein is most closely related to that of chicken. Two SNP sites were identified at 1749 and 1905 bp of the coding region of ACSL1 by sequencing. Quantitative real-time PCR and western blotting were used to measure mRNA and protein levels in abdominal fat, breast muscle and liver tissue of Pekin duck (BD) and Cherry Valley duck (CD). mRNA and protein expression were significantly higher in BD than in CD in abdominal fat and liver tissue (P < 0.05). In breast muscle, the mRNA level of ACSL1 was also significantly higher in BD than in CD (P < 0.05), and protein expression in BD tended to be higher than that of CD. These results suggest that ACSL1 may contribute to lipid deposition and meat quality in ducks.

scholarly journals First detection and characterisation of porcine hemagglutinating encephalomyelitis virus in the Czech Republic

2019 ◽  
Vol 64 (No. 02) ◽  
pp. 60-66
Author(s):  
R Moutelikova ◽  
J Prodelalova
Keyword(s):  
Czech Republic ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Phylogenetic Analyses ◽  
Economic Losses ◽  
The Czech Republic ◽  
Nucleocapsid Gene ◽  
Nasal Swabs ◽  
Encephalomyelitis Virus ◽  
Porcine Hemagglutinating Encephalomyelitis Virus

Porcine hemagglutinating encephalomyelitis virus (PHEV) is a highly neurovirulent coronavirus that invades the central nervous system in piglets. The incidence of PHEV among pigs in many countries is rising, and the economic losses to the pig industry may be significant. Serological studies suggest that PHEV is spread worldwide. However, no surveillance has been carried out in the Czech Republic. In this study, eight pig farms were screened for the presence of members of the Coronaviridae family with the use of reverse transcription PCR. A collection of 123 faecal samples and 151 nasal swabs from domestic pigs were analysed. In PHEV-positive samples, almost the complete coding sequence of the nucleocapsid gene was amplified and the acquired sequences were compared to those of geographically dispersed PHEV strains; phylogenetic analyses were also performed. PHEV was present in 7.9% of nasal swabs taken from different age categories of pigs. No other swine coronaviruses were detected. The amino acid sequence of the Czech PHEV strains showed 95.8–98.1% similarity to other PHEV reference strains in GenBank. PHEV strains collected from animals on the same farm were identical; however, strains from different farms have only exhibited only 96.7–98.7% amino acid sequence identity. Our study demonstrates the presence of PHEV in pigs in the Czech Republic. The Czech PHEV strains were evolutionarily closest to the Belgium strain VW572.

scholarly journals Cloning, sequencing and heterologous expression of a cDNA encoding pigeon liver carnitine acetyltransferase

1995 ◽  
Vol 305 (2) ◽  
pp. 439-444 ◽  
Author(s):  
T M Johnson ◽  
H P Kocher ◽  
R C Anderson ◽  
G M Nemecek
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Heterologous Expression ◽  
Stop Codon ◽  
Expression System ◽  
Breast Muscle ◽  
Cdna Clones ◽  
Carnitine Acetyltransferase ◽  
Western Blots ◽  
Pigeon Liver

Two overlapping cDNA clones encoding pigeon liver carnitine acetyltransferase (EC 2.3.1.7) (CAT) were isolated from a pigeon liver lambda gt11 cDNA library by gene amplification using oligonucleotide primers based on the N-terminal amino acid sequence of the enzyme. The two clones, which represent the 5′ and 3′ ends of the gene, were spliced together to form a single cDNA construct containing the entire coding sequence for CAT, with an in-frame TGA stop codon 42 bases before the first ATG start site and a 3′-untranslated segment of 1057 bases. The largest open reading frame of 1942 nucleotides predicted a polypeptide of 627 amino acids and a molecular mass of 71.1 kDa. The N-terminus and four internal peptides from the amino acid sequence of pigeon breast muscle CAT were identified in the predicted sequence of the liver cDNA clone. The identity of the CAT cDNA was confirmed by heterologous expression of active recombinant CAT (rCAT) in insect cells using the baculovirus expression system. Western blots of rCAT from infected insect cell lysates and immunodetection with a rabbit anti-CAT polyclonal serum showed an immunoreactive protein band similar in size to native CAT from pigeon breast muscle. Like the native enzyme, rCAT was capable of acylating carnitine with a preference for small-chain acyl-CoAs of carbon chain lengths C2-C4.

scholarly journals Broad-spectrum detection of papillomaviruses in bovine teat papillomas and healthy teat skin

2004 ◽  
Vol 85 (8) ◽  
pp. 2191-2197 ◽  
Author(s):  
Tomoko Ogawa ◽  
Yoshimi Tomita ◽  
Mineyuki Okada ◽  
Kuniko Shinozaki ◽  
Hiroko Kubonoya ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Broad Spectrum ◽  
Phylogenetic Analyses ◽  
Genomic Diversity ◽  
Bovine Papillomavirus ◽  
Subclinical Infection ◽  
Healthy Skin ◽  
Sequence Alignments ◽  
Spectrum Detection

To investigate the prevalence of bovine papillomavirus (BPV) in bovine papilloma and healthy skin, DNA extracted from teat papillomas and healthy teat skin swabs was analysed by PCR using the primer pairs FAP59/FAP64 and MY09/MY11. Papillomavirus (PV) DNA was detected in all 15 papilloma specimens using FAP59/FAP64 and in 8 of the 15 papilloma specimens using MY09/MY11. In swab samples, 21 and 8 of the 122 samples were PV DNA positive using FAP59/FAP64 and MY09/MY11, respectively. Four BPV types (BPV-1, -3, -5 and -6), two previously identified putative BPV types (BAA1 and -5) and 11 putative new PV types (designated BAPV1 to -10 and BAPV11MY) were found in the 39 PV DNA-positive samples. Amino acid sequence alignments of the putative new PV types with reported BPVs and phylogenetic analyses of the putative new PV types with human and animal PV types showed that BAPV1 to -10 and BAPV11MY are putative new BPV types. These results also showed the genomic diversity and extent of subclinical infection of BPV.

scholarly journals Two Low-molecular-weight Apoproteins (Apovitellenins I and II) from a Lipoprotein of Goose?s Egg Yolk: A Comparison with Related Species

1982 ◽  
Vol 35 (3) ◽  
pp. 263 ◽  
Author(s):  
AS Inglis ◽  
PM Strike ◽  
RW Burley
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Gel Filtration ◽  
Egg Yolk ◽  
Avian Species ◽  
Pekin Duck ◽  
Muscovy Duck ◽  
Hen’S Egg ◽  
Avian Family

As part of a comparative study of egg yolk from different avian species, the major lipoprotein and its mixed apoproteins from the egg yolk of the chinese goose (Anser cygnoides) have been prepared. From the apoprotein mixture, two new proteins, of molecular weight approximately 10000 and 22000 according to gel electrophoresis in detergent, have been isolated by gel-filtration chromato-graphy in urea. The protein of lower molecular weight corresponds in amino acid sequence to apovitellenin I, a protein previously isolated from other avian species. As a comparison with other members of the same avian family (Anatidae), the amino acid sequence of apovitellenin I from the pekin duck (Anas platyrhynchos) was re-investigated and that of the muscovy duck (Cairina moschata) investigated. These were found to be identical to the sequence of goose's apovitellenin I. The second new protein is similar in composition, molecular weight, and solubility to apovitellenin II, a protein present in small amount in hen's egg yolk. A protein corresponding to apovitellenin II could not, however, be detected in the egg yolk of either species of duck.

scholarly journals Studies on the subunit structure and amino acid sequence of triose phosphate isomerase from chicken breast muscle

1974 ◽  
Vol 139 (1) ◽  
pp. 11-22 ◽  
Author(s):  
Anna J. Furth ◽  
J. D. Milman ◽  
J. D. Priddle ◽  
R. E. Offord
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Triose Phosphate Isomerase ◽  
Breast Muscle ◽  
Chicken Breast ◽  
Rabbit Muscle ◽  
Tryptic Peptides ◽  
Amino Acid Compositions ◽  
Triose Phosphate

1. Triose phosphate isomerase was prepared by chromatography on DEAE-cellulose of an (NH4)2SO4 fraction of an extract of homogenized chicken breast muscle. The product is homogeneous on gel electrophoresis and is suitable for growing crystals for X-ray work. The specific activity is 10000 units/mg and the value for E0.1%280 is 1.20. 2. Comparison between the sum of the amino acid compositions of the tryptic peptides of the protein and the amino acid composition obtained on total hydrolysis of the protein indicates that the relative subunit mass is about 27000. 3. These data, together with the results of the examination of the amino acid compositions of a number of minor peptides, the number of peptides in the tryptic digest and the complete amino acid sequences of the tryptic peptides (the determination of which is described here), give no indication that the subunits are dissimilar. 4. A tentative amino acid sequence is presented for the protein, in which the ordering of the tryptic peptides is derived by homology with the sequence of the rabbit muscle enzyme (Corran & Waley, 1973). 5. An appendix describes the use that was made of mass spectrometry in the determination of some of the sequences. Mass-spectrometric data have been obtained for 35 residues, that is about 15% of the total sequence of the protein. 6. An extended version of the present paper has been deposited as Supplementary Publication SUP 50025 at the British Library, Lending Division (formerly the National Lending Library for Science and Technology), Boston Spa, Yorks. LS23 7BQ, U.K., from whom copies may be obtained on the terms given in Biochem. J. (1973) 131, 5.

scholarly journals Detection and Characterization of Cucumis melo Cryptic Virus, Cucumis melo Amalgavirus 1, and Melon Necrotic Spot Virus in Cucumis melo

Viruses ◽  
2019 ◽  
Vol 11 (1) ◽  
pp. 81 ◽  
Author(s):  
Binhui Zhan ◽  
Mengji Cao ◽  
Kaina Wang ◽  
Xifeng Wang ◽  
Xueping Zhou
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Sequence Alignment ◽  
Cucumis Melo ◽  
Amino Acid Sequence Identity ◽  
Phylogenetic Analyses ◽  
Necrotic Spot ◽  
Spot Virus ◽  
Cryptic Virus ◽  
Sequence Identity

Three RNA viruses—Cucumis melo cryptic virus (CmCV), Cucumis melo amalgavirus 1 (CmAV1), and melon necrotic spot virus (MNSV)—were identified from a melon (Cucumis melo) transcriptome dataset. CmCV has two dsRNA genome segments; dsRNA-1 is 1592 bp in size, containing a conserved RNA-dependent RNA polymerase (RdRp), and dsRNA-2 is 1715 bp in size, and encodes a coat protein (CP). The sequence alignment and phylogenetic analyses of the CmCV RdRp and CP indicated CmCV clusters with approved or putative deltapartitiviruses in well-supported monophyletic clade. The RdRp of CmCV shared an amino acid sequence identity of 60.7% with the closest RdRp of beet cryptic virus 3, and is <57% identical to other partitiviruses. CmAV1 is a nonsegmented dsRNA virus with a genome of 3424 bp, including two partially overlapping open reading frames (ORFs) encoding a putative CP and RdRp. The sequence alignment and phylogenetic analyses of CmAV1 RdRp revealed that it belongs to the genus Amalgavirus in the family Amalgaviridae. The RdRp of CmAV1 shares 57.7% of its amino acid sequence identity with the most closely related RdRp of Phalaenopsis equestris amalgavirus 1, and is <47% identical to the other reported amalgaviruses. These analyses suggest that CmCV and CmAV1 are novel species in the genera Amalgavirus and Deltapartitivirus, respectively. These findings enrich our understanding of new plant dsRNA virus species.

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