42 research outputs found

    125 GeV Higgs Boson from t-b-tau Yukawa Unification

    Full text link
    We identify a class of supersymmetric SU(4)_c x SU(2)_L x SU(2)_R models in which imposing essentially perfect t-b-tau Yukawa coupling unification at M_GUT yields a mass close to 122-126 GeV for the lightest CP-even (SM-like) Higgs boson. The squark and gluino masses in these models exceed 3 TeV, but the stau and charginos in some cases can be considerably lighter. We display some benchmark points corresponding to neutralino-stau and bino-wino coannihilations as well as A-resonance. The well-known MSSM parameter tan beta is around 46-52.Comment: 16 pages, 4 figure

    Valuing the investigation of Prion diseases in Ethiopia

    No full text
    Cellular Prion proteins have a wide variety of function from the birth of a cell to its programmed death. Prion protein can be the cause for a number of lethal animal and human diseases when misfolded. Furthermore, prion infection is transmissible. Polymorphisms of prion gene at different loci are associated with prion diseases development, the onset of symptoms and incubation period. Indel polymorphism in the promoter region of PRNP gene is found to be accoaited to BSE in cattle while the haplotype ARR at positions 136,154 and 171 is resistant to scrapie in sheep. Taking into account the severity of prion disease and its potential entrance to the food chain, genetic and clinical studies continued to be conducted in a different course of time in many countries. Even though African countries in general and Ethiopia in particular, are highly dependent on animals and animal products as food and income source, there are neither epidemiologic nor genetic studies addressed prion diseases yet. Moreover, high animal product consumption and poor regular animal health inspection are among the many good reasons to study prion in Ethiopia. Prion disease survey and prion gene profiling boldly contribute to the provision of prion-free animals to the market for local consumption and for export. Thus, the main objective of this work is to uncover the extent of the importance of prion-related studies in Ethiopia considering livestock management, food quality safeguard and contribution of the work for further study.</p

    Analysis of prion protein coding gene polymorphisms in palestinian native sheep breeds [Filistin yerli koyun ırklarında prion protein kodlama geni polimorfizmlerinin analizi]

    No full text
    2-s2.0-85077080786Prion protein coding gene (PRNP) is the genetic locus correlated with the greatest impact on classical scrapie susceptibility in sheep. At codons 136, 154, and 171 of PRNP alanine/arginine/glutamine (ARQ) and valine/arginine/glutamine (VRQ) haplotypes, in turn, are related to susceptibility to classical scrapie while alanine/arginine/arginine ARR haplotype is correlated with resistance. The aim of the present study was to genotype the Palestinian native sheep breeds for detection of genetic resistance. A total of 38 healthy sheep from Awassi and Assaf breeds were randomly sampled. Genomic DNA was isolated from blood samples. After PCR amplification and DNA sequencing, ARQ, ARR, ARH, AHQ, ARL and VRQ alleles and ARR/ARQ, ARQ/ARQ, ARQ/ARL, ARH/ARQ, ARH/ARL, AHQ/ARQ and ARQ/VRQ genotypes were detected in PRNP gene. ARQ allele was found as a predominant allele in this study with the frequency of 0.76 for Awassi and Assaf breeds while the uncommon allele ARL was identified at low frequencies in both breeds. In addition, two different polymorphisms were recognized (V12I and L23H) at different codons of PRNP. Results have indicated that most of the genotypes belong to risk group 3. The careful dissemination of ARR/ARR sheep is suggested to increase resistant allele frequencies in Assaf and Awassi breeds. © 2019, Chartered Inst. of Building Services Engineers. All rights reserved.Ege Ãœniversitesi Firat University Scientific Research Projects Management Unit, FÃœBAP: 2016-FEN-013Scientific Research Projects of Ege University with a project number 2016-FEN-013. 10th International Animal Science Conference, 26-28 October 2018, Antalya, Turkey.This study is the master thesis of the first author and was supported by Scientific Research Projects of Ege University with a project number 2016-FEN-013. The summary of this research was presented in 10th International Animal Science Conference, 26-28 October 2018, Antalya, Turkey

    In silico discovery of epitopes of gag and env proteins for the development of a multi-epitope vaccine candidate against Maedi Visna Virus using reverse vaccinology approach

    No full text
    Maedi Visna Virus (MVV) causes a chronic viral disease in sheep. Since there is no specific therapeutic drug that targets MVV, development of a vaccine against the MVV is inevitable. This study aimed to analyze the gag and env proteins as vaccine candidate proteins and to identify epitopes in these proteins. In addition, it was aimed to construct a multi-epitope vaccine candidate. According to the obtained results, the gag protein was detected to be more conserved and had a higher antigenicity value. Also, the number of alpha helix in the secondary structure was higher and transmembrane helices were not detected. Although many B cell and MHC-I/II epitopes were predicted, only 19 of them were detected to have the properties of antigenic, non-allergenic, non-toxic, soluble, and non-hemolytic. Of these epitopes, five were remarkable due to having the highest antigenicity value. However, the final multi-epitope vaccine was constructed with 19 epitopes. A strong affinity was shown between the final multi-epitope vaccine and TLR-2/4. In conclusion, the gag protein was a better antigen. However, both proteins had epitopes with high antigenicity value. Also, the final multi-epitope vaccine construct had a potential to be used as a peptide vaccine due to its immuno-informatics results. © 2023 International Alliance for Biological StandardizationThis study was supported by a project given by the Ege University Scientific Research Projects Coordination Unit (Project number: TGA-2022-23604) to C.Ü .Ege Üniversitesi: TGA-2022-2360
    corecore