Evolutionary mode for the functional preservation of fast-evolving Drosophila telomere capping proteins

DNA end protection is fundamental for the long-term preservation of the genome. In vertebrates the Shelterin protein complex protects telomeric DNA ends, thereby contributing to the maintenance of genome integrity. In the Drosophila genus, this function is thought to be performed by the Terminin complex, an assembly of fast-evolving subunits. Considering that DNA end protection is fundamental for successful genome replication, the accelerated evolution of Terminin subunits is counterintuitive, as conservation is supposed to maintain the assembly and concerted function of the interacting partners. This problem extends over Drosophila telomere biology and provides insight into the evolution of protein assemblies. In order to learn more about the mechanistic details of this phenomenon we have investigated the intra- and interspecies assemblies of Verrocchio and Modigliani, two Terminin subunits using in vitro assays. Based on our results and on homology-based three-dimensional models for Ver and Moi, we conclude that both proteins contain Ob-fold and contribute to the ssDNA binding of the Terminin complex. We propose that the preservation of Ver function is achieved by conservation of specific amino acids responsible for folding or localized in interacting surfaces. We also provide here the first evidence on Moi DNA binding

Non-primate hepacivirus infection with apparent hepatitis in a horse — Short communication

Non-primate hepacivirus (NPHV) is a recently identified hepacivirus (family Flaviviridae) in dog and horse; however, the disease associations remain unknown. This study reports the detection of natural NPHV infection in a horse with apparent hepatitis, liver damage and high-level viraemia. NPHV could be hepatotropic and associated with hepatitis in horses

Seroprevalence and genotype distribution of hepatitis A virus in the pre-vaccine era in South Transdanubia, Hungary (2010-2020).

In this study, the age-related seroprevalence of hepatitis A virus (HAV) infection was investigated in the population in South-Transdanubia, Southwest Hungary (Central Europe) between years 2010 and 2020. Up to the age of 40, the HAV seropositivity was less than 18% in all age groups indicating a low level of HAV endemicity in this part of the country in the covered study period. The HAV seropositivity started to increase at the age group 41-45 years, reaching the ∼50% at age group 56-60, and 75-80% at age group 66-70, respectively. A total of 43 (0.2%) of the 21,106 tested sera were HAV IgM-positive (the annual percentage range of HAV IgM-positivity was 0.046-0.6%). Total of 24 (55.8%) of the 43 HAV IgM-positive samples tested RT-PCR-positive confirmed as HAV sub-genotypes IA (N = 17; 70.8%) and IB (N = 7; 29.2%), respectively. Imported HAV infections (three cases from Romania, and one-one case from Austria and Italy), two small outbreaks and 11 cases of a genetically identical sub-genotype IA strain (GenBank number of the prototype strain: KM657825) from 2012 to 2014 were identified later connected directly to the enormous HAV outbreak initiated among men who have sex with men (MSM) at the end of 2011 in the capital Budapest. In summary, low endemicity but high and increased susceptibility for HAV infection was found in the population in Southwest Hungary, where repeated introduction of sub-genotypes IA and IB HAV strains were identified between 2010 and 2020

Evolutionary mode for the functional preservation of fast-evolving Drosophila telomere capping proteins

DNA end protection is fundamental for the long-term preservation of the genome. In vertebrates the Shelterin protein complex protects telomeric DNA ends, thereby contributing to the maintenance of genome integrity. In the Drosophila genus, this function is thought to be performed by the Terminin complex, an assembly of fast-evolving subunits. Considering that DNA end protection is fundamental for successful genome replication, the accelerated evolution of Terminin subunits is counterintuitive, as conservation is supposed to maintain the assembly and concerted function of the interacting partners. This problem extends over Drosophila telomere biology and provides insight into the evolution of protein assemblies. In order to learn more about the mechanistic details of this phenomenon we have investigated the intra- and interspecies assemblies of Verrocchio and Modigliani, two Terminin subunits using in vitro assays. Based on our results and on homology-based three-dimensional models for Ver and Moi, we conclude that both proteins contain Ob-fold and contribute to the ssDNA binding of the Terminin complex. We propose that the preservation of Ver function is achieved by conservation of specific amino acids responsible for folding or localized in interacting surfaces. We also provide here the first evidence on Moi DNA binding

Nonsuppurative (Aseptic) Meningoencephalomyelitis Associated with Neurovirulent Astrovirus Infections in Humans and Animals

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