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Wilson, William C.,Hornig-Do, Hue-Tran,Bruni, Francesco,Chang, Jeong Ho,Jourdain, Alexis A.,Martinou, Jean-Claude,Falkenberg, Maria,Spå,hr, Henrik,Larsson, Nils-Gö,ran,Lewis, Richard J.,Hewit Oxford University Press 2014 Human Molecular Genetics Vol.23 No.23
<P>The p.N478D missense mutation in human mitochondrial poly(A) polymerase (mtPAP) has previously been implicated in a form of spastic ataxia with optic atrophy. In this study, we have investigated fibroblast cell lines established from family members. The homozygous mutation resulted in the loss of polyadenylation of all mitochondrial transcripts assessed; however, oligoadenylation was retained. Interestingly, this had differential effects on transcript stability that were dependent on the particular species of transcript. These changes were accompanied by a severe loss of oxidative phosphorylation complexes I and IV, and perturbation of <I>de novo</I> mitochondrial protein synthesis. Decreases in transcript polyadenylation and in respiratory chain complexes were effectively rescued by overexpression of wild-type mtPAP. Both mutated and wild-type mtPAP localized to the mitochondrial RNA-processing granules thereby eliminating mislocalization as a cause of defective polyadenylation. <I>In vitro</I> polyadenylation assays revealed severely compromised activity by the mutated protein, which generated only short oligo(A) extensions on RNA substrates, irrespective of RNA secondary structure. The addition of LRPPRC/SLIRP, a mitochondrial RNA-binding complex, enhanced activity of the wild-type mtPAP resulting in increased overall tail length. The LRPPRC/SLIRP effect although present was less marked with mutated mtPAP, independent of RNA secondary structure. We conclude that (i) the polymerase activity of mtPAP can be modulated by the presence of LRPPRC/SLIRP, (ii) N478D mtPAP mutation decreases polymerase activity and (iii) the alteration in poly(A) length is sufficient to cause dysregulation of post-transcriptional expression and the pathogenic lack of respiratory chain complexes.</P>
X-ray detections of submillimetre galaxies: active galactic nuclei versus starburst contribution
Johnson, S. P.,Wilson, G. W.,Wang, Q. D.,Williams, C. C.,Scott, K. S.,Yun, M. S.,Pope, A.,Lowenthal, J.,Aretxaga, I.,Hughes, D. Oxford University Press 2013 Monthly notices of the Royal Astronomical Society Vol.431 No.1
Type VI secretion is a major virulence determinant in <i>Burkholderia mallei</i>
Schell, Mark A.,Ulrich, Ricky L.,Ribot, Wilson J.,Brueggemann, Ernst E.,Hines, Harry B.,Chen, Dan,Lipscomb, Lyla,Kim, H. Stanley,Mrá,zek, Jan,Nierman, William C.,DeShazer, David Blackwell Publishing Ltd 2007 Molecular microbiology Vol.64 No.6
<P><B>Summary</B></P><P> <I>Burkholderia mallei</I> is a host‐adapted pathogen and a category B biothreat agent. Although the <I>B. mallei</I> VirAG two‐component regulatory system is required for virulence in hamsters, the virulence genes it regulates are unknown. Here we show with expression profiling that overexpression of <I>virAG</I> resulted in transcriptional activation of ∼60 genes, including some involved in capsule production, actin‐based intracellular motility, and type VI secretion (T6S). The 15 genes encoding the major sugar component of the homopolymeric capsule were up‐expressed > 2.5‐fold, but capsule was still produced in the absence of <I>virAG</I>. Actin tail formation required <I>virAG</I> as well as <I>bimB</I>, <I>bimC</I> and <I>bimE</I>, three previously uncharacterized genes that were activated four‐ to 15‐fold when VirAG was overproduced. Surprisingly, actin polymerization was found to be dispensable for virulence in hamsters. In contrast, genes encoding a T6S system were up‐expressed as much as 30‐fold and mutations in this T6S gene cluster resulted in strains that were avirulent in hamsters. SDS‐PAGE and mass spectrometry demonstrated that BMAA0742 was secreted by the T6S system when <I>virAG</I> was overexpressed. Purified His‐tagged BMAA0742 was recognized by glanders antiserum from a horse, a human and mice, indicating that this Hcp‐family protein is produced <I>in vivo</I> during infection.</P>
Immunogenicity and Efficacy of Schmallenberg Virus Envelope Glycoprotein Subunit Vaccines
Abaineh D. Endalew,Bonto Faburay,Jessie D. Trujillo,Natasha N. Gaudreault,A. Sally Davis,Vinay Shivanna,Sun-Young Sunwoo,Wenjun Ma,Barbara S. Drolet,D. Scott McVey,Igor Morozov,William C. Wilson,Juerg 대한수의학회 2019 Journal of Veterinary Science Vol.20 No.6
The Schmallenberg virus (SBV) is an orthobunyavirus that causes abortions, stillbirths, and congenital defects in pregnant sheep and cattle. Inactivated or live attenuated vaccines have been developed in endemic countries, but there is still interest in the development of SBV vaccines that would allow a differentiationng of infected from vaccinated animals (DIVA). Therefore, an attempt was made to develop novel DIVA-compatible SBV vaccines using SBV glycoproteins expressed in baculovirus. All vaccines and phosphate buffered saline (PBS) controls were prepared with adjuvant and administered subcutaneously to cattle at six6 months (Ed note: Numerals 1 to 9 are written in words.)of age. The first trial included two2 groups of animals vaccinated with either carboxyl-terminus glycoprotein (Gc) or PBS and boosted after two2 weeks. In the second trial, three3 groups of cattle were administered either Gc, Gc and Gnamino-terminus glycoprotein, or PBS with a booster vaccination after three3 weeks. The animals were challenged with the SBV nine9 days after the booster vaccination in the first study, and three3 weeks after the booster vaccination in the second study. Using SBV Gc-specific ELISAenzyme-linked immunosorbent assay, antibodies were first detected in serum samples 14 days after the first vaccination in both trials, and peaked on days seven7 and nine9 after the booster in the first and second trials, respectively. Low titers of neutralizing antibodies were detected in serum from only 3/6 and 2/4 animals in the first and second trial, respectively, at 14 days after the first vaccination. The titers increased 2 to 3-fold after the booster vaccination. On the other hand, SBV-specific RNA was detected in the serum and selective tissues in all animals after the challenge. The SBV candidate vaccines neither prevented viremia nor conferred protection against the SBV infection.