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  1. Article: Hydrogenosomal succinyl-CoA synthetase from the rumen-dwelling fungus Neocallimastix patriciarum; an energy-producing enzyme of mitochondrial origin.

    Dacks, Joel B / Dyal, Patricia L / Embley, T Martin / van der Giezen, Mark

    Gene

    2006  Volume 373, Page(s) 75–82

    Abstract: Hydrogenosomes are hydrogen-producing organelles that are related to mitochondria and found in a variety of evolutionarily unrelated anaerobic microbial eukaryotes. Similar to classic mitochondria, hydrogenosomes contain the enzyme catalyzing the only ... ...

    Abstract Hydrogenosomes are hydrogen-producing organelles that are related to mitochondria and found in a variety of evolutionarily unrelated anaerobic microbial eukaryotes. Similar to classic mitochondria, hydrogenosomes contain the enzyme catalyzing the only reaction of the citric acid cycle directly producing energy; succinyl-CoA synthetase. We have isolated and characterized the genes encoding both subunits of this enzyme from the anaerobic chytrid fungus Neocallimastix patriciarum, a model organism in hydrogenosome research. Both subunits contain all characteristic features of this enzyme, including predicted hydrogenosomal targeting signals. Phylogenetic analyses of succinyl-CoA synthetase clearly indicate its mitochondrial ancestry, both by affiliation with mitochondrially localized fungal homologues and by the sisterhood of the eukaryotic succinyl-CoA synthetase clade with alpha-proteobacteria. Our analyses of the Trichomonas vaginalis SCS sequences also confirmed the mitochondrial affiliation of these hydrogenosomal enzymes, in contrast to previous results. While both hydrogenosomal and mitochondrial succinyl-CoA synthetase homologues have been identified, no succinyl-CoA synthetase proteins were identifiable in taxa possessing another mitochondrially derived organelle, the mitosome. Our analyses further confirm the mitochondrial ancestry of the Neocallimastix hydrogenosome and sheds light upon the stepwise process by which mitochondria evolve into alternate forms of the organelle.
    MeSH term(s) Amino Acid Sequence ; Animals ; Base Sequence ; Cloning, Molecular ; Mitochondria/enzymology ; Models, Biological ; Molecular Sequence Data ; Neocallimastix/enzymology ; Neocallimastix/genetics ; Organelles/enzymology ; Phylogeny ; Sequence Homology, Amino Acid ; Succinate-CoA Ligases/genetics
    Chemical Substances Succinate-CoA Ligases (EC 6.2.1.-)
    Language English
    Publishing date 2006-05-24
    Publishing country Netherlands
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 391792-7
    ISSN 1879-0038 ; 0378-1119
    ISSN (online) 1879-0038
    ISSN 0378-1119
    DOI 10.1016/j.gene.2006.01.012
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    In stock of ZB MED Cologne/Königswinter

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  2. Article: Mitochondria and hydrogenosomes are two forms of the same fundamental organelle.

    Embley, T Martin / van der Giezen, Mark / Horner, David S / Dyal, Patricia L / Foster, Peter

    Philosophical transactions of the Royal Society of London. Series B, Biological sciences

    2003  Volume 358, Issue 1429, Page(s) 191–201; discussion 201–2

    Abstract: Published data suggest that hydrogenosomes, organelles found in diverse anaerobic eukaryotes that make energy and hydrogen, were once mitochondria. As hydrogenosomes generally lack a genome, the conversion is probably one way. The sources of the key ... ...

    Abstract Published data suggest that hydrogenosomes, organelles found in diverse anaerobic eukaryotes that make energy and hydrogen, were once mitochondria. As hydrogenosomes generally lack a genome, the conversion is probably one way. The sources of the key hydrogenosomal enzymes, pyruvate : ferredoxin oxidoreductase (PFO) and hydrogenase, are not resolved by current phylogenetic analyses, but it is likely that both were present at an early stage of eukaryotic evolution. Once thought to be restricted to a few unusual anaerobic eukaryotes, the proteins are intimately integrated into the fabric of diverse eukaryotic cells, where they are targeted to different cell compartments, and not just hydrogenosomes. There is no evidence supporting the view that PFO and hydrogenase originated from the mitochondrial endosymbiont, as posited by the hydrogen hypothesis for eukaryogenesis. Other organelles derived from mitochondria have now been described in anaerobic and parasitic microbial eukaryotes, including species that were once thought to have diverged before the mitochondrial symbiosis. It thus seems possible that all eukaryotes may eventually be shown to contain an organelle of mitochondrial ancestry, to which different types of biochemistry can be targeted. It remains to be seen if, despite their obvious differences, this family of organelles shares a common function of importance for the eukaryotic cell, other than energy production, that might provide the underlying selection pressure for organelle retention.
    MeSH term(s) Anaerobiosis ; Biological Evolution ; Eukaryotic Cells/cytology ; Eukaryotic Cells/enzymology ; Eukaryotic Cells/metabolism ; Hydrogen/metabolism ; Hydrogenase/genetics ; Hydrogenase/metabolism ; Mitochondria/metabolism ; Organelles/metabolism ; Phylogeny
    Chemical Substances Hydrogen (7YNJ3PO35Z) ; Hydrogenase (EC 1.12.7.2)
    Language English
    Publishing date 2003-01-29
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 208382-6
    ISSN 1471-2970 ; 0962-8436 ; 0080-4622 ; 0264-3839
    ISSN (online) 1471-2970
    ISSN 0962-8436 ; 0080-4622 ; 0264-3839
    DOI 10.1098/rstb.2002.1190
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  3. Article ; Online: A genomic survey of the fish parasite Spironucleus salmonicida indicates genomic plasticity among diplomonads and significant lateral gene transfer in eukaryote genome evolution

    Logsdon John M / Svärd Staffan G / Murphy Colleen A / Dyal Patricia L / Horner David S / Sjögren Åsa M / Andersson Jan O / Ragan Mark A / Hirt Robert P / Roger Andrew J

    BMC Genomics, Vol 8, Iss 1, p

    2007  Volume 51

    Abstract: Abstract Background Comparative genomic studies of the mitochondrion-lacking protist group Diplomonadida (diplomonads) has been lacking, although Giardia lamblia has been intensively studied. We have performed a sequence survey project resulting in 2341 ... ...

    Abstract Abstract Background Comparative genomic studies of the mitochondrion-lacking protist group Diplomonadida (diplomonads) has been lacking, although Giardia lamblia has been intensively studied. We have performed a sequence survey project resulting in 2341 expressed sequence tags (EST) corresponding to 853 unique clones, 5275 genome survey sequences (GSS), and eleven finished contigs from the diplomonad fish parasite Spironucleus salmonicida (previously described as S. barkhanus ). Results The analyses revealed a compact genome with few, if any, introns and very short 3' untranslated regions. Strikingly different patterns of codon usage were observed in genes corresponding to frequently sampled ESTs versus genes poorly sampled, indicating that translational selection is influencing the codon usage of highly expressed genes. Rigorous phylogenomic analyses identified 84 genes – mostly encoding metabolic proteins – that have been acquired by diplomonads or their relatively close ancestors via lateral gene transfer (LGT). Although most acquisitions were from prokaryotes, more than a dozen represent likely transfers of genes between eukaryotic lineages. Many genes that provide novel insights into the genetic basis of the biology and pathogenicity of this parasitic protist were identified including 149 that putatively encode variant-surface cysteine-rich proteins which are candidate virulence factors. A number of genomic properties that distinguish S. salmonicida from its human parasitic relative G. lamblia were identified such as nineteen putative lineage-specific gene acquisitions, distinct mutational biases and codon usage and distinct polyadenylation signals. Conclusion Our results highlight the power of comparative genomic studies to yield insights into the biology of parasitic protists and the evolution of their genomes, and suggest that genetic exchange between distantly-related protist lineages may be occurring at an appreciable rate in eukaryote genome evolution.
    Keywords Genetics ; QH426-470 ; Biology (General) ; QH301-705.5 ; Science ; Q ; DOAJ:Genetics ; DOAJ:Biology ; DOAJ:Biology and Life Sciences ; Biotechnology ; TP248.13-248.65
    Subject code 572
    Language English
    Publishing date 2007-02-01T00:00:00Z
    Publisher BioMed Central
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  4. Article: Hydrogenosomes, mitochondria and early eukaryotic evolution.

    Embley, T Martin / van der Giezen, Mark / Horner, David S / Dyal, Patricia L / Bell, Samantha / Foster, Peter G

    IUBMB life

    2003  Volume 55, Issue 7, Page(s) 387–395

    Abstract: Available data suggest that unusual organelles called hydrogenosomes, that make ATP and hydrogen, and which are found in diverse anaerobic eukaryotes, were once mitochondria. The evolutionary origins of the enzymes used to make hydrogen, pyruvate: ... ...

    Abstract Available data suggest that unusual organelles called hydrogenosomes, that make ATP and hydrogen, and which are found in diverse anaerobic eukaryotes, were once mitochondria. The evolutionary origins of the enzymes used to make hydrogen, pyruvate:ferredoxin oxidoreductase (PFO) and hydrogenase, are unresolved, but it seems likely that both were present at an early stage of eukaryotic evolution. Once thought to be restricted to a few unusual anaerobes, these proteins are found in diverse eukaryotic cells, including our own, where they are targeted to different cell compartments. Organelles related to mitochondria and hydrogenosomes have now been found in species of anaerobic and parasitic protozoa that were previously thought to have separated from other eukaryotes before the mitochondrial endosymbiosis. Thus it is possible that all eukaryotes may eventually be shown to contain an organelle of mitochondrial ancestry, bearing testimony to the important role that the mitochondrial endosymbiosis has played in eukaryotic evolution. It remains to be seen if members of this family of organelles share a common function essential to the eukaryotic cell, that provides the underlying selection pressure for organelle retention under different living conditions.
    MeSH term(s) Adenosine Triphosphate/metabolism ; Animals ; Biological Evolution ; COS Cells ; Eukaryotic Cells/pathology ; Ferritins/metabolism ; Hydrogen/chemistry ; Hydrogen/metabolism ; Mitochondria/metabolism ; Mitochondria/pathology ; Organelles ; Oxidoreductases/metabolism ; Phylogeny ; Saccharomyces cerevisiae/metabolism ; Time Factors ; Transfection
    Chemical Substances Hydrogen (7YNJ3PO35Z) ; Adenosine Triphosphate (8L70Q75FXE) ; Ferritins (9007-73-2) ; Oxidoreductases (EC 1.-)
    Language English
    Publishing date 2003-07
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S. ; Research Support, U.S. Gov't, P.H.S. ; Review
    ZDB-ID 1492141-8
    ISSN 1521-6551 ; 1521-6543
    ISSN (online) 1521-6551
    ISSN 1521-6543
    DOI 10.1080/15216540310001592834
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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1611: Show issues Location:
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  5. Article ; Online: A genomic survey of the fish parasite Spironucleus salmonicida indicates genomic plasticity among diplomonads and significant lateral gene transfer in eukaryote genome evolution.

    Andersson, Jan O / Sjögren, Asa M / Horner, David S / Murphy, Colleen A / Dyal, Patricia L / Svärd, Staffan G / Logsdon, John M / Ragan, Mark A / Hirt, Robert P / Roger, Andrew J

    BMC genomics

    2007  Volume 8, Page(s) 51

    Abstract: Background: Comparative genomic studies of the mitochondrion-lacking protist group Diplomonadida (diplomonads) has been lacking, although Giardia lamblia has been intensively studied. We have performed a sequence survey project resulting in 2341 ... ...

    Abstract Background: Comparative genomic studies of the mitochondrion-lacking protist group Diplomonadida (diplomonads) has been lacking, although Giardia lamblia has been intensively studied. We have performed a sequence survey project resulting in 2341 expressed sequence tags (EST) corresponding to 853 unique clones, 5275 genome survey sequences (GSS), and eleven finished contigs from the diplomonad fish parasite Spironucleus salmonicida (previously described as S. barkhanus).
    Results: The analyses revealed a compact genome with few, if any, introns and very short 3' untranslated regions. Strikingly different patterns of codon usage were observed in genes corresponding to frequently sampled ESTs versus genes poorly sampled, indicating that translational selection is influencing the codon usage of highly expressed genes. Rigorous phylogenomic analyses identified 84 genes--mostly encoding metabolic proteins--that have been acquired by diplomonads or their relatively close ancestors via lateral gene transfer (LGT). Although most acquisitions were from prokaryotes, more than a dozen represent likely transfers of genes between eukaryotic lineages. Many genes that provide novel insights into the genetic basis of the biology and pathogenicity of this parasitic protist were identified including 149 that putatively encode variant-surface cysteine-rich proteins which are candidate virulence factors. A number of genomic properties that distinguish S. salmonicida from its human parasitic relative G. lamblia were identified such as nineteen putative lineage-specific gene acquisitions, distinct mutational biases and codon usage and distinct polyadenylation signals.
    Conclusion: Our results highlight the power of comparative genomic studies to yield insights into the biology of parasitic protists and the evolution of their genomes, and suggest that genetic exchange between distantly-related protist lineages may be occurring at an appreciable rate in eukaryote genome evolution.
    MeSH term(s) Amino Acid Sequence ; Animals ; Base Composition ; Base Sequence ; Codon/genetics ; Databases, Genetic ; Diplomonadida/classification ; Diplomonadida/genetics ; Eukaryotic Cells/metabolism ; Evolution, Molecular ; Expressed Sequence Tags ; Fishes/parasitology ; Gene Transfer, Horizontal/genetics ; Genes, Protozoan/genetics ; Genome, Protozoan ; Molecular Sequence Data ; Phylogeny ; Sequence Alignment ; Sequence Analysis, DNA/methods
    Chemical Substances Codon
    Language English
    Publishing date 2007-02-14
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2041499-7
    ISSN 1471-2164 ; 1471-2164
    ISSN (online) 1471-2164
    ISSN 1471-2164
    DOI 10.1186/1471-2164-8-51
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  6. Article: Fungal hydrogenosomes contain mitochondrial heat-shock proteins.

    van der Giezen, Mark / Birdsey, Graeme M / Horner, David S / Lucocq, John / Dyal, Patricia L / Benchimol, Marlene / Danpure, Christopher J / Embley, T Martin

    Molecular biology and evolution

    2003  Volume 20, Issue 7, Page(s) 1051–1061

    Abstract: At least three groups of anaerobic eukaryotes lack mitochondria and instead contain hydrogenosomes, peculiar organelles that make energy and excrete hydrogen. Published data indicate that ciliate and trichomonad hydrogenosomes share common ancestry with ... ...

    Abstract At least three groups of anaerobic eukaryotes lack mitochondria and instead contain hydrogenosomes, peculiar organelles that make energy and excrete hydrogen. Published data indicate that ciliate and trichomonad hydrogenosomes share common ancestry with mitochondria, but the evolutionary origins of fungal hydrogenosomes have been controversial. We have now isolated full-length genes for heat shock proteins 60 and 70 from the anaerobic fungus Neocallimastix patriciarum, which phylogenetic analyses reveal share common ancestry with mitochondrial orthologues. In aerobic organisms these proteins function in mitochondrial import and protein folding. Homologous antibodies demonstrated the localization of both proteins to fungal hydrogenosomes. Moreover, both sequences contain amino-terminal extensions that in heterologous targeting experiments were shown to be necessary and sufficient to locate both proteins and green fluorescent protein to the mitochondria of mammalian cells. This finding, that fungal hydrogenosomes use mitochondrial targeting signals to import two proteins of mitochondrial ancestry that play key roles in aerobic mitochondria, provides further strong evidence that the fungal organelle is also of mitochondrial ancestry. The extraordinary capacity of eukaryotes to repeatedly evolve hydrogen-producing organelles apparently reflects a general ability to modify the biochemistry of the mitochondrial compartment.
    MeSH term(s) Amino Acid Sequence ; Animals ; Chaperonin 60/genetics ; Green Fluorescent Proteins ; HSP70 Heat-Shock Proteins/genetics ; Hydrogen/metabolism ; Luminescent Proteins/metabolism ; Mitochondria/genetics ; Molecular Sequence Data ; Neocallimastix/genetics ; Phylogeny ; Sequence Homology, Amino Acid
    Chemical Substances Chaperonin 60 ; HSP70 Heat-Shock Proteins ; Luminescent Proteins ; Green Fluorescent Proteins (147336-22-9) ; Hydrogen (7YNJ3PO35Z)
    Language English
    Publishing date 2003-07
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 998579-7
    ISSN 1537-1719 ; 0737-4038
    ISSN (online) 1537-1719
    ISSN 0737-4038
    DOI 10.1093/molbev/msg103
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  7. Article: Conserved properties of hydrogenosomal and mitochondrial ADP/ATP carriers: a common origin for both organelles.

    van der Giezen, Mark / Slotboom, Dirk Jan / Horner, David S / Dyal, Patricia L / Harding, Marilyn / Xue, Gang-Ping / Embley, T Martin / Kunji, Edmund R S

    The EMBO journal

    2002  Volume 21, Issue 4, Page(s) 572–579

    Abstract: Mitochondria are one of the hallmarks of eukaryotic cells, exporting ATP in exchange for cytosolic ADP using ADP/ATP carriers (AAC) located in the inner mitochondrial membrane. In contrast, several evolutionarily important anaerobic eukaryotes lack ... ...

    Abstract Mitochondria are one of the hallmarks of eukaryotic cells, exporting ATP in exchange for cytosolic ADP using ADP/ATP carriers (AAC) located in the inner mitochondrial membrane. In contrast, several evolutionarily important anaerobic eukaryotes lack mitochondria but contain hydrogenosomes, peculiar organelles of controversial ancestry that also supply ATP but, like some fermentative bacteria, make molecular hydrogen in the process. We have now identified genes from two species of the hydrogenosome-containing fungus Neocallimastix that have three-fold sequence repeats and signature motifs that, along with phylogenetic analysis, identify them as AACs. When expressed in a mitochondrial AAC- deficient yeast strain, the hydrogenosomal protein was correctly targeted to the yeast mitochondria inner membrane and yielded mitochondria able to perform ADP/ATP exchange. Characteristic inhibitors of mitochondrial AACs blocked adenine nucleotide exchange by the Neocallimastix protein. Thus, our data demonstrate that fungal hydrogenosomes and yeast mitochondria use the same pathway for ADP/ATP exchange. These experiments provide some of the strongest evidence yet that yeast mitochondria and Neocallimastix hydrogenosomes are but two manifestations of the same fundamental organelle.
    MeSH term(s) Adenosine Diphosphate/metabolism ; Adenosine Triphosphate/metabolism ; Amino Acid Sequence ; Animals ; Base Sequence ; Cloning, Molecular ; DNA Primers ; Genetic Complementation Test ; Humans ; Hydrogen/metabolism ; Mitochondria/metabolism ; Mitochondrial ADP, ATP Translocases/chemistry ; Mitochondrial ADP, ATP Translocases/genetics ; Mitochondrial ADP, ATP Translocases/metabolism ; Molecular Sequence Data ; Phylogeny ; Saccharomyces cerevisiae/genetics ; Sequence Homology, Amino Acid
    Chemical Substances DNA Primers ; Adenosine Diphosphate (61D2G4IYVH) ; Hydrogen (7YNJ3PO35Z) ; Adenosine Triphosphate (8L70Q75FXE) ; Mitochondrial ADP, ATP Translocases (9068-80-8)
    Language English
    Publishing date 2002-02-06
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S. ; Research Support, U.S. Gov't, P.H.S.
    ZDB-ID 586044-1
    ISSN 1460-2075 ; 0261-4189
    ISSN (online) 1460-2075
    ISSN 0261-4189
    DOI 10.1093/emboj/21.4.572
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  8. Article ; Online: Evaluating the Effects of SARS-CoV-2 Spike Mutation D614G on Transmissibility and Pathogenicity

    Volz, Erik / Hill, Verity / McCrone, John T. / Price, Anna / Jorgensen, David / O’Toole, Áine / Southgate, Joel / Johnson, Robert / Jackson, Ben / Nascimento, Fabricia F. / Rey, Sara M. / Nicholls, Samuel M. / Colquhoun, Rachel M. / da Silva Filipe, Ana / Shepherd, James / Pascall, David J. / Shah, Rajiv / Jesudason, Natasha / Li, Kathy /
    Jarrett, Ruth / Pacchiarini, Nicole / Bull, Matthew / Geidelberg, Lily / Siveroni, Igor / Goodfellow, Ian / Loman, Nicholas J. / Pybus, Oliver G. / Robertson, Dave / Thomson, Emma C. / Rambaut, Andrew / Connor, Thomas R. / Koshy, Cherian / Wise, Emma / Cortes, Nick / Lynch, Jessica / Kidd, Stephen / Mori, Matilde / Fairley, Derek J. / Curran, Tanya / McKenna, James P. / Adams, Helen / Fraser, Christophe / Golubchik, Tanya / Bonsall, David / Moore, Catrin / Caddy, Sarah L. / Khokhar, Fahad A. / Wantoch, Michelle / Reynolds, Nicola / Warne, Ben / Maksimovic, Joshua / Spellman, Karla / McCluggage, Kathryn / John, Michaela / Beér, Robert / Afifi, Safiah / Morgan, Siân / Marchbank, Angela / Kitchen, C. / Gulliver, Huw / Merrick, Ian / Guest, Martyn / Munn, Robert / Workman, Trudy / Fuller, William / Bresner, Catherine / Snell, Luke B. / Charalampous, Themoula / Nebbia, Gaia / Batra, Rahul / Edgeworth, Jonathan / Robson, Samuel C. / Beckett, Angela / Loveson, Katie F. / Aanensen, David M. / Underwood, Anthony P. / Yeats, Corin A. / Abudahab, Khalil / Taylor, Ben E.W. / Menegazzo, Mirko / Clark, Gemma / Smith, Wendy / Khakh, Manjinder / Fleming, Vicki M. / Lister, Michelle M. / Howson-Wells, Hannah C. / Berry, Louise / Boswell, Tim / Joseph, Amelia / Willingham, Iona / Bird, Paul / Helmer, Thomas / Fallon, Karlie / Holmes, Christopher / Tang, Julian / Raviprakash, Veena / Campbell, Sharon / Sheriff, Nicola / Loose, Matthew W. / Holmes, Nadine / Moore, Christopher / Carlile, Matthew / Wright, Victoria / Sang, Fei / Debebe, Johnny / Coll, Francesc / Signell, Adrian W. / Betancor, Gilberto / Wilson, Harry D. / Feltwell, Theresa / Houldcroft, Charlotte J. / Eldirdiri, Sahar / Kenyon, Anita / Davis, Thomas / Pybus, Oliver / Du Plessis, L. / Zarebski, Alex / Raghwani, Jayna / Kraemer, Moritz / Francois, Sarah / Attwood, Stephen / Vasylyeva, Tetyana / Török, Estée / Hamilton, William L. / Goodfellow, Ian G. / Hall, Grant / Jahun, Aminu S. / Chaudhry, Yasmin / Hosmillo, Myra / Pinckert, Malte L. / Georgana, Iliana / Yakovleva, Anna / Meredith, Luke W. / Moses, S. / Lowe, Hannah / Ryan, Felicity / Fisher, Chloe L. / Awan, Ali R. / Boyes, John / Breuer, Judith / Harris, Kathryn Ann / Brown, Julianne Rose / Shah, Divya / Atkinson, Laura / Lee, Jack C.D. / Alcolea-Medina, Adela / Moore, Nathan / Cortes, Nicholas / Williams, Rebecca / Chapman, Michael R. / Levett, Lisa J. / Heaney, Judith / Smith, Darren L. / Bashton, Matthew / Young, Gregory R. / Allan, John / Loh, Joshua / Randell, Paul A. / Cox, Ali / Madona, Pinglawathee / Holmes, Alison / Bolt, Frances / Price, James / Mookerjee, Siddharth / Rowan, Aileen / Taylor, Graham P. / Ragonnet-Cronin, Manon / Johnson, Rob / Boyd, Olivia / Volz, Erik M. / Brunker, Kirstyn / Smollett, Katherine L. / Quick, Joshua / McMurray, Claire / Stockton, Joanne / Nicholls, Sam / Rowe, William / Poplawski, Radoslaw / Martinez-Nunez, Rocio T. / Mason, Jenifer / Robinson, Trevor I. / O'Toole, Elaine / Watts, Joanne / Breen, Cassie / Cowell, Angela / Ludden, Catherine / Sluga, Graciela / Machin, Nicholas W. / Ahmad, Shazaad S.Y. / George, Ryan P. / Halstead, Fenella / Sivaprakasam, Venkat / Shepherd, James G. / Asamaphan, Patawee / Niebel, Marc O. / Li, Kathy K. / Shah, Rajiv N. / Jesudason, Natasha G. / Parr, Yasmin A. / Tong, Lily / Broos, Alice / Mair, Daniel / Nichols, Jenna / Carmichael, Stephen N. / Nomikou, Kyriaki / Aranday-Cortes, Elihu / Johnson, NaTasha / Starinskij, Igor / Orton, Richard J. / Hughes, Joseph / Vattipally, Sreenu / Singer, Joshua B. / Hale, Antony D. / Macfarlane-Smith, Louissa R. / Harper, Katherine L. / Taha, Yusri / Payne, Brendan A.I. / Burton-Fanning, Shirelle / Waugh, Sheila / Collins, Jennifer / Eltringham, Gary / Templeton, Kate E. / McHugh, Martin P. / Dewar, Rebecca / Wastenge, Elizabeth / Dervisevic, Samir / Stanley, Rachael / Prakash, Reenesh / Stuart, Claire / Elumogo, Ngozi / Sethi, Dheeraj K. / Meader, Emma J. / Coupland, Lindsay J. / Potter, Will / Graham, Clive / Barton, Edward / Padgett, Debra / Scott, Garren / Swindells, Emma / Greenaway, Jane / Nelson, Andrew / Yew, Wen C. / Resende Silva, Paola C. / Andersson, Monique / Shaw, Robert / Peto, Timothy / Justice, Anita / Eyre, David / Crooke, Derrick / Hoosdally, Sarah / Sloan, Tim J. / Duckworth, Nichola / Walsh, Sarah / Chauhan, Anoop J. / Glaysher, Sharon / Bicknell, Kelly / Wyllie, Sarah / Butcher, Ethan / Elliott, Scott / Lloyd, Allyson / Impey, Robert / Levene, Nick / Monaghan, Lynn / Bradley, Declan T. / Allara, Elias / Pearson, Clare / Muir, Peter / Vipond, Ian B. / Hopes, Richard / Pymont, Hannah M. / Hutchings, Stephanie / Curran, Martin D. / Parmar, Surendra / Lackenby, Angie / Mbisa, Tamyo / Platt, Steven / Miah, Shâhjahân / Bibby, David / Manso, Carmen / Hubb, Jonathan / Chand, Meera / Dabrera, Gavin / Ramsay, Mary / Bradshaw, Daniel / Thornton, Alicia / Myers, Richard / Schaefer, Ulf / Groves, Natalie / Gallagher, Eileen / Lee, David / Williams, David / Ellaby, Nicholas / Harrison, Ian / Hartman, Hassan / Manesis, Nikos / Patel, Vineet / Bishop, Chloe / Chalker, Vicki / Osman, Husam / Bosworth, Andrew / Robinson, Esther / Holden, Matthew T.G. / Shaaban, Sharif / Birchley, Alec / Adams, Alexander / Davies, Alisha / Gaskin, Amy / Plimmer, Amy / Gatica-Wilcox, Bree / McKerr, Caoimhe / Moore, Catherine / Williams, Chris / Heyburn, David / De Lacy, Elen / Hilvers, Ember / Downing, Fatima / Shankar, Giri / Jones, Hannah / Asad, Hibo / Coombes, Jason / Watkins, Joanne / Evans, Johnathan M. / Fina, Laia / Gifford, Laura / Gilbert, Lauren / Graham, Lee / Perry, Malorie / Morgan, Mari / Cronin, Michelle / Craine, Noel / Jones, Rachel / Howe, Robin / Corden, Sally / Rey, Sara / Kumziene-Summerhayes, Sara / Taylor, Sarah / Cottrell, Simon / Jones, Sophie / Edwards, Sue / O’Grady, Justin / Page, Andrew J. / Wain, John / Webber, Mark A. / Mather, Alison E. / Baker, David J. / Rudder, Steven / Yāsir, Muḥammad / Thomson, Nicholas M. / Aydin, Alp / Tedim, Ana P. / Kay, Gemma L. / Trotter, Alexander J. / Gilroy, Rachel A.J. / Alikhan, Nabil-Fareed / de Oliveira Martins, Leonardo / Le-Viet, Thanh / Meadows, Lizzie / Kolyva, Anastasia / Diaz, Maria / Bell, Andrew / Gutierrez, Ana Victoria / Charles, Ian G. / Adriaenssens, Evelien M. / Kingsley, Robert A. / Casey, Anna / Simpson, D. A. / Molnár, Zoltán / Thompson, Thomas / Acheson, Erwan / Masoli, Jane A.H. / Knight, Bridget A. / Hattersley, Andrew / Ellard, Sian / Auckland, Cressida / Mahungu, Tabitha W. / Irish-Tavares, Dianne / Haque, Tanzina / Bourgeois, Yann / Scarlett, Garry P. / Partridge, David G. / Raza, Mohammad / Evans, Cariad / Johnson, Kate / Liggett, Steven / Baker, Paul / Essex, Sarah / Lyons, Ronan A. / Caller, Laura G. / Castellano, Sergi / Williams, Rachel J. / Kristiansen, Mark / Roy, Sunando / Williams, Charlotte A. / Dyal, Patricia L. / Tutill, Helena J. / Panchbhaya, Yasmin N. / Forrest, Leysa M. / Niola, Paola / Findlay, Jacqueline / Brooks, Tony T. / Gavriil, Artemis / Mestek-Boukhibar, Lamia / Weeks, Sam / Pandey, Sarojini / Berry, Lisa / Jones, K. E. / Richter, Alex / Beggs, Andrew / Smith, Colin P. / Bucca, Giselda / Hesketh, Andrew R. / Harrison, Ewan M. / Peacock, Sharon J. / Eser, Sophie / Churcher, Carol M. / Bellis, Katherine L. / Girgis, Sophia T. / Naydenova, Plamena / Blane, Beth / Sridhar, Sushmita / Ruis, Chris / Forrest, Sally / Cormie, Claire / Gill, Harmeet K. / Dias, Joana / Higginson, Ellen E. / Maes, Mailis / Young, Jamie / Kermack, Leanne M. / Hadjirin, Nazreen F. / Aggarwal, Dinesh / Griffith, Luke / Swingler, Tracey / Davidson, Rose K. / Williams, Thomas / Balcazar, Carlos E. / Gallagher, Michael D. / O'Toole, Áine / Rooke, Stefan / Colquhoun, Rachel / Ashworth, Jordan / McCrone, J.T. / Scher, Emily / Yu, Xiaoyu / Williamson, Kathleen A. / Stanton, Thomas D. / Michell, Stephen L. / Bewshea, Claire M. / Temperton, Ben / Michelsen, Michelle L. / Warwick-Dugdale, Joanna / Manley, Robin / Farbos, Audrey / Harrison, James W. / Sambles, Christine M. / Studholme, David J. / Jeffries, Aaron R. / Darby, Alistair C. / Hiscox, Julian A. / Paterson, Steve / Iturriza-Gomara, Miren / Jackson, Kathryn A. / Lucaci, Anita O. / Vamos, Edith E. / Hughes, Margaret / Rainbow, Lucille / Eccles, Richard / Nelson, Charlotte / Whitehead, Mark / Turtle, Lance / Haldenby, Sam T. / Gregory, Richard / Gemmell, Matthew / Kwiatkowski, Dominic / de Silva, Thushan I. / Smith, Nikki / Angyal, Adrienn / Lindsey, Benjamin B. / Groves, Danielle C. / Green, Luke R. / Wang, Dennis / Freeman, Timothy M. / Parker, Matthew D. / Keeley, Alexander J. / Parsons, Paul J. / Tucker, Rachel M. / Brown, Rebecca / Wyles, Matthew / Constantinidou, Chrystala / Unnikrishnan, Meera / Ott, Sascha / Cheng, Jeffrey K.J. / Bridgewater, Hannah E. / Frost, Lucy R. / Taylor-Joyce, Grace / Stark, Richard / Baxter, Laura / Alam, Mohammad T. / Brown, Paul E. / McClure, Patrick C. / Chappell, Joseph G. / Tsoleridis, Theocharis / Ball, Jonathan / Gramatopoulos, Dimitris / Buck, David / Todd, John A. / Green, Angie / Trebes, Amy / MacIntyre-Cockett, George / de Cesare, Mariateresa / Langford, Cordelia / Alderton, Alex / Amato, Roberto / Goncalves, Sonia / Jackson, David K. / Johnston, Ian / Sillitoe, John / Palmer, Steve / Lawniczak, Mara / Berriman, Matt / Danesh, John / Livett, Rich / Shirley, Lesley / Farr, Ben / Quail, Mike / Thurston, Scott / Park, Naomi / Betteridge, Emma / Weldon, Danni / Goodwin, Scott / Nelson, Rachel / Beaver, Charlotte / Letchford, Laura / Jackson, David A. / Foulser, Luke / McMinn, Liz / Prestwood, Liam / Kay, Sally / Kane, Leanne / Dorman, Matthew J. / Martincorena, Inigo / Puethe, Christoph / Keatley, Jon-Paul / Tonkin-Hill, Gerry / Smith, Christen / Jamrozy, Dorota / Beale, Mathew A. / Patel, Minal / Ariani, Cristina / Spencer-Chapman, Michael / Drury, Eleanor / Lo, Stephanie / Rajatileka, Shavanthi / Scott, Carol / James, Keith / Buddenborg, Sarah K. / Berger, Duncan J. / Patel, Gaurang / Garcia-Casado, Maria V. / Dibling, Thomas / McGuigan, Samantha / Rogers, Hazel A. / Hunter, Adam D. / Souster, Emily / Neaverson, Alexandra S.

    Cell. 2021 Jan. 07, v. 184, no. 1 p.64-75.e11

    2021  

    Abstract: Global dispersal and increasing frequency of the SARS-CoV-2 spike protein variant D614G are suggestive of a selective advantage but may also be due to a random founder effect. We investigate the hypothesis for positive selection of spike D614G in the ... ...

    Institution COG-UK Consortium
    Abstract Global dispersal and increasing frequency of the SARS-CoV-2 spike protein variant D614G are suggestive of a selective advantage but may also be due to a random founder effect. We investigate the hypothesis for positive selection of spike D614G in the United Kingdom using more than 25,000 whole genome SARS-CoV-2 sequences. Despite the availability of a large dataset, well represented by both spike 614 variants, not all approaches showed a conclusive signal of positive selection. Population genetic analysis indicates that 614G increases in frequency relative to 614D in a manner consistent with a selective advantage. We do not find any indication that patients infected with the spike 614G variant have higher COVID-19 mortality or clinical severity, but 614G is associated with higher viral load and younger age of patients. Significant differences in growth and size of 614G phylogenetic clusters indicate a need for continued study of this variant.
    Keywords COVID-19 infection ; Severe acute respiratory syndrome coronavirus 2 ; data collection ; founder effect ; genetic analysis ; genome ; mortality ; mutation ; pathogenicity ; phylogeny ; viral load ; United Kingdom ; COVID-19 ; SARS-CoV-2 ; evolution ; epidemiology ; spike
    Language English
    Dates of publication 2021-0107
    Size p. 64-75.e11.
    Publishing place Elsevier Inc.
    Document type Article ; Online
    Note NAL-AP-2-clean
    ZDB-ID 187009-9
    ISSN 1097-4172 ; 0092-8674
    ISSN (online) 1097-4172
    ISSN 0092-8674
    DOI 10.1016/j.cell.2020.11.020
    Database NAL-Catalogue (AGRICOLA)

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