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  1. Article: Physicochemical properties of SARS‐CoV‐2 for drug targeting, virus inactivation and attenuation, vaccine formulation and quality control

    Scheller, Christin / Krebs, Finja / Minkner, Robert / Astner, Isabel / Gil‐Moles, Maria / Wätzig, Hermann

    Electrophoresis. 2020 July, v. 41, no. 13-14

    2020  

    Abstract: The material properties of the severe acute respiratory syndrome coronavirus 2 (SARS‐CoV‐2) and its proteins are discussed. We review the viral structure, size, rigidity, lipophilicity, isoelectric point, buoyant density and centrifugation conditions, ... ...

    Abstract The material properties of the severe acute respiratory syndrome coronavirus 2 (SARS‐CoV‐2) and its proteins are discussed. We review the viral structure, size, rigidity, lipophilicity, isoelectric point, buoyant density and centrifugation conditions, stability against pH, temperature, UV light, gamma radiation, and susceptibility to various chemical agents including solvents and detergents. Possible inactivation, downstream, and formulation conditions are given including suitable buffers and some first ideas for quality‐control methods. This information supports vaccine development and discussion with competent authorities during vaccine approval and is certainly related to drug‐targeting strategies and hygienics. Several instructive tables are given, including the pI and grand average of hydropathicity (GRAVY) of SARS‐CoV‐1 and ‐2 proteins in comparison. SARS‐CoV‐1 and SARS‐CoV‐2 are similar in many regards, so information can often be derived. Both are unusually stable, but sensitive at their lipophilic membranes. However, since seemingly small differences can have strong effects, for example, on immunologically relevant epitope settings, unevaluated knowledge transfer from SARS‐CoV‐1 to SARS‐CoV‐2 cannot be advised. Published knowledge regarding downstream processes, formulations and quality assuring methods is, as yet, limited. However, standard approaches employed for other viruses and vaccines seem to be feasible including virus inactivation, centrifugation conditions, and the use of adjuvants.
    Keywords Severe acute respiratory syndrome coronavirus ; Severe acute respiratory syndrome coronavirus 2 ; centrifugation ; electrophoresis ; epitopes ; gamma radiation ; isoelectric point ; lipophilicity ; pH ; quality control ; temperature ; ultraviolet radiation ; vaccine development ; vaccines ; viral morphology ; viruses
    Language English
    Dates of publication 2020-07
    Size p. 1137-1151.
    Publishing place John Wiley & Sons, Ltd
    Document type Article
    Note NAL-AP-2-clean ; REVIEW
    ZDB-ID 619001-7
    ISSN 1522-2683 ; 0173-0835
    ISSN (online) 1522-2683
    ISSN 0173-0835
    DOI 10.1002/elps.202000121
    Database NAL-Catalogue (AGRICOLA)

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  2. Article ; Online: Physicochemical properties of SARS-CoV-2 for drug targeting, virus inactivation and attenuation, vaccine formulation and quality control.

    Scheller, Christin / Krebs, Finja / Minkner, Robert / Astner, Isabel / Gil-Moles, Maria / Wätzig, Hermann

    Electrophoresis

    2020  Volume 41, Issue 13-14, Page(s) 1137–1151

    Abstract: The material properties of the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) and its proteins are discussed. We review the viral structure, size, rigidity, lipophilicity, isoelectric point, buoyant density and centrifugation conditions, ... ...

    Abstract The material properties of the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) and its proteins are discussed. We review the viral structure, size, rigidity, lipophilicity, isoelectric point, buoyant density and centrifugation conditions, stability against pH, temperature, UV light, gamma radiation, and susceptibility to various chemical agents including solvents and detergents. Possible inactivation, downstream, and formulation conditions are given including suitable buffers and some first ideas for quality-control methods. This information supports vaccine development and discussion with competent authorities during vaccine approval and is certainly related to drug-targeting strategies and hygienics. Several instructive tables are given, including the pI and grand average of hydropathicity (GRAVY) of SARS-CoV-1 and -2 proteins in comparison. SARS-CoV-1 and SARS-CoV-2 are similar in many regards, so information can often be derived. Both are unusually stable, but sensitive at their lipophilic membranes. However, since seemingly small differences can have strong effects, for example, on immunologically relevant epitope settings, unevaluated knowledge transfer from SARS-CoV-1 to SARS-CoV-2 cannot be advised. Published knowledge regarding downstream processes, formulations and quality assuring methods is, as yet, limited. However, standard approaches employed for other viruses and vaccines seem to be feasible including virus inactivation, centrifugation conditions, and the use of adjuvants.
    MeSH term(s) Animals ; Betacoronavirus/chemistry ; Betacoronavirus/drug effects ; Betacoronavirus/radiation effects ; Disinfectants/pharmacology ; Electrophoresis ; Hot Temperature ; Humans ; Hydrogen-Ion Concentration ; Isoelectric Point ; SARS-CoV-2 ; Ultraviolet Rays ; Vaccines, Attenuated/immunology ; Vaccines, Attenuated/pharmacology ; Viral Proteins/chemistry ; Viral Vaccines/immunology ; Viral Vaccines/pharmacology ; Virus Inactivation/radiation effects
    Chemical Substances Disinfectants ; Vaccines, Attenuated ; Viral Proteins ; Viral Vaccines
    Keywords covid19
    Language English
    Publishing date 2020-06-08
    Publishing country Germany
    Document type Journal Article ; Review
    ZDB-ID 619001-7
    ISSN 1522-2683 ; 0173-0835
    ISSN (online) 1522-2683
    ISSN 0173-0835
    DOI 10.1002/elps.202000121
    Database MEDical Literature Analysis and Retrieval System OnLINE

    Full text online

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1868: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

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  3. Book ; Thesis: Klonierung, Reinigung, Kristallisation und Strukturlösung der 5-Aminolävulinsäuresynthase und Untersuchung der Auswirkung und Behandelbarkeit von XLSA-Mutationen

    Astner, Isabel

    2007  

    Author's details von Isabel Astner
    Language German
    Size 137 S., Ill., graph. Darst.
    Document type Book ; Thesis
    Thesis / German Habilitation thesis Techn. Univ., Diss.--Braunschweig, 2007
    Database Library catalogue of the German National Library of Science and Technology (TIB), Hannover

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  4. Article: Physicochemical properties of SARS-CoV-2 for drug targeting, virus inactivation and attenuation, vaccine formulation and quality control

    Scheller, Christin / Krebs, Finja / Minkner, Robert / Astner, Isabel / Gil-Moles, Maria / Wätzig, Hermann

    Electrophoresis

    Abstract: The material properties of the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) and its proteins are discussed. We review the viral structure, size, rigidity, lipophilicity, isoelectric point, buoyant density and centrifugation conditions, ... ...

    Abstract The material properties of the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) and its proteins are discussed. We review the viral structure, size, rigidity, lipophilicity, isoelectric point, buoyant density and centrifugation conditions, stability against pH, temperature, UV light, gamma radiation, and susceptibility to various chemical agents including solvents and detergents. Possible inactivation, downstream, and formulation conditions are given including suitable buffers and some first ideas for quality-control methods. This information supports vaccine development and discussion with competent authorities during vaccine approval and is certainly related to drug-targeting strategies and hygienics. Several instructive tables are given, including the pI and grand average of hydropathicity (GRAVY) of SARS-CoV-1 and -2 proteins in comparison. SARS-CoV-1 and SARS-CoV-2 are similar in many regards, so information can often be derived. Both are unusually stable, but sensitive at their lipophilic membranes. However, since seemingly small differences can have strong effects, for example, on immunologically relevant epitope settings, unevaluated knowledge transfer from SARS-CoV-1 to SARS-CoV-2 cannot be advised. Published knowledge regarding downstream processes, formulations and quality assuring methods is, as yet, limited. However, standard approaches employed for other viruses and vaccines seem to be feasible including virus inactivation, centrifugation conditions, and the use of adjuvants.
    Keywords covid19
    Publisher WHO
    Document type Article
    Note WHO #Covidence: #32469436
    Database COVID19

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  5. Article ; Online: Physicochemical properties of SARS‐CoV‐2 for drug targeting, virus inactivation and attenuation, vaccine formulation and quality control

    Scheller, Christin / Krebs, Finja / Minkner, Robert / Astner, Isabel / Gil‐Moles, Maria / Wätzig, Hermann

    ELECTROPHORESIS

    2020  Volume 41, Issue 13-14, Page(s) 1137–1151

    Keywords Clinical Biochemistry ; Biochemistry ; covid19
    Language English
    Publisher Wiley
    Publishing country us
    Document type Article ; Online
    ZDB-ID 619001-7
    ISSN 1522-2683 ; 0173-0835
    ISSN (online) 1522-2683
    ISSN 0173-0835
    DOI 10.1002/elps.202000121
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

    Full text online

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    In stock of ZB MED Cologne/Königswinter

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  6. Article: Crystal structure of 5-aminolevulinate synthase, the first enzyme of heme biosynthesis, and its link to XLSA in humans.

    Astner, Isabel / Schulze, Jörg O / van den Heuvel, Joop / Jahn, Dieter / Schubert, Wolf-Dieter / Heinz, Dirk W

    The EMBO journal

    2005  Volume 24, Issue 18, Page(s) 3166–3177

    Abstract: 5-Aminolevulinate synthase (ALAS) is the first and rate-limiting enzyme of heme biosynthesis in humans, animals, other non-plant eukaryotes, and alpha-proteobacteria. It catalyzes the synthesis of 5-aminolevulinic acid, the first common precursor of all ... ...

    Abstract 5-Aminolevulinate synthase (ALAS) is the first and rate-limiting enzyme of heme biosynthesis in humans, animals, other non-plant eukaryotes, and alpha-proteobacteria. It catalyzes the synthesis of 5-aminolevulinic acid, the first common precursor of all tetrapyrroles, from glycine and succinyl-coenzyme A (sCoA) in a pyridoxal 5'-phosphate (PLP)-dependent manner. X-linked sideroblastic anemias (XLSAs), a group of severe disorders in humans characterized by inadequate formation of heme in erythroblast mitochondria, are caused by mutations in the gene for erythroid eALAS, one of two human genes for ALAS. We present the first crystal structure of homodimeric ALAS from Rhodobacter capsulatus (ALAS(Rc)) binding its cofactor PLP. We, furthermore, present structures of ALAS(Rc) in complex with the substrates glycine or sCoA. The sequence identity of ALAS from R. capsulatus and human eALAS is 49%. XLSA-causing mutations may thus be mapped, revealing the molecular basis of XLSA in humans. Mutations are found to obstruct substrate binding, disrupt the dimer interface, or hamper the correct folding. The structure of ALAS completes the structural analysis of enzymes in heme biosynthesis.
    MeSH term(s) 5-Aminolevulinate Synthetase/chemistry ; 5-Aminolevulinate Synthetase/metabolism ; Acyl Coenzyme A/chemistry ; Acyl Coenzyme A/metabolism ; Amino Acid Sequence ; Anemia, Sideroblastic/enzymology ; Anemia, Sideroblastic/genetics ; Binding Sites ; Crystallography, X-Ray ; Dimerization ; Genetic Diseases, X-Linked/enzymology ; Glycine/chemistry ; Glycine/metabolism ; Heme/biosynthesis ; Humans ; Models, Molecular ; Molecular Sequence Data ; Mutation/genetics ; Protein Structure, Quaternary ; Pyridoxal Phosphate/chemistry ; Pyridoxal Phosphate/metabolism ; Rhodobacter capsulatus/enzymology ; Sequence Alignment ; Substrate Specificity
    Chemical Substances Acyl Coenzyme A ; Heme (42VZT0U6YR) ; Pyridoxal Phosphate (5V5IOJ8338) ; succinyl-coenzyme A (BSI27HW5EQ) ; 5-Aminolevulinate Synthetase (EC 2.3.1.37) ; Glycine (TE7660XO1C)
    Language English
    Publishing date 2005-08-25
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 586044-1
    ISSN 1460-2075 ; 0261-4189
    ISSN (online) 1460-2075
    ISSN 0261-4189
    DOI 10.1038/sj.emboj.7600792
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 1808: Show issues Location:
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    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
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  7. Article: The substrate radical of Escherichia coli oxygen-independent coproporphyrinogen III oxidase HemN.

    Layer, Gunhild / Pierik, Antonio J / Trost, Matthias / Rigby, Steve E / Leech, Helen K / Grage, Katrin / Breckau, Daniela / Astner, Isabel / Jänsch, Lothar / Heathcote, Peter / Warren, Martin J / Heinz, Dirk W / Jahn, Dieter

    The Journal of biological chemistry

    2006  Volume 281, Issue 23, Page(s) 15727–15734

    Abstract: During porphyrin biosynthesis the oxygen-independent coproporphyrinogen III oxidase (HemN) catalyzes the oxidative decarboxylation of the propionate side chains of rings A and B of coproporphyrinogen III to form protoporphyrinogen IX. The enzyme utilizes ...

    Abstract During porphyrin biosynthesis the oxygen-independent coproporphyrinogen III oxidase (HemN) catalyzes the oxidative decarboxylation of the propionate side chains of rings A and B of coproporphyrinogen III to form protoporphyrinogen IX. The enzyme utilizes a 5'-deoxyadenosyl radical to initiate the decarboxylation reaction, and it has been proposed that this occurs by stereo-specific abstraction of the pro-S-hydrogen atom at the beta-position of the propionate side chains leading to a substrate radical. Here we provide EPR-spectroscopic evidence for intermediacy of the latter radical by observation of an organic radical EPR signal in reduced HemN upon addition of S-adenosyl-L-methionine and the substrate coproporphyrinogen III. This signal (g(av) = 2.0029) shows a complex pattern of well resolved hyperfine splittings from at least five different hydrogen atoms. The radical was characterized using regiospecifically labeled (deuterium or 15N) coproporphyrinogen III molecules. They had been generated from a multienzyme mixture and served as efficient substrates. Reaction of HemN with coproporphyrinogen III, perdeuterated except for the methyl groups, led to the complete loss of resolved proton hyperfine splittings. Substrates in which the hydrogens at both alpha- and beta-positions, or only at the beta-positions of the propionate side chains, or those of the methylene bridges, were deuterated showed that there is coupling with hydrogens at the alpha-, beta-, and methylene bridge positions. Deuterium or 15N labeling of the pyrrole nitrogens without labeling the side chains only led to a slight sharpening of the radical signal. Together, these observations clearly identified the radical signal as substrate-derived and indicated that, upon abstraction of the pro-S-hydrogen atom at the beta-position of the propionate side chain by the 5'-deoxyadenosyl radical, a comparatively stable delocalized substrate radical intermediate is formed in the absence of electron acceptors. The observed hyperfine constants and g values show that this coproporphyrinogenyl radical is allylic and encompasses carbon atoms 3', 3, and 4.
    MeSH term(s) Bacillus megaterium/enzymology ; Bacterial Proteins/metabolism ; Chromatography, High Pressure Liquid ; Coproporphyrinogen Oxidase/metabolism ; Electron Spin Resonance Spectroscopy ; Escherichia coli/enzymology ; Oxygen/metabolism ; Substrate Specificity
    Chemical Substances Bacterial Proteins ; HemN protein, Bacteria (EC 1.-.-.-) ; Coproporphyrinogen Oxidase (EC 1.3.3.3) ; Oxygen (S88TT14065)
    Language English
    Publishing date 2006-04-09
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.M512628200
    Database MEDical Literature Analysis and Retrieval System OnLINE

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