LIVIVO - The Search Portal for Life Sciences

zur deutschen Oberfläche wechseln
Advanced search

Search results

Result 1 - 6 of total 6

Search options

  1. Article ; Online: Tandem sialoglycan-binding modules in a

    Stubbs, Haley E / Bensing, Barbara A / Yamakawa, Izumi / Sharma, Pankaj / Yu, Hai / Chen, Xi / Sullam, Paul M / Iverson, T M

    The Journal of biological chemistry

    2020  Volume 295, Issue 43, Page(s) 14737–14749

    Abstract: ... ...

    Abstract S
    MeSH term(s) Adhesins, Bacterial/chemistry ; Adhesins, Bacterial/metabolism ; Amino Acid Motifs ; Binding Sites ; Crystallography, X-Ray ; Glycoproteins/chemistry ; Glycoproteins/metabolism ; Host-Pathogen Interactions ; Humans ; Protein Binding ; Protein Conformation ; Protein Domains ; Sialic Acid Binding Immunoglobulin-like Lectins/chemistry ; Sialic Acid Binding Immunoglobulin-like Lectins/metabolism ; Streptococcal Infections/metabolism ; Streptococcus sanguis/chemistry ; Streptococcus sanguis/physiology
    Chemical Substances Adhesins, Bacterial ; Glycoproteins ; Sialic Acid Binding Immunoglobulin-like Lectins
    Language English
    Publishing date 2020-08-20
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.RA120.014177
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Uc I Zs.108: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  2. Article ; Online: Origins of glycan selectivity in streptococcal Siglec-like adhesins suggest mechanisms of receptor adaptation.

    Bensing, Barbara A / Stubbs, Haley E / Agarwal, Rupesh / Yamakawa, Izumi / Luong, Kelvin / Solakyildirim, Kemal / Yu, Hai / Hadadianpour, Azadeh / Castro, Manuel A / Fialkowski, Kevin P / Morrison, KeAndreya M / Wawrzak, Zdzislaw / Chen, Xi / Lebrilla, Carlito B / Baudry, Jerome / Smith, Jeremy C / Sullam, Paul M / Iverson, T M

    Nature communications

    2022  Volume 13, Issue 1, Page(s) 2753

    Abstract: Bacterial binding to host receptors underlies both commensalism and pathogenesis. Many streptococci adhere to protein-attached carbohydrates expressed on cell surfaces using Siglec-like binding regions (SLBRs). The precise glycan repertoire recognized ... ...

    Abstract Bacterial binding to host receptors underlies both commensalism and pathogenesis. Many streptococci adhere to protein-attached carbohydrates expressed on cell surfaces using Siglec-like binding regions (SLBRs). The precise glycan repertoire recognized may dictate whether the organism is a strict commensal versus a pathogen. However, it is currently not clear what drives receptor selectivity. Here, we use five representative SLBRs and identify regions of the receptor binding site that are hypervariable in sequence and structure. We show that these regions control the identity of the preferred carbohydrate ligand using chimeragenesis and single amino acid substitutions. We further evaluate how the identity of the preferred ligand affects the interaction with glycoprotein receptors in human saliva and plasma samples. As point mutations can change the preferred human receptor, these studies suggest how streptococci may adapt to changes in the environmental glycan repertoire.
    MeSH term(s) Adhesins, Bacterial/chemistry ; Humans ; Ligands ; Polysaccharides/metabolism ; Sialic Acid Binding Immunoglobulin-like Lectins/metabolism ; Streptococcus/metabolism
    Chemical Substances Adhesins, Bacterial ; Ligands ; Polysaccharides ; Sialic Acid Binding Immunoglobulin-like Lectins
    Language English
    Publishing date 2022-05-18
    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, N.I.H., Extramural
    ZDB-ID 2553671-0
    ISSN 2041-1723 ; 2041-1723
    ISSN (online) 2041-1723
    ISSN 2041-1723
    DOI 10.1038/s41467-022-30509-y
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  3. Article ; Online: An alternative N-terminal fold of the intestine-specific annexin A13a induces dimerization and regulates membrane-binding.

    McCulloch, Kathryn M / Yamakawa, Izumi / Shifrin, David A / McConnell, Russell E / Foegeding, Nora J / Singh, Prashant K / Mao, Suli / Tyska, Matthew J / Iverson, T M

    The Journal of biological chemistry

    2019  Volume 294, Issue 10, Page(s) 3454–3463

    Abstract: Annexin proteins function as ... ...

    Abstract Annexin proteins function as Ca
    MeSH term(s) Animals ; Annexins/chemistry ; Annexins/metabolism ; Cell Membrane/metabolism ; Epithelial Cells/cytology ; Humans ; Hydrogen-Ion Concentration ; Intestinal Mucosa/metabolism ; Intestines ; Liposomes/metabolism ; Mice ; Models, Molecular ; Organ Specificity ; Protein Binding ; Protein Conformation, alpha-Helical ; Protein Multimerization ; Protein Structure, Quaternary ; Protein Transport
    Chemical Substances ANXA13 protein, human ; Annexins ; Anxa13 protein, mouse ; Liposomes
    Language English
    Publishing date 2019-01-04
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.RA118.004571
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Uc I Zs.108: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  4. Article ; Online: The Structure of the Bifunctional Everninomicin Biosynthetic Enzyme EvdMO1 Suggests Independent Activity of the Fused Methyltransferase-Oxidase Domains.

    Starbird, C A / Perry, Nicole A / Chen, Qiuyan / Berndt, Sandra / Yamakawa, Izumi / Loukachevitch, Lioudmila V / Limbrick, Emilianne M / Bachmann, Brian O / Iverson, T M / McCulloch, Kathryn M

    Biochemistry

    2018  Volume 57, Issue 50, Page(s) 6827–6837

    Abstract: Members of the orthosomycin family of natural products are decorated polysaccharides with potent antibiotic activity and complex biosynthetic pathways. The defining feature of the orthosomycins is an orthoester linkage between carbohydrate moieties that ... ...

    Abstract Members of the orthosomycin family of natural products are decorated polysaccharides with potent antibiotic activity and complex biosynthetic pathways. The defining feature of the orthosomycins is an orthoester linkage between carbohydrate moieties that is necessary for antibiotic activity and is likely formed by a family of conserved oxygenases. Everninomicins are octasaccharide orthosomycins produced by Micromonospora carbonacea that have two orthoester linkages and a methylenedioxy bridge, three features whose formation logically requires oxidative chemistry. Correspondingly, the evd gene cluster encoding everninomicin D encodes two monofunctional nonheme iron, α-ketoglutarate-dependent oxygenases and one bifunctional enzyme with an N-terminal methyltransferase domain and a C-terminal oxygenase domain. To investigate whether the activities of these domains are linked in the bifunctional enzyme EvdMO1, we determined the structure of the N-terminal methyltransferase domain to 1.1 Å and that of the full-length protein to 3.35 Å resolution. Both domains of EvdMO1 adopt the canonical folds of their respective superfamilies and are connected by a short linker. Each domain's active site is oriented such that it faces away from the other domain, and there is no evidence of a channel connecting the two. Our results support EvdMO1 working as a bifunctional enzyme with independent catalytic activities.
    MeSH term(s) Amino Acid Sequence ; Aminoglycosides/biosynthesis ; Aminoglycosides/chemistry ; Bacterial Proteins/chemistry ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Biosynthetic Pathways ; Catalytic Domain ; Conserved Sequence ; Crystallography, X-Ray ; Gene Fusion ; Genes, Bacterial ; Methyltransferases/chemistry ; Methyltransferases/genetics ; Methyltransferases/metabolism ; Micromonospora/enzymology ; Micromonospora/genetics ; Models, Molecular ; Oxygenases/chemistry ; Oxygenases/genetics ; Oxygenases/metabolism ; Protein Interaction Domains and Motifs ; Sequence Homology, Amino Acid
    Chemical Substances Aminoglycosides ; Bacterial Proteins ; evernimicin (5X287491KH) ; Oxygenases (EC 1.13.-) ; Methyltransferases (EC 2.1.1.-)
    Language English
    Publishing date 2018-12-07
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 1108-3
    ISSN 1520-4995 ; 0006-2960
    ISSN (online) 1520-4995
    ISSN 0006-2960
    DOI 10.1021/acs.biochem.8b00836
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 217: 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)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  5. Article: A quantitative method for analyzing establishing-efficiency of persistent viral infection.

    Ito, Morihiro / Yamakawa, Izumi / Nishio, Machiko / Tsurudome, Masato / Kawano, Mitsuo / Komada, Hiroshi / Ito, Yasuhiko

    Microbiology and immunology

    2009  Volume 53, Issue 5, Page(s) 259–265

    Abstract: A quantitative method for analyzing establishing-efficiency of persistent infection was devised. The efficiency of hPIV2 CA and SV5 T1 strains was found to be high, that is, 0.1 approximately 0.3 (an efficiency of 1.0 indicates that 100% of the virus- ... ...

    Abstract A quantitative method for analyzing establishing-efficiency of persistent infection was devised. The efficiency of hPIV2 CA and SV5 T1 strains was found to be high, that is, 0.1 approximately 0.3 (an efficiency of 1.0 indicates that 100% of the virus-infected cells became persistently infected). The efficiency of the SV5 WR strain was also high, approximately 0.1, though the virus had no ability to immediately establish a steady state of persistent infection in whole cell-culture systems. At about 0.0007, the efficiency of SV41 was almost the same as that of the hPIV2 Toshiba strain. The establishing efficiencies of various rSeV were further analyzed in detail. The efficiencies of the rSeV(PA), rSeV(Ppi) and rSeV(HNpi) were below the limit of detection, while that of rSeV(Lpi) was nearly 1. Although the efficiency was around 0.001, the rSeV(Mpi) and the rSeV(Fpi) were unexpectedly found to be capable of forming persistently-infected cells, indicating that both the Fpi and Mpi proteins contribute to the establishing efficiency of persistent infection of SeVpi.
    MeSH term(s) Animals ; Cercopithecus aethiops ; Chick Embryo ; Guinea Pigs ; HeLa Cells ; Humans ; Paramyxoviridae Infections/virology ; Paramyxovirinae/physiology ; Vero Cells ; Viral Proteins/analysis ; Virus Cultivation/methods
    Chemical Substances Viral Proteins
    Language English
    Publishing date 2009-05
    Publishing country Australia
    Document type Evaluation Studies ; Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 224792-6
    ISSN 1348-0421 ; 0385-5600
    ISSN (online) 1348-0421
    ISSN 0385-5600
    DOI 10.1111/j.1348-0421.2009.00122.x
    Database MEDical Literature Analysis and Retrieval System OnLINE

    Full text online

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Ud II Zs.204: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  6. Article: Failure of multinucleated giant cell formation in k562 cells infected with newcastle disease virus and human parainfluenza type 2 virus.

    Yamakawa, Izumi / Tsurudome, Masato / Kawano, Mitsuo / Nishio, Machiko / Komada, Hiroshi / Ito, Morihiro / Uji, Yukitaka / Ito, Yasuhiko

    Microbiology and immunology

    2007  Volume 51, Issue 6, Page(s) 601–608

    Abstract: When K562 cells were infected with Newcastle disease virus (NDV) or human parainfluenza type 2 virus (hPIV-2), polykaryocyte formation could not be detected. Failure of multinucleated giant cell formation in K562 cells infected with either NDV or hPIV-2 ... ...

    Abstract When K562 cells were infected with Newcastle disease virus (NDV) or human parainfluenza type 2 virus (hPIV-2), polykaryocyte formation could not be detected. Failure of multinucleated giant cell formation in K562 cells infected with either NDV or hPIV-2 is due to disturbance of the viral envelope-cell fusion step or to defect in the cell-cell fusion step, respectively. Especially, NDV completely replicated in K562 cells, and the hemagglutinin-neuraminidase and fusion proteins expressed on the cell surface of NDV-infected K562 cell were fully functional for fusion inducing activity. Therefore, the cell membranes of K562 cells are considered to be resistant to virus-induced cell fusion. Membrane fusion is regulated by many host factors including membrane fluidity, cytoskeletal systems, and fusion regulatory proteins system. An unknown regulatory mechanism of virus-induced cell fusion may function on the cell surface of K562 cells.
    MeSH term(s) Electrophoresis, Polyacrylamide Gel ; Flow Cytometry ; Giant Cells/pathology ; Giant Cells/virology ; HeLa Cells ; Humans ; K562 Cells ; Newcastle disease virus/metabolism ; Newcastle disease virus/physiology ; Parainfluenza Virus 2, Human/genetics ; Parainfluenza Virus 2, Human/metabolism ; Parainfluenza Virus 2, Human/physiology ; Paramyxoviridae Infections/metabolism ; Paramyxoviridae Infections/pathology ; Paramyxoviridae Infections/virology ; RNA, Viral/chemistry ; RNA, Viral/genetics ; Reverse Transcriptase Polymerase Chain Reaction ; U937 Cells ; Viral Proteins/metabolism ; Virus Replication
    Chemical Substances RNA, Viral ; Viral Proteins
    Language English
    Publishing date 2007-01-11
    Publishing country Australia
    Document type Journal Article
    ZDB-ID 224792-6
    ISSN 1348-0421 ; 0385-5600
    ISSN (online) 1348-0421
    ISSN 0385-5600
    DOI 10.1111/j.1348-0421.2007.tb03946.x
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Ud II Zs.204: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

To top