LIVIVO - The Search Portal for Life Sciences

zur deutschen Oberfläche wechseln
Advanced search

Search results

Result 1 - 10 of total 161

Search options

  1. Article ; Online: Staphylococcus aureus TarP: A Brick in the Wall or Rosetta Stone?

    Missiakas, Dominique

    Cell host & microbe

    2019  Volume 25, Issue 2, Page(s) 182–183

    Abstract: Staphylococcus aureus infection elicits antibodies against wall teichoic acid (WTA). Several glycosyltransferases modify WTA to generate anomeric heterogeneity. In recent work, Gerlach et al. (2018) show that modification by prophage-encoded TarP ... ...

    Abstract Staphylococcus aureus infection elicits antibodies against wall teichoic acid (WTA). Several glycosyltransferases modify WTA to generate anomeric heterogeneity. In recent work, Gerlach et al. (2018) show that modification by prophage-encoded TarP diminishes WTA immunogenicity, allowing staphylococci to evade host adaptive immune responses, and propose to exploit these insights for vaccines.
    MeSH term(s) Adaptive Immunity ; Antibodies ; Cell Wall/chemistry ; Cell Wall/immunology ; Glycosyltransferases ; Humans ; Staphylococcal Infections/immunology ; Staphylococcal Infections/microbiology ; Staphylococcus aureus/immunology ; Streptococcal Vaccines ; Teichoic Acids/immunology
    Chemical Substances Antibodies ; Streptococcal Vaccines ; Teichoic Acids ; Glycosyltransferases (EC 2.4.-)
    Language English
    Publishing date 2019-02-19
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2278004-X
    ISSN 1934-6069 ; 1931-3128
    ISSN (online) 1934-6069
    ISSN 1931-3128
    DOI 10.1016/j.chom.2019.01.013
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 6578: 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: Processing of LtaS restricts LTA assembly and YSIRK preprotein trafficking into

    Ibrahim, Amany M / Azam, Muhammad S / Schneewind, Olaf / Missiakas, Dominique

    mBio

    2024  Volume 15, Issue 2, Page(s) e0285223

    Abstract: Septal membranes ... ...

    Abstract Septal membranes of
    MeSH term(s) Humans ; Staphylococcus aureus/metabolism ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Lipopolysaccharides/metabolism ; Teichoic Acids/metabolism ; Staphylococcal Infections ; Nitric Oxide Synthase/metabolism
    Chemical Substances lipoteichoic acid (56411-57-5) ; Bacterial Proteins ; Lipopolysaccharides ; Teichoic Acids ; Nitric Oxide Synthase (EC 1.14.13.39)
    Language English
    Publishing date 2024-01-04
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2557172-2
    ISSN 2150-7511 ; 2161-2129
    ISSN (online) 2150-7511
    ISSN 2161-2129
    DOI 10.1128/mbio.02852-23
    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: The Type 7b Secretion System of S. aureus and Its Role in Colonization and Systemic Infection.

    Bobrovskyy, Maksym / Chen, Xinhai / Missiakas, Dominique

    Infection and immunity

    2023  Volume 91, Issue 5, Page(s) e0001523

    Abstract: Staphylococcus aureus bears a type 7b secretion system (T7bSS) that assembles in the bacterial envelope to promote the secretion of WXG-like proteins and toxic effectors bearing LXG domains. Cognate immunity proteins bind cytosolic effectors to mute ... ...

    Abstract Staphylococcus aureus bears a type 7b secretion system (T7bSS) that assembles in the bacterial envelope to promote the secretion of WXG-like proteins and toxic effectors bearing LXG domains. Cognate immunity proteins bind cytosolic effectors to mute their toxicity prior to secretion. T7b-secreted factors have been associated with the pathogenesis of staphylococcal disease and intraspecies competition. We identified earlier strain WU1, an S. aureus ST88 isolate that caused outbreaks of skin and soft tissue infections in mouse breeding facilities. WU1 was also found to persistently colonize the nasopharynx of animals, suggesting a strong host adaptation. In this manner, WU1 colonization and infectivity in mice resembles that of methicillin-sensitive and -resistant S. aureus strains in humans, where nasal carriage is a major risk factor for invasive infections. Here, animals were colonized with wild-type or T7-deficient WU1 strains or combinations thereof. Absence of the T7bSS did not affect colonization in the nasopharynx of animals, and although fluctuations were observed in weekly samplings, the wild-type strain did not replace the T7-deficient strain in cocolonization experiments. Bloodstream infection with a T7b-deficient strain resulted in enhanced survival and reduced bacterial loads and abscesses in soft tissues compared to infection with wild-type WU1. Together, experiments using a mouse-adapted strain suggest that the T7bSS of S. aureus is an important contributor to the pathogenesis of invasive disease.
    MeSH term(s) Humans ; Animals ; Staphylococcus aureus ; Methicillin-Resistant Staphylococcus aureus ; Staphylococcal Infections/microbiology ; Skin ; Sepsis
    Language English
    Publishing date 2023-04-11
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 218698-6
    ISSN 1098-5522 ; 0019-9567
    ISSN (online) 1098-5522
    ISSN 0019-9567
    DOI 10.1128/iai.00015-23
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 684: 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.

  4. Article ; Online: Selective Host Cell Death by

    Missiakas, Dominique / Winstel, Volker

    Frontiers in immunology

    2021  Volume 11, Page(s) 621733

    Abstract: Host cell death programs are fundamental processes that shape cellular homeostasis, embryonic development, and tissue regeneration. Death signaling and downstream host cell responses are not only critical to guide mammalian development, they often act as ...

    Abstract Host cell death programs are fundamental processes that shape cellular homeostasis, embryonic development, and tissue regeneration. Death signaling and downstream host cell responses are not only critical to guide mammalian development, they often act as terminal responses to invading pathogens. Here, we briefly review and contrast how invading pathogens and specifically
    MeSH term(s) Animals ; Cell Death/immunology ; Hematopoietic Stem Cells/immunology ; Humans ; Immune Evasion ; Immune Tolerance ; Staphylococcal Infections/immunology ; Staphylococcal Infections/pathology ; Staphylococcus aureus/immunology ; Staphylococcus aureus/pathogenicity ; Virulence Factors/immunology
    Chemical Substances Virulence Factors
    Language English
    Publishing date 2021-01-21
    Publishing country Switzerland
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2606827-8
    ISSN 1664-3224 ; 1664-3224
    ISSN (online) 1664-3224
    ISSN 1664-3224
    DOI 10.3389/fimmu.2020.621733
    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.

  5. Article ; Online: Engineered human antibodies for the opsonization and killing of

    Chen, Xinhai / Schneewind, Olaf / Missiakas, Dominique

    Proceedings of the National Academy of Sciences of the United States of America

    2022  Volume 119, Issue 4

    Abstract: Gram-positive organisms with their thick envelope cannot be lysed by complement alone. Nonetheless, antibody-binding on the surface can recruit complement and mark these invaders for uptake and killing by phagocytes, a process known as opsonophagocytosis. ...

    Abstract Gram-positive organisms with their thick envelope cannot be lysed by complement alone. Nonetheless, antibody-binding on the surface can recruit complement and mark these invaders for uptake and killing by phagocytes, a process known as opsonophagocytosis. The crystallizable fragment of immunoglobulins (Fcγ) is key for complement recruitment. The cell surface of
    MeSH term(s) Amino Acid Sequence ; Antibodies, Bacterial/genetics ; Antibodies, Bacterial/immunology ; Antibodies, Monoclonal/genetics ; Antibodies, Monoclonal/immunology ; Antibody-Dependent Cell Cytotoxicity/immunology ; Complement Activation ; Dose-Response Relationship, Drug ; Dose-Response Relationship, Immunologic ; Humans ; Opsonization/immunology ; Phagocytosis/immunology ; Protein Binding ; Protein Engineering/methods ; Protein Interaction Domains and Motifs/genetics ; Protein Interaction Domains and Motifs/immunology ; Receptors, Fc/genetics ; Staphylococcal Protein A/immunology ; Staphylococcus aureus/immunology
    Chemical Substances Antibodies, Bacterial ; Antibodies, Monoclonal ; Receptors, Fc ; Staphylococcal Protein A
    Language English
    Publishing date 2022-01-17
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 209104-5
    ISSN 1091-6490 ; 0027-8424
    ISSN (online) 1091-6490
    ISSN 0027-8424
    DOI 10.1073/pnas.2114478119
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 1148: 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.

  6. Article ; Online: Contribution of TagA-Like Glycosyltransferases to the Assembly of the Secondary Cell Wall Polysaccharide in Bacillus anthracis.

    Tomatsidou, Anastasia / Krunic, Maria / Missiakas, Dominique

    Journal of bacteriology

    2022  Volume 204, Issue 9, Page(s) e0025322

    Abstract: Bacillus anthracis elaborates a secondary cell wall polysaccharide (SCWP) made of 6 to 12 trisaccharide units. Pyruvyl and acetyl substitutions of the distal unit are prerequisites for the noncovalent retention of 22 ... ...

    Abstract Bacillus anthracis elaborates a secondary cell wall polysaccharide (SCWP) made of 6 to 12 trisaccharide units. Pyruvyl and acetyl substitutions of the distal unit are prerequisites for the noncovalent retention of 22 secreted
    MeSH term(s) Bacillus anthracis/metabolism ; Bacterial Proteins/metabolism ; Cell Wall/metabolism ; Glycosyltransferases/genetics ; Glycosyltransferases/metabolism ; Membrane Glycoproteins/metabolism ; Polymers ; Polysaccharides/metabolism ; Sugars/metabolism ; Trisaccharides/chemistry ; Uridine Diphosphate/analysis ; Uridine Diphosphate/metabolism
    Chemical Substances Bacterial Proteins ; Membrane Glycoproteins ; Polymers ; Polysaccharides ; Sugars ; Trisaccharides ; Uridine Diphosphate (58-98-0) ; Glycosyltransferases (EC 2.4.-)
    Language English
    Publishing date 2022-08-23
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 2968-3
    ISSN 1098-5530 ; 0021-9193
    ISSN (online) 1098-5530
    ISSN 0021-9193
    DOI 10.1128/jb.00253-22
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Ud II Zs.50: 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.

  7. Article ; Online: Contribution of the EssC ATPase to the assembly of the type 7b secretion system in Staphylococcus aureus.

    Bobrovskyy, Maksym / Oh, So Young / Missiakas, Dominique

    The Journal of biological chemistry

    2022  Volume 298, Issue 9, Page(s) 102318

    Abstract: Secretion systems utilize ATPase activity to facilitate the translocation of proteins into and across membranes. In bacteria, the universally conserved SecA ATPase binds a large repertoire of preproteins and interacts with the SecYEG translocon. In ... ...

    Abstract Secretion systems utilize ATPase activity to facilitate the translocation of proteins into and across membranes. In bacteria, the universally conserved SecA ATPase binds a large repertoire of preproteins and interacts with the SecYEG translocon. In contrast, the type 7b secretion system (T7bSS) of Staphylococcus aureus supports the secretion of a restricted subset of proteins. T7bSSs are found in several Firmicutes as gene clusters encoding secreted WXG100 proteins and FtsK/SpoIIIE-like ATPase. In S. aureus, this ATPase is called EssC and comprises two cytosolic forkhead-associated domains (FHA
    MeSH term(s) Adenosine Triphosphatases/genetics ; Adenosine Triphosphatases/metabolism ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Protein Transport ; SEC Translocation Channels/genetics ; SEC Translocation Channels/metabolism ; Staphylococcus aureus/genetics ; Staphylococcus aureus/metabolism ; Type VII Secretion Systems/metabolism
    Chemical Substances Bacterial Proteins ; SEC Translocation Channels ; Type VII Secretion Systems ; Adenosine Triphosphatases (EC 3.6.1.-)
    Language English
    Publishing date 2022-07-31
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1016/j.jbc.2022.102318
    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.

  8. Article ; Online: Regulated cleavage of glycan strands by the murein hydrolase SagB in

    Willing, Stephanie / Schneewind, Olaf / Missiakas, Dominique

    Journal of bacteriology

    2021  Volume 203, Issue 9

    Abstract: LyrA (SpdC), a homologue of eukaryotic CAAX proteases that act on prenylated substrates, has been implicated in the assembly of several pathways of the envelope ... ...

    Abstract LyrA (SpdC), a homologue of eukaryotic CAAX proteases that act on prenylated substrates, has been implicated in the assembly of several pathways of the envelope of
    Language English
    Publishing date 2021-02-16
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2968-3
    ISSN 1098-5530 ; 0021-9193
    ISSN (online) 1098-5530
    ISSN 0021-9193
    DOI 10.1128/JB.00014-21
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Ud II Zs.50: 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.

  9. Article ; Online: Corrigendum to: Staphylococcus aureus Decolonization of Mice With Monoclonal Antibody Neutralizing Protein A.

    Chen, Xinhai / Sun, Yan / Missiakas, Dominique / Schneewind, Olaf

    The Journal of infectious diseases

    2021  Volume 225, Issue 2, Page(s) 358

    Language English
    Publishing date 2021-07-29
    Publishing country United States
    Document type Published Erratum
    ZDB-ID 3019-3
    ISSN 1537-6613 ; 0022-1899
    ISSN (online) 1537-6613
    ISSN 0022-1899
    DOI 10.1093/infdis/jiab438
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Uh II Zs.50: 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)
    Zs.MO 445: Show issues

    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.

  10. Article ; Online: A humanized monoclonal antibody targeting protein a promotes opsonophagocytosis of Staphylococcus aureus in human umbilical cord blood.

    Bernardino, Paola Nol / Bhattacharya, Mohini / Chen, Xinhai / Jenkins, Julia / Missiakas, Dominique / Thammavongsa, Vilasack

    Vaccine

    2023  Volume 41, Issue 35, Page(s) 5079–5084

    Abstract: Low and very-low-birth-weight (V/LBW) neonates are highly susceptible to bacterial sepsis and meningitis. Bacterial infections caused by Staphylococcus aureus can be particularly dangerous for neonates and can result in high mortality and long-term ... ...

    Abstract Low and very-low-birth-weight (V/LBW) neonates are highly susceptible to bacterial sepsis and meningitis. Bacterial infections caused by Staphylococcus aureus can be particularly dangerous for neonates and can result in high mortality and long-term disabilities.Antibody-based strategies have been attempted to protect V/LBW neonates against staphylococcal disease. However, these efforts have so far been unsuccessful. Failures were attributed to the immaturity of the neonatal immune system but did not account for the anti-opsonic activity of Staphylococcal protein A (SpA). Here we show that monoclonal antibody 3F6, which blocks SpA activity, promotes complement-dependent cell-mediated phagocytosis of S. aureus in human umbilical cord blood. A substitution in the crystallizable fragment (Fc) region of 3F6 that enhances recruitment of complement component C1q further increases the phagocytic activity of cord blood. Our data demonstrate that the neonatal immune system possesses bactericidal activity that can be harnessed by antibodies that circumvent a key innate immune strategy of S. aureus.
    MeSH term(s) Infant, Newborn ; Humans ; Staphylococcus aureus ; Staphylococcal Protein A/metabolism ; Fetal Blood ; Opsonization ; Antibodies, Bacterial ; Antibodies, Monoclonal, Humanized ; Staphylococcal Infections ; Antibodies, Monoclonal
    Chemical Substances Staphylococcal Protein A ; Antibodies, Bacterial ; Antibodies, Monoclonal, Humanized ; Antibodies, Monoclonal
    Language English
    Publishing date 2023-07-16
    Publishing country Netherlands
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 605674-x
    ISSN 1873-2518 ; 0264-410X
    ISSN (online) 1873-2518
    ISSN 0264-410X
    DOI 10.1016/j.vaccine.2023.07.018
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 1930: 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)
    Zs.MO 458: Show issues

    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