Di Girolamo, Salvatore

Profilbild
E-Mail-Adresse
Geburtsdatum
Projekt
Organisationseinheiten
Berufsbeschreibung
Nachname
Di Girolamo
Vorname
Salvatore
Name
Di Girolamo, Salvatore

Filter

2019 - 20202

Einstellungen

Suchergebnisse

Gerade angezeigt 1 - 2 von 2
  • Kein Vorschaubild vorhanden
    Publikation
    Stable and selective permeable hydrogel microcapsules for high-throughput cell cultivation and enzymatic analysis
    (Springer, 27.08.2020) Di Girolamo, Salvatore; Puorger, Chasper; Lipps, Georg
    01A - Beitrag in wissenschaftlicher Zeitschrift
  • Kein Vorschaubild vorhanden
    Publikation
    Characterization of the housekeeping sortase from the human pathogen Propionibacterium acnes - first investigation of a class F sortase
    (Portland Press, 2019) Di Girolamo, Salvatore; Lipps, Georg
    Sortase enzymes play an important role in Gram-positive bacteria. They are responsible for the covalent attachment of proteins to the surface of the bacteria and perform this task via a highly sequence-specific transpeptidation reaction. Since these immobilized proteins are often involved in pathogenicity of Gram-positive bacteria, characterization of this type of enzyme is also of medical relevance. Different classes of sortases (A-F) have been found, which recognize characteristic recognition sequences present in substrate proteins. Up to date, sortase A from Staphylococcus aureus, a housekeeping class A sortase, is the most thoroughly studied representative of the sortase family of enzymes. Here we report the in-depth characterization of the class F sortase from Propionibacterium acnes, a class of sortases that has not been investigated before. As Sortase F is the only transpeptidase found in the P. acnes genome, it is the housekeeping sortase of this organism. Sortase F from P. acnes shows a behavior similar to sortases from class A in terms of pH dependence, recognition sequence and catalytic activity; furthermore, its activity is independent of bivalent ions, which contrasts to sortase A from S. aureus We demonstrate that sortase F is useful for protein engineering applications, by producing a site-specifically conjugated homogenous antibody-drug conjugate with a potency similar to that of a conjugate prepared with sortase A. Thus, the detailed characterization presented here will not only enable the development of anti-virulence agents targeting P. acnes but also provides a powerful alternative to sortase A for protein engineering applications. © 2019 The Author(s). Published by Portland Press Limited on behalf of the Biochemical Society.
    01A - Beitrag in wissenschaftlicher Zeitschrift