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    Wyświetlanie 1-4 z 4
    Tytuł:
    Evaluation of P1 substrate specificity of staphylococcal SplB protease
    Autorzy:
    Pustelny, Katarzyna
    Stach, Natalia
    Wladyka, Benedykt
    Dubin, Adam
    Dubin, Grzegorz
    Powiązania:
    https://bibliotekanauki.pl/articles/1039355.pdf
    Data publikacji:
    2014
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    serine protease
    serine protease-like
    SplB
    Staphylococcus aureus
    substrate specificity
    Opis:
    Staphylococcus aureus is a dangerous human pathogen characterized by growing antibiotic resistance. Virulence of S. aureus relies on a variety of secreted and cell surface associated virulence factors among which certain proteolytic enzymes play an important role. Amid staphylococcal extracellular proteases, those encoded by the spl operon remain poorly characterized, both in terms of enzymology and their physiological role. Initial data demonstrated that Spl proteases exhibit restricted substrate specificity. This study describes development of convenient protein FRET substrates for SplB protease and characterization of the substrate preference of the protease at the P1' position. Kinetic data on hydrolysis of a panel of substrates substituted at the said position is provided.
    Źródło:
    Acta Biochimica Polonica; 2014, 61, 1; 149-152
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    A systematic investigation of the stability of green fluorescent protein fusion proteins
    Autorzy:
    Janczak, Monika
    Bukowski, Michał
    Górecki, Andrzej
    Dubin, Grzegorz
    Dubin, Adam
    Wladyka, Benedykt
    Powiązania:
    https://bibliotekanauki.pl/articles/1038973.pdf
    Data publikacji:
    2015
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    crystallography
    fusion protein
    recombinant protein
    toxin-antitoxin system
    Opis:
    X-ray crystallography provides important insights into structure-function relationship in biomolecules. However, protein crystals are usually hard to obtain which hinders our understanding of multiple important processes. Crystallization requires large amount of protein sample, whereas recombinant proteins are often unstable or insoluble. Green fluorescent protein (GFP) fusion is one of the approaches to increase protein synthesis, solubility and stability, facilitating crystallization. In this study we analyze the influence of the linker length, composition and the position of GFP relative to the fusion partner on the fusion protein production and stability. To this end, multiple constructs of enzymatically impaired variant of PemKSa toxin from Staphylococcus aureus CH91 fused to GFP were generated. Fusion protein production in Escherichia coli was evaluated. The proteins were purified and their stability tested. PemKSa-α14aa-GFP fusion provided best production and stability. Obtained results demonstrate the importance of optimization of fusion protein construct, including linker selection and the order of fusion partners, in obtaining high quantities of stable protein for crystallization.
    Źródło:
    Acta Biochimica Polonica; 2015, 62, 3; 407-411
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Defense against own arms: staphylococcal cysteine proteases and their inhibitors.
    Autorzy:
    Dubin, Grzegorz
    Powiązania:
    https://bibliotekanauki.pl/articles/1043443.pdf
    Data publikacji:
    2003
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    staphostatin
    staphylococcus
    ssp
    proteinase
    protease inhibitor
    staphopain
    Opis:
    Staphylococcus aureus is a human pathogen causing a wide range of diseases. Most staphylococcal infections, unlike those caused by other bacteria are not toxigenic and very little is known about their pathogenesis. It has been proposed that a core of secreted proteins common to many infectious strains is responsible for colonization and infection. Among those proteins several proteases are present and over the years many different functions in the infection process have been attributed to them. However, little direct, in vivo data has been presented. Two cysteine proteases, staphopain A (ScpA) and staphopain B (SspB) are important members of this group of enzymes. Recently, two cysteine protease inhibitors, staphostatin A and staphostatin B (ScpB and SspC, respectively) were described in S. aureus shedding new light on the complexity of the processes involving the two proteases. The scope of this review is to summarize current knowledge on the network of staphylococcal cysteine proteases and their inhibitors in view of their possible role as virulence factors.
    Źródło:
    Acta Biochimica Polonica; 2003, 50, 3; 715-724
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    New generation of peptide antibiotics
    Autorzy:
    Dubin, Adam
    Mak, Paweł
    Dubin, Grzegorz
    Rzychon, Małgorzata
    Stec-Niemczyk, Justyna
    Wladyka, Benedykt
    Maziarka, Katarzyna
    Chmiel, Dorota
    Powiązania:
    https://bibliotekanauki.pl/articles/1041366.pdf
    Data publikacji:
    2005
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    staphostatin
    Staphylococcus
    virulence factor
    hemoglobin
    protease inhibitor
    hemocidins
    antimicrobial agents
    antibiotics
    Opis:
    The increasing antibiotic resistance of pathogenic bacteria calls for the development of alternative antimicrobial strategies. Possible approaches include the development of novel, broad-spectrum antibiotics as well as specific targeting of individual bacterial virulence factors. It is impossible to decide currently which strategy will prove more successful in the future since they both promise different advantages, but also introduce diverse problems. Considering both approaches, our laboratory's research focuses on the evaluation of hemocidins, broad-spectrum antibacterial peptides derived from hemoglobin and myoglobin, and staphostatins, specific inhibitors of staphopains - Staphylococcus aureus secreted proteases that are virulence factors regarded as possible targets for therapy. The article summarizes recent advances in both fields of study and presents perspectives for further development and possible applications.
    Źródło:
    Acta Biochimica Polonica; 2005, 52, 3; 633-638
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
      Wyświetlanie 1-4 z 4

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