Autor: Chodaczek, Grzegorz - Katalog OPAC zbiorów

Skocz do pozycji: 1.

Tytuł:: Lactoferrin-monophosphoryl lipid a complex enhances immunity of mice to Plesiomonas shigelloides CNCTC 138/92
Autorzy:: Chodaczek, Grzegorz
Zimecki, Michal
Lukasiewicz, Jolanta
Lugowski, Czesław
Powiązania:: https://bibliotekanauki.pl/articles/1040820.pdf
Data publikacji:: 2008
Wydawca:: Polskie Towarzystwo Biochemiczne
Tematy:: lactoferrin
Plesiomonas shigelloides
adjuvant
monophosphoryl lipid A
Opis:: Our previous study showed the efficacy of lactoferrin-monophosphoryl lipid A isolated from Hafnia alvei LPS complex (LF-MPLH.a.) as an adjuvant in stimulation of humoral and cellular immune response in mice to conventional antigens and a lower pyrogenicity of the complex as compared with MPLH.a. alone. In the present investigation we demonstrated that LF-MPLH.a. complex enhanced the immunity of BALB/c mice immunized with Plesiomonas shigelloides CNCTC 138/92 bacterial vaccine, against P. shigelloides infection. The adjuvant effect was evidenced by a significant increase of the antigen-specific serum IgG, IgG2a, and IgG1 and elevation of antigen-specific serum IgA concentrations. In addition, application of the adjuvant facilitated better clearance of the bacteria in spleens and livers of infected mice when compared with MPLH.a. alone. These features of the new adjuvant may predispose it for vaccination protocols in humans.
Źródło:: Acta Biochimica Polonica; 2008, 55, 1; 91-96
0001-527X
Pojawia się w:: Acta Biochimica Polonica
Dostawca treści:: Biblioteka Nauki

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Tytuł:: Design of small molecule inhibitors of type III secretion system ATPase EscN from enteropathogenic Escherichia coli
Autorzy:: Bzdzion, Lukasz
Krezel, Hanna
Wrzeszcz, Karol
Grzegorek, Irmina
Nowinska, Katarzyna
Chodaczek, Grzegorz
Swietnicki, Wieslaw
Powiązania:: https://bibliotekanauki.pl/articles/1038684.pdf
Data publikacji:: 2017
Wydawca:: Polskie Towarzystwo Biochemiczne
Tematy:: Escherichia coli (E. coli)
type III secretion system (T3SS)
enzyme inhibitor
small molecule
Opis:: Enteropathogenic E. coli (EPEC) is a human pathogen using type III secretion system for delivery of proteins directly into the human host. The system contains a single ATPase, EscN, which is essential for uncoupling of proteins from their complexes with chaperones before the delivery. The structure of EscN ATPase (PDB code: 2obm) was used to screen computationally for small molecule inhibitors blocking its active site. Two lead candidates were examined but only one, Compound 54, was selected for further optimization. After extended QSAR optimization, two derivatives were found to be competitive inhibitors of EscN capable of blocking ATPase activity with a Ki below 50 µM. One candidate, WEN05-03, with a Ki=16±2 µM, was also minimally toxic to mammalian cells as determined by other assays. In the cell infection model of HeLa cells with EPEC, Compound WEN05-03 completely blocked actin cluster formation at 100 µM concentration, when analyzed by confocal microscopy. The second best inhibitor of EscN ATPase activity was WEN04-34 with a Ki=46±2 µM. However, the compound was highly toxic to the BALB/3T3 cell line. In summary, the work identifies a compound blocking bacterial ATPase in its active site without causing cellular toxicity to the host cells. It is the first report showing feasibility of using bacterial virulence system ATPase as a target for safe, non-toxic compounds and offering a proof-of-concept for non-antibiotic alternatives.
Źródło:: Acta Biochimica Polonica; 2017, 64, 1; 49-63
0001-527X
Pojawia się w:: Acta Biochimica Polonica
Dostawca treści:: Biblioteka Nauki

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