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1

Lactoferrin-monophosphoryl lipid A complex enhances immunity of mice to Plesiomonas shigelloides CNCTC 138-92

100%
Chodaczek G., Zimecki M., Lukasiewicz J., Lugowski C.
Acta Biochimica Polonica
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2008
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tom 55
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nr 1
Our previous study showed the efficacy of lactoferrin-monophosphoryl lipid A isolated from Hafnia alvei LPS complex (LF-MPL H.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 MPL H.a. alone. In the present investigation we demonstrated that LF-MPL H.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 MPL H.a. alone. These features of the new adjuvant may predispose it for vaccination protocols in humans.
2

The charakterization of a human lactoferrin [HLF] cell line - HLF K1

100%
Kocieba M., Zimecki M., Chodaczek G.
Cellular and Molecular Biology Letters
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2002
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tom 07
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nr Suppl.
3

Characterization of the human lactoferrin [HLF] cell line HLFK1, generated in CBA mice

100%
Kocieba M., Zimecki M., Chodaczek G.
Cellular and Molecular Biology Letters
|
2003
|
tom 08
|
nr 1
A human lactoferrin-specific cell line was generated in CBA mice, sensitized with 200 μg HLF in Freund’s complete adjuvant. HLFK1 cells derived from the lymph nodes of these mice were maintained using HLF as the antigen. HLF was added at the beginning of each 14-day restimulation cycle, at a concentration of 100 μg/ml. The presentation of the antigen to HLFK1 was demonstrated using glass-adherent lymphocytes from spleens (GAL) as the antigen-presenting cells (APC). The presentation of HLF by GAL was highly efficient; a very low concentration of the antigen (1 μg/ml) was enough to stimulate proliferation of the HLFK1 cell line. HLFK1 did not proliferate in the presence of ovalbumin or bovine lactoferrin (BLF), which is structurally related to HLF. However, we found that BLF caused a reduction in the proliferation of the HLFK1 cell line when BLF was added to the cultures together with the antigen - (HLF). On the other hand, proliferation of the HLFK1 cell line was not inhibited by pretreatment of the antigen-presenting cells or T cells with BLF. Therefore, we suggest that bovine lactoferrin may interfere with the binding or uptake of the antigen (HLF). Alternatively, BLF may nonspecifically inhibit the activation of the HLFK1 cell line.
4

Glycomacropeptide protects against experimental endotoxemia and bacteremia in mice

76%
Zimecki M., Artym J., Chodaczek G., Kocieba M., Rybka J., Skorska A., Kruzel M.
Electronic Journal of Polish Agricultural Universities. Series Veterinary Medicine
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2006
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tom 09
|
nr 2
The aim of this study was to evaluate protective effects of glycomacropeptide (GMP), a kappa casein-derived peptide, in experimentally induced endotoxemia or bacteremia in mice. The results showed that BALB/c mice, given intraperitoneally (i.p.) GMP, 24h before intravenous (i.v.) injection of a high dose of lipopolysaccharide (LPS) from Escherichia coli, strongly inhibited serum levels of tumor necrosis factor alpha (TNF alpha) and interleukin 6 (IL-6), measured 2h later by bioassays. In addition, GMP, administered 24h before infection of CBA mice with a sublethal dose of E. coli, significantly lowered the number of bacterial cells in the spleen. The analysis of main blood cell types in mice pretreated 24h prior to infection with GMP revealed significant increase in the content of granulocytes and immature neutrophils. We, therefore, postulate, that induction of myelopoiesis by GMP may be a primary cause of the increased clearance of bacteria during the development of bacteremia in mice.
5

Design of small molecule inhibitors of type III secretion system ATPase EscN from enteropathogenic Escherichia coli

76%
Bzdzion L., Krezel H., Wrzeszcz K., Grzegorek I., Nowinska K., Chodaczek G., Swietnicki W.
Acta Biochimica Polonica
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2017
|
tom 64
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nr 1
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