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Natural mannose-binding lectin [MBL] down-regulates phagocytosis of Helicobacter pylori

100%

Strapagiel D., Grebowska A., Rozalska B., Bak-Romaniszyn L., Czkwianianc E., Planeta-Malecka I., Rechcinski T., Rudnicka W., Chmiela M.

Polish Journal of Microbiology

2006

tom 55

nr 2

Considering the role of lectin-carbohydrate interactions between Helicobacter pylori bacteria and the host cells we addressed the question on how mannose binding lectin - MBL, present in human plasma, may influence the phagocytosis of H. pylori by peripheral blood granulocytes. For phagocytosis assay the granulocytes separated from peripheral blood of healthy H. pylori-seronegative donors were used. Phagocytosis was estimated by fluorescence assay using FITC-labelled H. pylori cells. The MBL level in the serum samples as well as MBL-binding to H. pylori bacteria were estimated by ELISA. In this study all H. pylori isolates bound recombinant mannose binding lectin-MBL as shown by ELISA. The ingestion of H. pylori bacteria in the medium with human serum depleted in natural MBL (nMBL) was more intensive than in the medium with complete serum containing nMBL. Moreover, the ingestion of H. pylori bacteria in the medium with complete serum was increased by an addition of anti-rMBL IgG. The results indicate that interaction of bacterial and host lectins may regulate the phagocytosis of H. pylori bacteria and in this way influence an outcome of the infection caused by these microbes.

Mannose-binding lectin enhances the attachment and phagocytosis of mycobacteria in vitro

84%

Bonar A., Chmiela M., Rudnicka W., Rozalska B.

Archivum Immunologiae et Therapiae Experimentalis

2005

tom 53

nr 5

A novel tetrameric lectin from Lycoris aurea with four mannose binding sites per monomer

67%

Liu J., Xu X., Liu J., Balzarini J., Luo Y., Kong Y., Li J., Chen F., Van Damme E., Bao J.

Acta Biochimica Polonica

2007

tom 54

nr 1

The mannose-binding agglutinin from bulbs of Lycoris aurea (LAA) agglutinates rabbit but not human erythrocytes. The molecular mass of the monomer in SDS/PAGE is 12 kDa while the apparent molecular mass in gel filtration is 48 kDa, indicating that LAA is a homotetramer. The full-length cDNA of LAA contains 683 bp with an open reading frame encoding a protomer of 162 amino-acid residues. Hydrophobic Cluster Analysis and molecular modeling of the 109-residue mature polypeptide suggested a similar secondary and tertiary structure to those of Narcissus pseudonarcissus agglutinin (NPA). Molecular docking revealed that, besides the three mannose-binding sites common among Amaryllidaceae lectins, LAA also contains a fourth unique mannose-binding site formed by a tryptophan cluster. The existence of four mannose-binding sites in each monomer of LAA is very unusual and has only been reported for NPA earlier.

Ograniczanie wyników

1 Acta Biochimica Polonica

1 Archivum Immunologiae et Therapiae Experimentalis

1 Polish Journal of Microbiology

2 Chmiela M.

2 Rozalska B.

2 Rudnicka W.

1 Bak-Romaniszyn L.

1 Balzarini J.

1 Bao J.

1 Bonar A.

1 Chen F.

1 Czkwianianc E.

1 Grebowska A.

1 Kong Y.

1 Li J.

1 Liu J.

1 Luo Y.

1 Planeta-Malecka I.

1 Rechcinski T.

1 Strapagiel D.

1 Van Damme E.

1 Xu X.

1 2007

1 2006

1 2005

Wyniki wyszukiwania

Natural mannose-binding lectin [MBL] down-regulates phagocytosis of Helicobacter pylori

Mannose-binding lectin enhances the attachment and phagocytosis of mycobacteria in vitro

A novel tetrameric lectin from Lycoris aurea with four mannose binding sites per monomer