Search

Your search keyword '"Lindner, Buko"' showing total 760 results
Start Over Author "Lindner, Buko"
760 results on '"Lindner, Buko"'

12. Relationship of the Lipopolysaccharide Structure of Yersinia bpestis to Resistance to Antimicrobial Factors

Author

Knirel, Yuriy A., Kocharova, Nina A., Titareva, Galina M., Bakhteeva, Irina V., Senchenkova, Sof'ya N., Bystrova, Olga V., Dentovskaya, Svetlana V., Anisimov, Andrey P., Pier, Gerald B., Lindner, Buko, Shaikhutdinova, Rima Z., Back, Nathan, Series Editor, Cohen, Irun R., Series Editor, Kritchevsky, David, Series Editor, Lajtha, Abel, Series Editor, Paoletti, Rodolfo, Series Editor, Perry, Robert D., editor, and Fetherston, Jacqueline D., editor

Published
2007
Full Text
View/download PDF

18. The Core Structure of the Lipopolysaccharide of Yersinia pestis Strain KM218 : Influence of Growth Temperature

Author

Gremyakova, Tat’yana A., Vinogradov, Evgeny V., Lindner, Buko, Kocharova, Nina A., Senchenkova, Sof’ya N., Shashkov, Aleksander S., Knirel, Yuriy A., Holst, Otto, Shaikhutdinova, Rima Z., Anisimov, Andrei P., Back, Nathan, editor, Cohen, Irun R., editor, Kritchevsky, David, editor, Lajtha, Abel, editor, Paoletti, Rodolfo, editor, Skurnik, Mikael, editor, Bengoechea, José Antonio, editor, and Granfors, Kaisa, editor

Published
2003
Full Text
View/download PDF

25. Structural reorganization of the antigen-binding groove of human CD1b for presentation of mycobacterial sulfoglycolipids

Author

Garcia-Alles, Luis F., Collmann, Anthony, Versluis, Cees, Lindner, Buko, Guiard, Julie, Maveyraud, Laurent, Huc, Emilie, Im, Jin S., Sansano, Sebastiano, Brando, Thérèse, Julien, Sylviane, Prandi, Jacques, Gilleron, Martine, Porcelli, Steven A., de la Salle, Henri, Heck, Albert J. R., Mori, Lucia, Puzo, Germain, Mourey, Lionel, and De Libero, Gennaro

Published
2011

44. Biolabeling with 2,4-dichlorophenoxyacetic acid derivatives: the 2,4-D tag

Author

Bade, Steffen, Rockendorf, Niels, Franek, Milan, Gorris, Hans H., Lindner, Buko, Olivier, Verena, Schaper, Klaus-Jurgen, and Frey, Andreas

Subjects
Acetic acid -- Chemical properties, Antibodies -- Chemical properties, Viral antibodies -- Chemical properties, Biochemistry -- Research, Chemistry
Abstract

Many bioanalytic and diagnostic procedures rely on labels with which the molecule of interest can be tracked in or discriminated from accompanying like substances. Herein, we describe a new labeling and detection system based on derivatives of 2,4-dichlorophenoxyacetic acid (2,4-D) and anti-2,4-D antibodies. The 2,4-D system is highly sensitive with a [K.sub.D] of 7 x [l0.sup.-11] M for the hapten--antibody pair, can be used on a large variety of biomolecules such as proteins, peptides, carbohydrates, and nucleic acids, is not hampered by endogenous backgrounds because 2,4-D is a xenobiotic, and is robust because 2,4-D is a very stable compound that withstands the conditions of most reactions usually performed on biomolecules. With this unique blend of properties, the 2,4-D system compares favorably with its rivals digoxigenin (DIG)/anti-DIG and biotin/(strept)avidin and provides an interesting and powerful tool in biomolecular labeling. 10.1021/ac901900n

Published
2009

45. Molecular analysis of three Aeromonas hydrophila AH-3 (serotype O34) lipopolysaccharide core biosynthesis gene clusters

Author

Jimenez, Natalia, Canals, Rocio, Lacasta, Anna, Kondakova, Anna N., Lindner, Buko, Knirel, Yuriy A., Merino, Susana, Regue, Miguel, and Tomas, Juan M.

Subjects
Aeromonas -- Genetic aspects, Aeromonas -- Physiological aspects, Biological sciences
Abstract

By the isolation of three different Aeromonas hydrophila strain AH-3 (serotype O34) mutants with an altered lipopolysaccharide (LPS) migration in gels, three genomic regions encompassing LPS core biosynthesis genes were identified and characterized. When possible, mutants were constructed using each gene from the three regions, containing seven, four, and two genes (regions 1 to 3, respectively). The mutant LPS core structures were elucidated by using mass spectrometry, methylation analysis, and comparison with the full core structure of an O-antigen-lacking AH-3 mutant previously established by us. Combining the gene sequence and complementation test data with the structural data and phenotypic characterization of the mutant LPSs enabled a presumptive assignment of all LPS core biosynthesis gene functions in A. hydrophila AH-3. The three regions and the genes contained are in complete agreement with the recently sequenced genome of A. hydrophila ATCC 7966. The functions of the A. hydrophila genes waaC in region 3 and waaF in region 2 were completely established, allowing the genome annotations of the two heptosyl transferase products not previously assigned. Having the functions of all genes involved with the LPS core biosynthesis and most corresponding single-gene mutants now allows experimental work on the role of the LPS core in the virulence of A. hydrophila.

Published
2008

48. MS/MS approach for characterization of the fatty acid distribution on mycobacterial phosphatidyl-myo-inositol mannosides

Author

Gilleron, Martine, Lindner, Buko, and Puzo, Germain

Subjects
Ligands (Biochemistry) -- Research, Molecular microbiology -- Research, Lymphocytes -- Research, Chemistry
Abstract

Phosphatidyl-myo-inositol mannosides (PIM) are not only important structural components of the mycobacterial envelope but also are major non-peptidic antigens of the host innate and acquired immune responses. Indeed, they are ligands of TLR-2 and they activate CD1-restricted T lymphocytes. In addition, PIM constitute the basic structure of the lipidic anchor of two lipoglycans, lipomannans and lipoarabinomannans, which are important immuno-modulators in the course of tuberculosis. The fatty acyl substituents present on PIM molecules play a crucial role for both their physical properties and biological activities. PIM contain four acylation sites, two on the glycerol, one on a mannose, and one on the myo-inositol units. We propose here an analytical procedure, based on mass spectrometry, to determine the structure of the fatty acids present on each of these different acylafion sites. We show that the nature of the fatty acids located on both positions of glycerol can be deduced from IRMPD analysis of negative precursor ions from native PIM species, while the fatty acids located on myo-inositol and mannose units can be identified by MALDI-TOF CID MS of protonated and cationized molecular ions. Thus, the combination of MS/MS data obtained from positive and negative pseudo-molecular ions generated by ESI or MALDI appears as a powerful approach for the structural characterization of the PIM acyl form structure.

Published
2006

49. Cholesterol glucosylation promotes immune evasion by Helicobacter pylori

Author

Wunder, Christian, Churin, Yuri, Winau, Florian, Warnecke, Dirk, Vieth, Michael, Lindner, Buko, Zahringer, Ulrich, Mollenkopf, Hans-Joachim, Heinz, Ernst, and Meyer, Thomas F

Abstract

Helicobacter pylori infection causes gastric pathology such as ulcer and carcinoma. Because H. pylori is auxotrophic for cholesterol, we have explored the assimilation of cholesterol by H. pylori in infection. Here we show that H. pylori follows a cholesterol gradient and extracts the lipid from plasma membranes of epithelial cells for subsequent glucosylation. Excessive cholesterol promotes phagocytosis of H. pylori by antigen-presenting cells, such as macrophages and dendritic cells, and enhances antigen-specific T cell responses. A cholesterol-rich diet during bacterial challenge leads to T cell-dependent reduction of the H. pylori burden in the stomach. Intrinsic [alpha]-glucosylation of cholesterol abrogates phagocytosis of H. pylori and subsequent T cell activation. We identify the gene hp0421 as encoding the enzyme cholesterol-[alpha]-glucosyltransferase responsible for cholesterol glucosylation. Generation of knockout mutants lacking hp0421 corroborates the importance of cholesteryl glucosides for escaping phagocytosis, T cell activation and bacterial clearance in vivo. Thus, we propose a mechanism regulating the host-pathogen interaction whereby glucosylation of a lipid tips the scales towards immune evasion or response., Author(s): Christian Wunder (corresponding author) [1, 7, 8]; Yuri Churin [1, 8]; Florian Winau [2, 8]; Dirk Warnecke [3]; Michael Vieth [4, 7]; Buko Lindner [5]; Ulrich Zahringer [5]; Hans-Joachim [...]

Published
2006
Full Text
View/download PDF

50. OpsX from Haemophilus influenzae represents a novel type of heptosyltransferase I in lipopolysaccharide biosynthesis

Author

Gronow, Sabine, Brabetz, Werner, Lindner, Buko, and Brade, Helmut

Subjects
Polysaccharides -- Genetic aspects, Influenza -- Research, Biological sciences
Abstract

The inner core region of the lipopolysaccharide (LPS) of Haemophilus influenzae is characterized by the presence of a phosphorylated 3-deoxy-[alpha]-D-manno-octulosonic acid (Kdo). In this study, we show that the heptosyltransferase I adding the first L-glycero-D-manno-heptose residue to this acceptor is encoded by the gene opsX, which differs in substrate specificity from the other heptosyltransferase I, known as WaaC.

Published
2005

Catalog

Books, media, physical & digital resources
See catalog results