Inhibition of selectin binding

Nagy, Jon O; Spevak, Wayne R; Dasgupta, Falguni; Bertozzi, Carolyn

Title: Inhibition of selectin binding

Patent · Fri Jan 01 00:00:00 EST 1999

OSTI ID:872565

Nagy, Jon O ^[1]; Spevak, Wayne R ^[2]; Dasgupta, Falguni ^[3]; Bertozzi, Carolyn ^[2]

Rodeo, CA
Albany, CA
New Delhi, IN

This invention provides a system for inhibiting the binding between two cells, one expressing P- or L-selectin on the surface and the other expressing the corresponding ligand. A covalently crosslinked lipid composition is prepared having saccharides and acidic group on separate lipids. The composition is then interposed between the cells so as to inhibit binding. Inhibition can be achieved at an effective oligosaccharide concentration as low as 10.sup.6 fold below that of the free saccharide. Since selectins are involved in recruiting cells to sites of injury, this system can be used to palliate certain inflammatory and immunological conditions.

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Research Organization:: Lawrence Berkeley National Laboratory (LBNL), Berkeley, CA (United States)

DOE Contract Number:: AC03-76SF00098

Assignee:: Regents of University of California (Oakland, CA)

Patent Number(s):: US 5962422

Application Number:: 08/807428

OSTI ID:: 872565

Country of Publication:: United States

Language:: English

References (34)

A plasmid facilitating in vitro construction of phoA gene fusions in Escherichia coli Gutierrez, Claude; Devedjian, Jean Christophe Nucleic Acids Research, Vol. 17, Issue 10 https://doi.org/10.1093/nar/17.10.3999	journal	January 1989
Characterization of a Calcium Porter of Streptococcus Pneumoniae Involved In Calcium Regulation of Growth and Competence Trombe, M. -C. Journal of General Microbiology, Vol. 139, Issue 3 https://doi.org/10.1099/00221287-139-3-433	journal	March 1993
The mgtB Mg2+ transport locus of Salmonella typhimurium encodes a P-type ATPase. Snavely, M. D.; Miller, C. G.; Maguire, M. E. Journal of Biological Chemistry, Vol. 266, Issue 2 https://doi.org/10.1016/S0021-9258(17)35246-8	journal	January 1991
Genetic immunization is a simple method for eliciting an immune response Tang, De-chu; DeVit, Michael; Johnston, Stephen A. Nature, Vol. 356, Issue 6365 https://doi.org/10.1038/356152a0	journal	March 1992
Secretion of cyclolysin, the calmodulin-sensitive adenylate cyclase-haemolysin bifunctional protein of Bordetella pertussis. Glaser, P.; Sakamoto, H.; Bellalou, J. The EMBO Journal, Vol. 7, Issue 12 https://doi.org/10.1002/j.1460-2075.1988.tb03288.x	journal	December 1988
Evidence for high affinity binding-protein dependent transport systems in gram-positive bacteria and in Mycoplasma. Gilson, E.; Alloing, G.; Schmidt, T. The EMBO Journal, Vol. 7, Issue 12 https://doi.org/10.1002/j.1460-2075.1988.tb03284.x	journal	December 1988
Construction and properties of a new insertion vector, pJDC9, that is protected by transcriptional terminators and useful for cloning of DNA from Streptococcus pneumoniae Chen, Jau-Der; Morrison, Donald A. Gene, Vol. 64, Issue 1 https://doi.org/10.1016/0378-1119(88)90489-1	journal	April 1988
A sandwich adhesin on Streptococcus pneumoniae attaching to human oropharyngeal epithelial cells in vitro Andersson, B.; Beachey, E. H.; Tomasz, A. Microbial Pathogenesis, Vol. 4, Issue 4 https://doi.org/10.1016/0882-4010(88)90087-3	journal	April 1988
Truncated forms of PspA that are secreted from Streptococcus pneumoniae and their use in functional studies and cloning of the pspA gene. Yother, J.; Handsome, G. L.; Briles, D. E. Journal of Bacteriology, Vol. 174, Issue 2 https://doi.org/10.1128/JB.174.2.610-618.1992	journal	January 1992
Pilin expression in Neisseria gonorrhoeae is under both positive and negative transcriptional control. Taha, M. K.; So, M.; Seifert, H. S. The EMBO Journal, Vol. 7, Issue 13 https://doi.org/10.1002/j.1460-2075.1988.tb03335.x	journal	December 1988
The ami locus of the Gram-positive bacterium Streptococcus pneumoniae is similar to binding protein-dependent transport operons of Gram-negative bacteria Alloing, G.; Trombe, M. C.; Claverys, J. P. Molecular Microbiology, Vol. 4, Issue 4 https://doi.org/10.1111/j.1365-2958.1990.tb00632.x	journal	April 1990
Adherence, coaggregation, and hydrophobicity of Streptococcus gordonii associated with expression of cell surface lipoproteins. Jenkinson, H. F. Infection and Immunity, Vol. 60, Issue 3 https://doi.org/10.1128/IAI.60.3.1225-1228.1992	journal	January 1992
Bacterial Adherence: Adhesin-Receptor Interactions Mediating the Attachment of Bacteria to Mucosal Surfaces Beachey, E. H. Journal of Infectious Diseases, Vol. 143, Issue 3 https://doi.org/10.1093/infdis/143.3.325	journal	March 1981
Genetic identification of exported proteins in Streptococcus pneumoniae Pearce, B. J.; Yin, Y. B.; Masure, H. R. Molecular Microbiology, Vol. 9, Issue 5 https://doi.org/10.1111/j.1365-2958.1993.tb01233.x	journal	September 1993
D-E-A-D protein family of putative RNA helicases Schmid, S. R.; Linder, P. Molecular Microbiology, Vol. 6, Issue 3 https://doi.org/10.1111/j.1365-2958.1992.tb01470.x	journal	February 1992
Role of pilA, an essential regulatory gene of Neisseria gonorrhoeae, in the stress response. Taha, M. K.; Larribe, M.; Dupuy, B. Journal of Bacteriology, Vol. 174, Issue 18 https://doi.org/10.1128/JB.174.18.5978-5981.1992	journal	January 1992
TnphoA: a transposon probe for protein export signals. Manoil, C.; Beckwith, J. Proceedings of the National Academy of Sciences, Vol. 82, Issue 23 https://doi.org/10.1073/pnas.82.23.8129	journal	December 1985
Consequences of microbial attachment: directing host cell functions with adhesins. Hoepelman, A. I.; Tuomanen, E. I. Infection and Immunity, Vol. 60, Issue 5 https://doi.org/10.1128/IAI.60.5.1729-1733.1992	journal	January 1992
Peptide permeases modulate transformation in Streptococcus pneumoniae Pearce, B. J.; Naughton, A. M.; Masure, H. R. Molecular Microbiology, Vol. 12, Issue 6 https://doi.org/10.1111/j.1365-2958.1994.tb01076.x	journal	June 1994
Cloning of the amiA locus of Streptococcus pneumoniae and identification of its functional limits Alloing, Geneviéve; Trombe, Marie-Claude; Claverys, Jean-Pierre Gene, Vol. 76, Issue 2 https://doi.org/10.1016/0378-1119(89)90177-7	journal	March 1989
Analysis of pneumococcal PspA microheterogeneity in SDS polyacrylamide gels and the association of PspA with the cell membrane Talkington, Deborah F.; Voellinger, David C.; Mcdaniel, Larry S. Microbial Pathogenesis, Vol. 13, Issue 5 https://doi.org/10.1016/0882-4010(92)90078-3	journal	November 1992
The Clp proteins: proteolysis regulators or molecular chaperones? Squires, C.; Squires, C. L. Journal of Bacteriology, Vol. 174, Issue 4 https://doi.org/10.1128/JB.174.4.1081-1085.1992	journal	January 1992
Title Page Blood Purification, Vol. 11, Issue 3, p. 175-175 https://doi.org/10.1159/000170117	journal	January 1993
Construction and use of signal sequence selection vectors in Escherichia coli and Bacillus subtilis. Smith, H.; Bron, S.; Van Ee, J. Journal of Bacteriology, Vol. 169, Issue 7 https://doi.org/10.1128/JB.169.7.3321-3328.1987	journal	January 1987
Cloning and characterization of a region of the Enterococcus faecalis conjugative plasmid, pCF10, encoding a sex pheromone-binding function. Ruhfel, R. E.; Manias, D. A.; Dunny, G. M. Journal of Bacteriology, Vol. 175, Issue 16 https://doi.org/10.1128/JB.175.16.5253-5259.1993	journal	January 1993
The cell wall mediates pneumococcal attachment to and cytopathology in human endothelial cells. Geelen, S.; Bhattacharyya, C.; Tuomanen, E. Infection and Immunity, Vol. 61, Issue 4 https://doi.org/10.1128/IAI.61.4.1538-1543.1993	journal	January 1993
The glucose permease of the phosphotransferase system of Bacillus subtilis: evidence for II ^Glc and III ^Glc domains Gonzy-Tréboul, G.; Waard, J. H.; Zagorec, M. Molecular Microbiology, Vol. 5, Issue 5 https://doi.org/10.1111/j.1365-2958.1991.tb01898.x	journal	May 1991
Marker Discrimination in Transformation and Mutation of Pneumococcus Tiraby, J. - G.; Fox, M. S. Proceedings of the National Academy of Sciences, Vol. 70, Issue 12 https://doi.org/10.1073/pnas.70.12.3541	journal	December 1973
Nucleotide sequences of genes encoding penicillin-binding proteins from Streptococcus pneumoniae and Streptococcus oralis with high homology to Escherichia coli penicillin-binding proteins 1a and 1b. Martin, C.; Briese, T.; Hakenbeck, R. Journal of Bacteriology, Vol. 174, Issue 13 https://doi.org/10.1128/JB.174.13.4517-4523.1992	journal	January 1992
The calmodulin-sensitive adenylate cyclase of Bordetella pertussis : cloning and expression in Escherichia col Glaser, P.; Ladant, D.; Sezer, O. Molecular Microbiology, Vol. 2, Issue 1 https://doi.org/10.1111/j.1365-2958.1988.tb00003.x	journal	January 1988
Characterization of signal-sequence-coding regions selected from the Bacillus subtilis chromosome Smith, Hilde; de Jong, Anne; Bron, Sierd Gene, Vol. 70, Issue 2 https://doi.org/10.1016/0378-1119(88)90207-7	journal	October 1988
Gene inoculation generates immune responses against human immunodeficiency virus type 1. Wang, B.; Ugen, K. E.; Srikantan, V. Proceedings of the National Academy of Sciences, Vol. 90, Issue 9 https://doi.org/10.1073/pnas.90.9.4156	journal	May 1993
Protein export elements from Lactococcus lactis Perez-Martinez, Gaspar; Kok, Jan; Venema, Gerard Molecular and General Genetics MGG, Vol. 234, Issue 3 https://doi.org/10.1007/BF00538699	journal	September 1992
Relatedness of penicillin-binding protein 1a genes from different clones of penicillin-resistant Streptococcus pneumoniae isolated in South Africa and Spain. Martin, C.; Sibold, C.; Hakenbeck, R. The EMBO Journal, Vol. 11, Issue 11 https://doi.org/10.1002/j.1460-2075.1992.tb05475.x	journal	November 1992

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Related Subjects

inhibition
selectin
binding
provides
inhibiting
cells
expressing
p-
l-selectin
surface
corresponding
ligand
covalently
crosslinked
lipid
composition
prepared
saccharides
acidic
separate
lipids
interposed
inhibit
achieved
effective
oligosaccharide
concentration
10
fold
below
free
saccharide
selectins
involved
recruiting
sites
injury
palliate
inflammatory
immunological
conditions
recruiting cells
selectin binding
separate lipids
oligosaccharide concentration
expressing p-
fold below
free saccharide
lipid composition
effective oligosaccharide
covalently crosslinked
crosslinked lipid
corresponding ligand
immunological conditions
inhibit binding
/514/435/

Title: Inhibition of selectin binding

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References (34)

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