| Predicate |
Object |
| assignee |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_1faac18f8237eeb75b8f335cefa6139f
http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_1c8cbbf2290b3f3a9988da29598baa2c |
| classificationCPCAdditional |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/A61K38-00
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/G01N2333-4725
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/G01N2333-245
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/G01N2333-21
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/G01N2333-195
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/Y02A50-30 |
| classificationCPCInventive |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/A61K38-1735
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/G01N33-56911
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/G01N33-56916
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/A61K31-546
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C07K14-4727
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/A61P31-04 |
| classificationIPCInventive |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12P21-02
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C07K14-435
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/A61K39-00
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/A61K38-17
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/A61K38-16 |
| filingDate |
2015-12-23-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| inventor |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_6a81fa91951e53f2a621dd78bddfcad3
http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_7f7d35825f221733613f5f2867338aea
http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_fd8a5320ece8ff4bcbda41e84dbefa74 |
| publicationDate |
2017-11-01-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| publicationNumber |
EP-3236995-A2 |
| titleOfInvention |
Muc1 decoy peptides for treatment and prevention of bacterial infections |
| abstract |
Pseudomonas aeruginosa flagellin protein recruits the mammalian host sialidase enzyme neuraminidase- 1 (NEU1) to remove sialic acid residues from the extracellular domain of the mammalian cell-surface protein MUC l (MUC l -ED), thereby exposing a cryptic binding site on the MUC l -ED protein backbone for flagellin binding. NEU1 -driven MUC l -ED desialylation rapidly increases P. aeruginosa adhesion to the airway epithelium. MUCl -ED desialylation also increases MUC l -ED cleavage and shedding from the cell surface, where desialylated, shed MUCl -ED competitively blocks P. aeruginosa adhesion to cell-associated MUCl -ED. Presented herein are data showing that exogenously-administered, deglycosylated MUCl -ED peptides reduced adhesion of P. aeruginosa to airway epithelial cells. Also presented are data showing that administration of P. aeruginosa to mice in combination with deglycosylated MUC 1 -ED decreased P. aeruginosa recovered from the lungs at 48 hr and 72 hr post-infection. Such findings are extended to the methods of treatment and prevention of bacterial infections defined herein. |
| priorityDate |
2014-12-23-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| type |
http://data.epo.org/linked-data/def/patent/Publication |