http://rdf.ncbi.nlm.nih.gov/pubchem/patent/US-2014065127-A1
Outgoing Links
| Predicate | Object |
|---|---|
| assignee | http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_9930dd6926edc181a4e058e989843453 http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_892388e8e6c74a8a6cadecd6859ee58b http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_b6bbee82108ad927eddffb12f4e186bc |
| classificationCPCInventive | http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12N9-2462 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12N9-2402 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12Y302-01017 |
| classificationIPCInventive | http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N9-24 |
| filingDate | 2012-09-06-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| inventor | http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_9e2ccf779bc216be816186a83d8d3415 http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_27ed42f3df7d5955f1f99740e90debbf http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_a162a2c379324372b42d0fcbc2623b0d |
| publicationDate | 2014-03-06-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| publicationNumber | US-2014065127-A1 |
| titleOfInvention | Staphylococcus haemolyticus Prophage PhiSH2 Endolysin is Lytic for Staphylococcus aureus |
| abstract | Methicillin-resistant (MRSA) and multi-drug resistant strains of Staphylococcus aureus are becoming increasingly prevalent in both human and veterinary clinics. S. aureus -causing bovine mastitis yields high annual losses to the dairy industry. Treatment of mastitis by broad range antibiotics is often not successful and may contribute to development of antibiotic resistance. Bacteriophage endolysins are a promising new source of antimicrobials. The endolysin of prophage φSH2 of Staphylococcus haemolyticus strain JCSC1435 (φSH2 lysin) shows lytic activity against live staphylococcal cells. Deletion constructs were tested in zymograms and turbidity reduction assays to evaluate the contribution of each functional module to lysis. The CHAP domain exhibited three-fold higher activity than the full length protein. Activity was further enhanced in the presence of bivalent calcium ions. The full length enzyme and the CHAP domain showed activity against multiple staphylococcal strains, including MRSA strains, mastitis isolates, and coagulase negative staphylococcal (CoNS) strains. |
| isCitedBy | http://rdf.ncbi.nlm.nih.gov/pubchem/patent/CN-116640754-A |
| priorityDate | 2012-09-06-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| type | http://data.epo.org/linked-data/def/patent/Publication |
Incoming Links
Total number of triples: 212.