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Extended-spectrum beta-lactamase
Beta-lactamase is produced by certain bacteria that break down antibiotics species spread spectrum. For example, beta-lactamase broad spectrum, can be obtained by the specific strain of bacteria living in the intestines, usually E. coli or E. coli, and (E.coli). Treatment of infections caused by ESBL-producing bacteria is difficult. It is possible that not only occurs around the urinary tract, affecting wound, blood and lungs of these infections. The people who were admitted to the hospital, the risk of infection is high. Treatment of some disease, surgery, and medicine, you can weaken the body's ability to fight off infection. However, it is stable, there are other antibiotics that can be used to treat infections physician. Infection can be prevented by using a good hygiene among visitors staff and patients.
History of ESBL
Is described in the mid-1980s first, intensive care mainly in the 1990s, in the treatment of the most vulnerable patients, often, especially in the hospital, ESBLs were found in species of the genus Klebsiella. Public Health England (PHE), and monitors changes in the production cell count these enzymes. Until recently, the number of patients affected showed little signs of growing small problems would remain. However, they have been detected in Escherichia coli (E. coli) bacteria between widely (called CTX-M enzymes) new class of ESBL If you have emerged. Is to resistance to cephalosporin and penicillin, ESBL-producing E. coli of these, it is most common on urinary tract infection - cystitis is not simple. Be concerned, it has been discovered, such as the following, in the hospital and community, but, hospitals.PHE has a research program active for studying the biological ESBLs and enzymes, and genetics of their infection may have had contact with previously and are "community, the acquired" patient which produce them.
Cause and Treatment
Members of the Enterobacteriaceae, often, is expressed (eg, SHV-1 and TEM-1, TEM-2) is a plasmid encoding β-lactamase. Which provides resistance to penicillin, but it does not extend the spectrum cephalosporin. In the mid-1980s, a new group of enzymes broad-spectrum β-lactamase and (ESBLs) have been discovered. (First, found in Germany in 1983). Hydrolyzing the extended spectrum cephalosporin and the side chain imino ESBLs are β-lactamase. Cephalosporin such, oximino and ceftazidime, cefotaxime, and ceftriaxone - including those tapir Tam aztreonam. Therefore relates to oxyimino-β-lactam and ESBLs, the antibiotic resistance. In typical conditions, they are derived from SHV-1 gene or TEM-1, TEM-2, by changing the amino acid mutations structure of the active site around these β-lactamase of. This will expand the spectrum susceptible to hydrolysis by this enzyme of β-lactam antibiotics. An increase in the number of ESBLs not of SHV or TEM descent systems have been recently described. ESBLs, plasmid, are encoded often. In many cases, drugs (eg, aminoglycosides) plasmid producing ESBL carries a gene encoding resistance to other classes. Therefore, the choice of antibiotics is extremely limited for the treatment of ESBL-producing organisms. Carbapenem is the perfect tool for serious infections caused by ESBL-producing organisms, carbapenem-resistant strains, has been reported recently. The ESBL-producing organisms, may be susceptible to cephalosporins extended spectrum some. However, antibiotic treatment such is associated with a high failure rate.
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