Characterizing the co-existence of metallo-β-lactamase and extended spectrum beta-lactamase genes in Escherichia coli and Klebsiella pneumoniae isolates in community wastewater samples of Dhaka, Bangladesh
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BRAC University
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Abstract
Gram-negative bacteria with Metallo Beta-Lactamase (MBL) and Extended-Spectrum
Beta-Lactamase (ESBL) production are a new concern worldwide. And these are the most
concerning topics as they are being antibiotic-resistant day by day which is becoming a
world-alarming situation in medical therapies. Here the sample was collected from the
community wastewater and the main concern was to find gram-negative bacteria Escherichia
coli which are producing MBL and ESBL, MBL is a type of carbapenemase enzyme that
displays the ability to inactivate all classes of β-lactam antibiotics, including the last-resort
carbapenems, except for monobactams. ESBL enzymes, also most commonly found in
Enterobacteriaceae, can inactivate cephalosporins and monobactams such as aztreonam.
In this project, the water sample was collected to isolate E.coli by using selective media with the
addition of supplements after proper dilution. And antibiotic sensitivity tests were run throughout
the project to identify the Multidrug Resistant (MDR) and then proceed with the PCR with
multiple coexisting genes blaNDM-1, blaIMP,blaSHV, blaTEM, and blaCTX-M.
As a result, 110 isolates of E.coli were found after implying a proper way of spreading and
streaking. 76 isolates were found to be resistant towards amoxicillin and 7 isolates were found to
be resistant towards both gentamicin and meropenem where 30% of isolates of community
wastewater exhibited multi-drug resistant properties. 48 isolates were confirmed for blaNDM-1,
blaIMP,blaSHV, blaTEM, and blaCTX-M and 7 isolates of E.coli displayed co-existence genes.
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This thesis is submitted in partial fulfillment of the requirements for the degree of Bachelor of Science in Microbiology, 2022.
Catalogued from PDF version of thesis.
Includes bibliographical references (pages 26-30).
Catalogued from PDF version of thesis.
Includes bibliographical references (pages 26-30).
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Thesis