iMedPub Journals www.imedpub.com 2017 Vol. 1 No. 4:15 Research Article 1 © Under License of Creative Commons Attribution 3.0 License | This artcle is available in: htp://www.imedpub.com/applied-microbiology-and-biochemistry Journal of Applied Microbiology and Biochemistry ISSN 2576-1412 DOI: 10.21767/2576-1412.100015 Ejikeugwu Chika 1 *, Iroha Ifeanyichukwu 1 , Amaechi Clement O 1 , Ugwu Malachy 2 , Eze Peter 2 , Iroha Chidinma S 3 , Ogene Lilian 1 and Orinya Chinedu 1 1 Department of Applied Microbiology, Ebonyi State University, Ebonyi State, Nigeria 2 Department of Pharmaceutcal Microbiology and Biotechnology, Faculty of Pharmaceutcal Sciences, Nnamdi Azikiwe University, Anambra State, Nigeria 3 Department of Pharmacy, Federal Teaching Hospital Abakaliki (FETHA I), Ebonyi State, Nigeria *Corresponding author: Ejikeugwu Chika  ejikeugwu_chika@yahoo.com Department of Applied Microbiology, Faculty of Science, Ebonyi State University, Abakaliki, P.M.B 053, Ebonyi State, Nigeria. Tel: +2348097684562 Citation: Chika E, Ifeanyichukwu I, Clement OA, Malachy U, Peter E, et al. (2017) Multple Antbiotc Resistance, Antbiogram and Phenotypic Detecton of Metallo-Beta- Lactamase (MBL) from Escherichia coli of Poultry Origin. J Appl Microbiol Biochem. Vol. 1 No. 4:15 Introducton In Nigeria, the detecton rate of multdrug resistant Gram- negatve bacteria in both the community and hospital environment is stll at a pitable state. More worrisome is the fact that the detecton of multdrug resistant bacteria such Multple Antbiotc Resistance, Antbiogram and Phenotypic Detecton of Metallo-Beta- Lactamase (MBL) from Escherichia coli of Poultry Origin Abstract Background: Bacteria produce antbiotc-degrading enzymes such as carbapenemases. Carbapenemases are a consortum of carbapenem-hydrolyzing enzymes such as metallo-β-lactamase (MBL) that gives Gram-negatve bacteria the exceptonal ability to degrade and render the carbapenems inefcacious. Aim: This study evaluated the antbiogram, multple antbiotc resistance and occurrence of MBL-producing E. coli from cloacal swabs of poultry birds in a local poultry farm in Abakaliki, Nigeria. Materials and methods: A total of 40 cloacal swab samples from the cloacal region of poultry birds were bacteriologically analyzed for the isolaton of E. coli. E. coli isolates were identfed using standard microbiology techniques and the antbiogram of the isolates was determined using the disk difusion technique. The multdrug resistance nature of the E. coli isolates was determined using multple antbiotcs resistance index (MARI) protocol while MBL producton was phenotypically confrmed using the inhibiton based assay. Results: A total of 29 (72.5%) E. coli isolates was recovered from the 40 cloacal swab samples. The E. coli isolates were highly resistant to imipenem (31%), meropenem (58.6%), ertapenem (75.9%), cefotaxime (55.2%), ciprofoxacin (89.7%), cefoxitn (93.1%). and cefazidime (69.0%). MBL producton was phenotypically detected in 3 (10.3%) E. coli isolates out of the 29 isolates of E. coli recovered in this study. The resistant E. coli isolates were multply resistant to antbiotcs in the class of fuoroquinolones, cephalosporins, aminoglycosides and carbapenems; and they had a multple antbiotc resistance of 0.4 on average. Conclusion: This presumptve study has shown that E. coli isolates of poultry origin produce MBL. The emergence and spread of drug resistant bacteria in the community can be contained if we use antbiotcs ratonally and fnd alternatve measures for promotng animal growth without the use of antmicrobial agents. Keywords: Metallo-β-lactamase; Escherichia coli; Multdrug resistance; Pathogens Received: August 08, 2017; Accepted: August 21, 2017; Published: August 28, 2017 as metallo-β-lactamase (MBL)-producing bacteria has not yet been insttutonalized in our healthcare system. And this could contribute to poor prognosis of the patent as well as lead to inappropriate use or applicaton of antmicrobial therapy. The emergence of new beta-lactamases such as metallo-β-lactamases (MBLs), extended spectrum β-lactamases (ESBLs) and AmpC