CTX-M-127 with I176F mutations found in bacteria isolates from Bangladeshi circulating banknotes

Abstract Extended-spectrum beta-lactamase (ESBL)-producing organisms are widely recognized as clinically relevant causes of difficult-to-treat infections. CTX-M has formed a rapidly growing family distributed worldwide among a wide range of clinical bacteria, particularly members of Enterobacteriace...

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Main Authors: Md. Zannat Ali, Sankaranarayanan Srinivasan, Selina Akter
Format: Article
Language:English
Published: Nature Portfolio 2024-03-01
Series:Scientific Reports
Subjects:
Online Access:https://doi.org/10.1038/s41598-024-56207-x
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author Md. Zannat Ali
Sankaranarayanan Srinivasan
Selina Akter
author_facet Md. Zannat Ali
Sankaranarayanan Srinivasan
Selina Akter
author_sort Md. Zannat Ali
collection DOAJ
description Abstract Extended-spectrum beta-lactamase (ESBL)-producing organisms are widely recognized as clinically relevant causes of difficult-to-treat infections. CTX-M has formed a rapidly growing family distributed worldwide among a wide range of clinical bacteria, particularly members of Enterobacteriaceae. Circulating banknotes, exchanged daily among people, pose a potential vehicle for transmitting multidrug resistance. We screened for ESBL-carrying bacteria in the present study and reported CTX-M mutations in Bangladesh's banknotes. We sequenced the genes and performed homology modeling using the Swiss model with CTX-M-15 (4HBT) as a template. Then, we performed molecular docking of mecillinam with the template and the generated model using Autodock 4.2 (Release 4.2.6). After docking, we visually inspected the complexes built using Autodock tools for polar contacts and pi-pi interactions in PyMOL 2.5.4. Our partially sequenced bla CTX-M was related to bla CTX-M-10 and bla CTX-M-15. We observed multiple single-nucleotide substitution mutations, i.e., G613T (silent mutation), A626T (I176F), and A503G (N135D). Homology modeling showed high similarity when the model was superimposed over the template. The orientation of Asn (135) in the template and Asp (135) in the model does not show a significant difference. Likewise, Ile (176) in the template and Phe (176) in the model offer the same orientation. Our generated model could bind to Lys237, Ser240, and Asp135 residues with the lowest binding energy on docking. Our predicted binding of the mecillinam to the mutated D-135 residue in the model indicates contributions and supports previous reports proposing CTX-M-15 to CTX-M-127 mutational conversion on the mecillinum resistance phenotype.
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spelling doaj.art-f3fda785f2544be69dfceee735c589fb2024-03-17T12:23:37ZengNature PortfolioScientific Reports2045-23222024-03-011411710.1038/s41598-024-56207-xCTX-M-127 with I176F mutations found in bacteria isolates from Bangladeshi circulating banknotesMd. Zannat Ali0Sankaranarayanan Srinivasan1Selina Akter2Department of Microbiology, Jashore University of Science and TechnologyDepartment of Biotechnology, Indian Institute of Technology MadrasDepartment of Microbiology, Jashore University of Science and TechnologyAbstract Extended-spectrum beta-lactamase (ESBL)-producing organisms are widely recognized as clinically relevant causes of difficult-to-treat infections. CTX-M has formed a rapidly growing family distributed worldwide among a wide range of clinical bacteria, particularly members of Enterobacteriaceae. Circulating banknotes, exchanged daily among people, pose a potential vehicle for transmitting multidrug resistance. We screened for ESBL-carrying bacteria in the present study and reported CTX-M mutations in Bangladesh's banknotes. We sequenced the genes and performed homology modeling using the Swiss model with CTX-M-15 (4HBT) as a template. Then, we performed molecular docking of mecillinam with the template and the generated model using Autodock 4.2 (Release 4.2.6). After docking, we visually inspected the complexes built using Autodock tools for polar contacts and pi-pi interactions in PyMOL 2.5.4. Our partially sequenced bla CTX-M was related to bla CTX-M-10 and bla CTX-M-15. We observed multiple single-nucleotide substitution mutations, i.e., G613T (silent mutation), A626T (I176F), and A503G (N135D). Homology modeling showed high similarity when the model was superimposed over the template. The orientation of Asn (135) in the template and Asp (135) in the model does not show a significant difference. Likewise, Ile (176) in the template and Phe (176) in the model offer the same orientation. Our generated model could bind to Lys237, Ser240, and Asp135 residues with the lowest binding energy on docking. Our predicted binding of the mecillinam to the mutated D-135 residue in the model indicates contributions and supports previous reports proposing CTX-M-15 to CTX-M-127 mutational conversion on the mecillinum resistance phenotype.https://doi.org/10.1038/s41598-024-56207-xCTX-M-127CTX-M-15BanknotesAntibiotic resistanceExtended-spectrum beta-lactamaseMutation
spellingShingle Md. Zannat Ali
Sankaranarayanan Srinivasan
Selina Akter
CTX-M-127 with I176F mutations found in bacteria isolates from Bangladeshi circulating banknotes
Scientific Reports
CTX-M-127
CTX-M-15
Banknotes
Antibiotic resistance
Extended-spectrum beta-lactamase
Mutation
title CTX-M-127 with I176F mutations found in bacteria isolates from Bangladeshi circulating banknotes
title_full CTX-M-127 with I176F mutations found in bacteria isolates from Bangladeshi circulating banknotes
title_fullStr CTX-M-127 with I176F mutations found in bacteria isolates from Bangladeshi circulating banknotes
title_full_unstemmed CTX-M-127 with I176F mutations found in bacteria isolates from Bangladeshi circulating banknotes
title_short CTX-M-127 with I176F mutations found in bacteria isolates from Bangladeshi circulating banknotes
title_sort ctx m 127 with i176f mutations found in bacteria isolates from bangladeshi circulating banknotes
topic CTX-M-127
CTX-M-15
Banknotes
Antibiotic resistance
Extended-spectrum beta-lactamase
Mutation
url https://doi.org/10.1038/s41598-024-56207-x
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