Predicted transmembrane proteins with homology to Mef(A) are not responsible for complementing mef(A) deletion in the mef(A)–msr(D) macrolide efflux system in Streptococcus pneumoniae
Abstract Objectives In streptococci, the type M resistance to macrolides is due to the mef(A)–msr(D) efflux transport system of the ATP-Binding cassette (ABC) superfamily, where it is proposed that mef(A) codes for the transmembrane channel and msr(D) for the two ATP-binding domains. Phage ϕ1207.3 o...
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oai:doaj.org-article:0204ba6d66fb4f25a21adf1da90dc25e2021-11-28T12:25:18ZPredicted transmembrane proteins with homology to Mef(A) are not responsible for complementing mef(A) deletion in the mef(A)–msr(D) macrolide efflux system in Streptococcus pneumoniae10.1186/s13104-021-05856-61756-0500https://doaj.org/article/0204ba6d66fb4f25a21adf1da90dc25e2021-11-01T00:00:00Zhttps://doi.org/10.1186/s13104-021-05856-6https://doaj.org/toc/1756-0500Abstract Objectives In streptococci, the type M resistance to macrolides is due to the mef(A)–msr(D) efflux transport system of the ATP-Binding cassette (ABC) superfamily, where it is proposed that mef(A) codes for the transmembrane channel and msr(D) for the two ATP-binding domains. Phage ϕ1207.3 of Streptococcus pyogenes, carrying the mef(A)–msr(D) gene pair, is able to transfer the macrolide efflux phenotype to Streptococcus pneumoniae. Deletion of mef(A) in pneumococcal ϕ1207.3-carrying strains did not affect erythromycin efflux. In order to identify candidate genes likely involved in complementation of mef(A) deletion, the Mef(A) amino acid sequence was used as probe for database searching. Results In silico analysis identified 3 putative candidates in the S. pneumoniae R6 genome, namely spr0971, spr1023 and spr1932. Isogenic deletion mutants of each candidate gene were constructed and used in erythromycin sensitivity assays to investigate their contribution to mef(A) complementation. Since no change in erythromycin sensitivity was observed compared to the parental strain, we produced double and triple mutants to assess the potential synergic activity of the selected genes. Also these mutants did not complement the mef(A) function.Valeria FoxFrancesco SantoroGianni PozziFrancesco IannelliBMCarticleMef(A)Msr(D)Macrolide effluxStreptococcus pyogenesStreptococcus pneumoniaeABC-transporterMedicineRBiology (General)QH301-705.5Science (General)Q1-390ENBMC Research Notes, Vol 14, Iss 1, Pp 1-7 (2021) |
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Mef(A) Msr(D) Macrolide efflux Streptococcus pyogenes Streptococcus pneumoniae ABC-transporter Medicine R Biology (General) QH301-705.5 Science (General) Q1-390 |
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Mef(A) Msr(D) Macrolide efflux Streptococcus pyogenes Streptococcus pneumoniae ABC-transporter Medicine R Biology (General) QH301-705.5 Science (General) Q1-390 Valeria Fox Francesco Santoro Gianni Pozzi Francesco Iannelli Predicted transmembrane proteins with homology to Mef(A) are not responsible for complementing mef(A) deletion in the mef(A)–msr(D) macrolide efflux system in Streptococcus pneumoniae |
description |
Abstract Objectives In streptococci, the type M resistance to macrolides is due to the mef(A)–msr(D) efflux transport system of the ATP-Binding cassette (ABC) superfamily, where it is proposed that mef(A) codes for the transmembrane channel and msr(D) for the two ATP-binding domains. Phage ϕ1207.3 of Streptococcus pyogenes, carrying the mef(A)–msr(D) gene pair, is able to transfer the macrolide efflux phenotype to Streptococcus pneumoniae. Deletion of mef(A) in pneumococcal ϕ1207.3-carrying strains did not affect erythromycin efflux. In order to identify candidate genes likely involved in complementation of mef(A) deletion, the Mef(A) amino acid sequence was used as probe for database searching. Results In silico analysis identified 3 putative candidates in the S. pneumoniae R6 genome, namely spr0971, spr1023 and spr1932. Isogenic deletion mutants of each candidate gene were constructed and used in erythromycin sensitivity assays to investigate their contribution to mef(A) complementation. Since no change in erythromycin sensitivity was observed compared to the parental strain, we produced double and triple mutants to assess the potential synergic activity of the selected genes. Also these mutants did not complement the mef(A) function. |
format |
article |
author |
Valeria Fox Francesco Santoro Gianni Pozzi Francesco Iannelli |
author_facet |
Valeria Fox Francesco Santoro Gianni Pozzi Francesco Iannelli |
author_sort |
Valeria Fox |
title |
Predicted transmembrane proteins with homology to Mef(A) are not responsible for complementing mef(A) deletion in the mef(A)–msr(D) macrolide efflux system in Streptococcus pneumoniae |
title_short |
Predicted transmembrane proteins with homology to Mef(A) are not responsible for complementing mef(A) deletion in the mef(A)–msr(D) macrolide efflux system in Streptococcus pneumoniae |
title_full |
Predicted transmembrane proteins with homology to Mef(A) are not responsible for complementing mef(A) deletion in the mef(A)–msr(D) macrolide efflux system in Streptococcus pneumoniae |
title_fullStr |
Predicted transmembrane proteins with homology to Mef(A) are not responsible for complementing mef(A) deletion in the mef(A)–msr(D) macrolide efflux system in Streptococcus pneumoniae |
title_full_unstemmed |
Predicted transmembrane proteins with homology to Mef(A) are not responsible for complementing mef(A) deletion in the mef(A)–msr(D) macrolide efflux system in Streptococcus pneumoniae |
title_sort |
predicted transmembrane proteins with homology to mef(a) are not responsible for complementing mef(a) deletion in the mef(a)–msr(d) macrolide efflux system in streptococcus pneumoniae |
publisher |
BMC |
publishDate |
2021 |
url |
https://doaj.org/article/0204ba6d66fb4f25a21adf1da90dc25e |
work_keys_str_mv |
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