BacSJ—Another Bacteriocin with Distinct Spectrum of Activity that Targets Man-PTS
Lactic acid bacteria produce diverse antimicrobial peptides called bacteriocins. Most bacteriocins target sensitive bacteria by binding to specific receptors. Although a plethora of bacteriocins have been identified, for only a few of them the receptors they recognize are known. Here, we identified...
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| Format: | Article |
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MDPI AG
2020-10-01
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| Series: | International Journal of Molecular Sciences |
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| Online Access: | https://www.mdpi.com/1422-0067/21/21/7860 |
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| author | Aleksandra Tymoszewska Piotr Walczak Tamara Aleksandrzak-Piekarczyk |
| author_facet | Aleksandra Tymoszewska Piotr Walczak Tamara Aleksandrzak-Piekarczyk |
| author_sort | Aleksandra Tymoszewska |
| collection | DOAJ |
| description | Lactic acid bacteria produce diverse antimicrobial peptides called bacteriocins. Most bacteriocins target sensitive bacteria by binding to specific receptors. Although a plethora of bacteriocins have been identified, for only a few of them the receptors they recognize are known. Here, we identified permease IIC and surface protein IID, two membrane subunits of the mannose-specific quaternary phosphotransferase system (Man-PTS), as a receptor for BacSJ, a subclass IId bacteriocin produced by <i>Lactobacillus paracasei</i> subsp. <i>paracasei</i> BGSJ2-8. BacSJ shares 45% identity with another Man-PTS binding bacteriocin, garvicin Q (GarQ). Similarly to GarQ, BacSJ has a relatively broad activity spectrum acting against several Gram-positive bacteria, such as <i>Lactococcus lactis</i> and <i>Listeria monocytogenes,</i> harboring fairly similar Man-PTSs, but not against <i>Lactococcus garvieae</i>. To identify specific Man-PTS amino acids responsible for the <i>L.</i><i>lactis</i> sensitivity to BacSJ, and thus likely involved in the interaction with this bacteriocin, we generated eight independent BacSJ resistant <i>L.</i><i>lactis</i> mutants harboring five distinct missense mutations in the <i>ptnC</i> or <i>ptnD</i> genes encoding the IIC and IID subunits. Concurrently with the resistance to BacSJ, the mutants efficiently utilized mannose as a carbon source, which indicated functionality of their mutated Man-PTS. The amino acid substitutions in the mutants localized to the intracellular region of the IIC permease or to the extracellular parts of IID. This localization coincides with regions targeted by GarQ and some other Man-PTS-binding garvicins, pointing to similarities between all these bacteriocins in the mechanism of their interaction with Man-PTS. During the attack by these bacteriocins, subunits IID and IIC are assumed to function sequentially as a docking and an entry module allowing the toxic peptide to bind the cell and then open the pore. However, since not all of the BacSJ-resistant mutants exhibited cross-resistance to GarQ, we propose that BacSJ interacts with Man-PTS in a manner slightly different from that of GarQ. |
| first_indexed | 2024-03-10T15:23:43Z |
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| id | doaj.art-7942eb2e3f934ab3834badd9fa7fec98 |
| institution | Directory Open Access Journal |
| issn | 1661-6596 1422-0067 |
| language | English |
| last_indexed | 2024-03-10T15:23:43Z |
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| spelling | doaj.art-7942eb2e3f934ab3834badd9fa7fec982023-11-20T18:15:17ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672020-10-012121786010.3390/ijms21217860BacSJ—Another Bacteriocin with Distinct Spectrum of Activity that Targets Man-PTSAleksandra Tymoszewska0Piotr Walczak1Tamara Aleksandrzak-Piekarczyk2Institute of Biochemistry and Biophysics, Polish Academy of Sciences (IBB PAS), Pawińskiego 5a, 02-106 Warsaw, PolandInstitute of Biochemistry and Biophysics, Polish Academy of Sciences (IBB PAS), Pawińskiego 5a, 02-106 Warsaw, PolandInstitute of Biochemistry and Biophysics, Polish Academy of Sciences (IBB PAS), Pawińskiego 5a, 02-106 Warsaw, PolandLactic acid bacteria produce diverse antimicrobial peptides called bacteriocins. Most bacteriocins target sensitive bacteria by binding to specific receptors. Although a plethora of bacteriocins have been identified, for only a few of them the receptors they recognize are known. Here, we identified permease IIC and surface protein IID, two membrane subunits of the mannose-specific quaternary phosphotransferase system (Man-PTS), as a receptor for BacSJ, a subclass IId bacteriocin produced by <i>Lactobacillus paracasei</i> subsp. <i>paracasei</i> BGSJ2-8. BacSJ shares 45% identity with another Man-PTS binding bacteriocin, garvicin Q (GarQ). Similarly to GarQ, BacSJ has a relatively broad activity spectrum acting against several Gram-positive bacteria, such as <i>Lactococcus lactis</i> and <i>Listeria monocytogenes,</i> harboring fairly similar Man-PTSs, but not against <i>Lactococcus garvieae</i>. To identify specific Man-PTS amino acids responsible for the <i>L.</i><i>lactis</i> sensitivity to BacSJ, and thus likely involved in the interaction with this bacteriocin, we generated eight independent BacSJ resistant <i>L.</i><i>lactis</i> mutants harboring five distinct missense mutations in the <i>ptnC</i> or <i>ptnD</i> genes encoding the IIC and IID subunits. Concurrently with the resistance to BacSJ, the mutants efficiently utilized mannose as a carbon source, which indicated functionality of their mutated Man-PTS. The amino acid substitutions in the mutants localized to the intracellular region of the IIC permease or to the extracellular parts of IID. This localization coincides with regions targeted by GarQ and some other Man-PTS-binding garvicins, pointing to similarities between all these bacteriocins in the mechanism of their interaction with Man-PTS. During the attack by these bacteriocins, subunits IID and IIC are assumed to function sequentially as a docking and an entry module allowing the toxic peptide to bind the cell and then open the pore. However, since not all of the BacSJ-resistant mutants exhibited cross-resistance to GarQ, we propose that BacSJ interacts with Man-PTS in a manner slightly different from that of GarQ.https://www.mdpi.com/1422-0067/21/21/7860BacSJsubclass IId bacteriocinbacteriocin receptormannose-specific PTS (Man-PTS)<i>Lactococcus lactis</i> |
| spellingShingle | Aleksandra Tymoszewska Piotr Walczak Tamara Aleksandrzak-Piekarczyk BacSJ—Another Bacteriocin with Distinct Spectrum of Activity that Targets Man-PTS International Journal of Molecular Sciences BacSJ subclass IId bacteriocin bacteriocin receptor mannose-specific PTS (Man-PTS) <i>Lactococcus lactis</i> |
| title | BacSJ—Another Bacteriocin with Distinct Spectrum of Activity that Targets Man-PTS |
| title_full | BacSJ—Another Bacteriocin with Distinct Spectrum of Activity that Targets Man-PTS |
| title_fullStr | BacSJ—Another Bacteriocin with Distinct Spectrum of Activity that Targets Man-PTS |
| title_full_unstemmed | BacSJ—Another Bacteriocin with Distinct Spectrum of Activity that Targets Man-PTS |
| title_short | BacSJ—Another Bacteriocin with Distinct Spectrum of Activity that Targets Man-PTS |
| title_sort | bacsj another bacteriocin with distinct spectrum of activity that targets man pts |
| topic | BacSJ subclass IId bacteriocin bacteriocin receptor mannose-specific PTS (Man-PTS) <i>Lactococcus lactis</i> |
| url | https://www.mdpi.com/1422-0067/21/21/7860 |
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