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Role of the LytSR Two-Component Regulatory System in Adaptation to Cationic Antimicrobial Peptides in Staphylococcus aureus
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| Zeitschriftentitel: | Antimicrobial Agents and Chemotherapy |
|---|---|
| Personen und Körperschaften: | , , , , , |
| In: | Antimicrobial Agents and Chemotherapy, 57, 2013, 8, S. 3875-3882 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
American Society for Microbiology
|
| Schlagwörter: |
| author_facet |
Yang, Soo-Jin Xiong, Yan Q. Yeaman, Michael R. Bayles, Kenneth W. Abdelhady, Wessam Bayer, Arnold S. Yang, Soo-Jin Xiong, Yan Q. Yeaman, Michael R. Bayles, Kenneth W. Abdelhady, Wessam Bayer, Arnold S. |
|---|---|
| author |
Yang, Soo-Jin Xiong, Yan Q. Yeaman, Michael R. Bayles, Kenneth W. Abdelhady, Wessam Bayer, Arnold S. |
| spellingShingle |
Yang, Soo-Jin Xiong, Yan Q. Yeaman, Michael R. Bayles, Kenneth W. Abdelhady, Wessam Bayer, Arnold S. Antimicrobial Agents and Chemotherapy Role of the LytSR Two-Component Regulatory System in Adaptation to Cationic Antimicrobial Peptides in Staphylococcus aureus Infectious Diseases Pharmacology (medical) Pharmacology |
| author_sort |
yang, soo-jin |
| spelling |
Yang, Soo-Jin Xiong, Yan Q. Yeaman, Michael R. Bayles, Kenneth W. Abdelhady, Wessam Bayer, Arnold S. 0066-4804 1098-6596 American Society for Microbiology Infectious Diseases Pharmacology (medical) Pharmacology http://dx.doi.org/10.1128/aac.00412-13 <jats:title>ABSTRACT</jats:title> <jats:p> Many host defense cationic antimicrobial peptides (HDPs) perturb the staphylococcal cell membrane (CM) and alter transmembrane potential (ΔΨ) as key parts of their lethal mechanism. Thus, a sense-response system for detecting and mediating adaptive responses to such stresses could impact organism survival; the <jats:named-content xmlns:xlink="http://www.w3.org/1999/xlink" content-type="genus-species" xlink:type="simple">Staphylococcus aureus</jats:named-content> LytSR two-component regulatory system (TCRS) may serve as such a ΔΨ sensor. One well-known target of this system is the <jats:italic>lrgAB</jats:italic> operon, which, along with the related <jats:italic>cidABC</jats:italic> operon, has been shown to be a regulator in the control of programmed cell death and lysis. We used an isogenic set of <jats:named-content xmlns:xlink="http://www.w3.org/1999/xlink" content-type="genus-species" xlink:type="simple">S. aureus</jats:named-content> strains: (i) UAMS-1, (ii) its isogenic Δ <jats:italic>lytS</jats:italic> and Δ <jats:italic>lrgAB</jats:italic> mutants, and (iii) plasmid-complemented Δ <jats:italic>lytSR</jats:italic> and Δ <jats:italic>lrgAB</jats:italic> mutants. The Δ <jats:italic>lytS</jats:italic> strain displayed significantly increased <jats:italic>in vitro</jats:italic> susceptibilities to all HDPs tested (neutrophil-derived human neutrophil peptide 1 [hNP-1], platelet-derived thrombin-induced platelet microbicidal proteins [tPMPs], and the tPMP-mimetic peptide RP-1), as well as to calcium-daptomycin (DAP), a cationic antimicrobial peptide (CAP). In contrast, the Δ <jats:italic>lrgAB</jats:italic> strain exhibited no significant changes in susceptibilities to these cationic peptides, indicating that although <jats:italic>lytSR</jats:italic> positively regulates transcription of <jats:italic>lrgAB</jats:italic> , increased HDP/CAP susceptibilities in the Δ <jats:italic>lytS</jats:italic> mutant were <jats:italic>lrgAB</jats:italic> independent. Further, parental UAMS-1 (but not the Δ <jats:italic>lytS</jats:italic> mutant) became more resistant to hNP-1 and DAP following pretreatment with carbonyl cyanide <jats:italic>m</jats:italic> -chlorophenylhydrazone (CCCP) (a CM-depolarizing agent). Of note, <jats:italic>lytSR</jats:italic> -dependent survival against CAP/HDP killing was not associated with changes in either surface positive charge, expression of <jats:italic>mprF</jats:italic> and <jats:italic>dlt</jats:italic> , or CM fluidity. The Δ <jats:italic>lytS</jats:italic> strain (but not the Δ <jats:italic>lrgAB</jats:italic> mutant) displayed a significant reduction in target tissue survival in an endocarditis model during DAP treatment. Collectively, these results suggest that the <jats:italic>lytSR</jats:italic> TCRS plays an important role in adaptive responses of <jats:named-content xmlns:xlink="http://www.w3.org/1999/xlink" content-type="genus-species" xlink:type="simple">S. aureus</jats:named-content> to CM-perturbing HDPs/CAPs, likely by functioning as a sense-response system for detecting subtle changes in ΔΨ. </jats:p> Role of the LytSR Two-Component Regulatory System in Adaptation to Cationic Antimicrobial Peptides in Staphylococcus aureus Antimicrobial Agents and Chemotherapy |
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Antimicrobial Agents and Chemotherapy |
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| title |
Role of the LytSR Two-Component Regulatory System in Adaptation to Cationic Antimicrobial Peptides in Staphylococcus aureus |
| title_unstemmed |
Role of the LytSR Two-Component Regulatory System in Adaptation to Cationic Antimicrobial Peptides in Staphylococcus aureus |
| title_full |
Role of the LytSR Two-Component Regulatory System in Adaptation to Cationic Antimicrobial Peptides in Staphylococcus aureus |
| title_fullStr |
Role of the LytSR Two-Component Regulatory System in Adaptation to Cationic Antimicrobial Peptides in Staphylococcus aureus |
| title_full_unstemmed |
Role of the LytSR Two-Component Regulatory System in Adaptation to Cationic Antimicrobial Peptides in Staphylococcus aureus |
| title_short |
Role of the LytSR Two-Component Regulatory System in Adaptation to Cationic Antimicrobial Peptides in Staphylococcus aureus |
| title_sort |
role of the lytsr two-component regulatory system in adaptation to cationic antimicrobial peptides in staphylococcus aureus |
| topic |
Infectious Diseases Pharmacology (medical) Pharmacology |
| url |
http://dx.doi.org/10.1128/aac.00412-13 |
| publishDate |
2013 |
| physical |
3875-3882 |
| description |
<jats:title>ABSTRACT</jats:title>
<jats:p>
Many host defense cationic antimicrobial peptides (HDPs) perturb the staphylococcal cell membrane (CM) and alter transmembrane potential (ΔΨ) as key parts of their lethal mechanism. Thus, a sense-response system for detecting and mediating adaptive responses to such stresses could impact organism survival; the
<jats:named-content xmlns:xlink="http://www.w3.org/1999/xlink" content-type="genus-species" xlink:type="simple">Staphylococcus aureus</jats:named-content>
LytSR two-component regulatory system (TCRS) may serve as such a ΔΨ sensor. One well-known target of this system is the
<jats:italic>lrgAB</jats:italic>
operon, which, along with the related
<jats:italic>cidABC</jats:italic>
operon, has been shown to be a regulator in the control of programmed cell death and lysis. We used an isogenic set of
<jats:named-content xmlns:xlink="http://www.w3.org/1999/xlink" content-type="genus-species" xlink:type="simple">S. aureus</jats:named-content>
strains: (i) UAMS-1, (ii) its isogenic Δ
<jats:italic>lytS</jats:italic>
and Δ
<jats:italic>lrgAB</jats:italic>
mutants, and (iii) plasmid-complemented Δ
<jats:italic>lytSR</jats:italic>
and Δ
<jats:italic>lrgAB</jats:italic>
mutants. The Δ
<jats:italic>lytS</jats:italic>
strain displayed significantly increased
<jats:italic>in vitro</jats:italic>
susceptibilities to all HDPs tested (neutrophil-derived human neutrophil peptide 1 [hNP-1], platelet-derived thrombin-induced platelet microbicidal proteins [tPMPs], and the tPMP-mimetic peptide RP-1), as well as to calcium-daptomycin (DAP), a cationic antimicrobial peptide (CAP). In contrast, the Δ
<jats:italic>lrgAB</jats:italic>
strain exhibited no significant changes in susceptibilities to these cationic peptides, indicating that although
<jats:italic>lytSR</jats:italic>
positively regulates transcription of
<jats:italic>lrgAB</jats:italic>
, increased HDP/CAP susceptibilities in the Δ
<jats:italic>lytS</jats:italic>
mutant were
<jats:italic>lrgAB</jats:italic>
independent. Further, parental UAMS-1 (but not the Δ
<jats:italic>lytS</jats:italic>
mutant) became more resistant to hNP-1 and DAP following pretreatment with carbonyl cyanide
<jats:italic>m</jats:italic>
-chlorophenylhydrazone (CCCP) (a CM-depolarizing agent). Of note,
<jats:italic>lytSR</jats:italic>
-dependent survival against CAP/HDP killing was not associated with changes in either surface positive charge, expression of
<jats:italic>mprF</jats:italic>
and
<jats:italic>dlt</jats:italic>
, or CM fluidity. The Δ
<jats:italic>lytS</jats:italic>
strain (but not the Δ
<jats:italic>lrgAB</jats:italic>
mutant) displayed a significant reduction in target tissue survival in an endocarditis model during DAP treatment. Collectively, these results suggest that the
<jats:italic>lytSR</jats:italic>
TCRS plays an important role in adaptive responses of
<jats:named-content xmlns:xlink="http://www.w3.org/1999/xlink" content-type="genus-species" xlink:type="simple">S. aureus</jats:named-content>
to CM-perturbing HDPs/CAPs, likely by functioning as a sense-response system for detecting subtle changes in ΔΨ.
</jats:p> |
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| description | <jats:title>ABSTRACT</jats:title> <jats:p> Many host defense cationic antimicrobial peptides (HDPs) perturb the staphylococcal cell membrane (CM) and alter transmembrane potential (ΔΨ) as key parts of their lethal mechanism. Thus, a sense-response system for detecting and mediating adaptive responses to such stresses could impact organism survival; the <jats:named-content xmlns:xlink="http://www.w3.org/1999/xlink" content-type="genus-species" xlink:type="simple">Staphylococcus aureus</jats:named-content> LytSR two-component regulatory system (TCRS) may serve as such a ΔΨ sensor. One well-known target of this system is the <jats:italic>lrgAB</jats:italic> operon, which, along with the related <jats:italic>cidABC</jats:italic> operon, has been shown to be a regulator in the control of programmed cell death and lysis. We used an isogenic set of <jats:named-content xmlns:xlink="http://www.w3.org/1999/xlink" content-type="genus-species" xlink:type="simple">S. aureus</jats:named-content> strains: (i) UAMS-1, (ii) its isogenic Δ <jats:italic>lytS</jats:italic> and Δ <jats:italic>lrgAB</jats:italic> mutants, and (iii) plasmid-complemented Δ <jats:italic>lytSR</jats:italic> and Δ <jats:italic>lrgAB</jats:italic> mutants. The Δ <jats:italic>lytS</jats:italic> strain displayed significantly increased <jats:italic>in vitro</jats:italic> susceptibilities to all HDPs tested (neutrophil-derived human neutrophil peptide 1 [hNP-1], platelet-derived thrombin-induced platelet microbicidal proteins [tPMPs], and the tPMP-mimetic peptide RP-1), as well as to calcium-daptomycin (DAP), a cationic antimicrobial peptide (CAP). In contrast, the Δ <jats:italic>lrgAB</jats:italic> strain exhibited no significant changes in susceptibilities to these cationic peptides, indicating that although <jats:italic>lytSR</jats:italic> positively regulates transcription of <jats:italic>lrgAB</jats:italic> , increased HDP/CAP susceptibilities in the Δ <jats:italic>lytS</jats:italic> mutant were <jats:italic>lrgAB</jats:italic> independent. Further, parental UAMS-1 (but not the Δ <jats:italic>lytS</jats:italic> mutant) became more resistant to hNP-1 and DAP following pretreatment with carbonyl cyanide <jats:italic>m</jats:italic> -chlorophenylhydrazone (CCCP) (a CM-depolarizing agent). Of note, <jats:italic>lytSR</jats:italic> -dependent survival against CAP/HDP killing was not associated with changes in either surface positive charge, expression of <jats:italic>mprF</jats:italic> and <jats:italic>dlt</jats:italic> , or CM fluidity. The Δ <jats:italic>lytS</jats:italic> strain (but not the Δ <jats:italic>lrgAB</jats:italic> mutant) displayed a significant reduction in target tissue survival in an endocarditis model during DAP treatment. Collectively, these results suggest that the <jats:italic>lytSR</jats:italic> TCRS plays an important role in adaptive responses of <jats:named-content xmlns:xlink="http://www.w3.org/1999/xlink" content-type="genus-species" xlink:type="simple">S. aureus</jats:named-content> to CM-perturbing HDPs/CAPs, likely by functioning as a sense-response system for detecting subtle changes in ΔΨ. </jats:p> |
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| spelling | Yang, Soo-Jin Xiong, Yan Q. Yeaman, Michael R. Bayles, Kenneth W. Abdelhady, Wessam Bayer, Arnold S. 0066-4804 1098-6596 American Society for Microbiology Infectious Diseases Pharmacology (medical) Pharmacology http://dx.doi.org/10.1128/aac.00412-13 <jats:title>ABSTRACT</jats:title> <jats:p> Many host defense cationic antimicrobial peptides (HDPs) perturb the staphylococcal cell membrane (CM) and alter transmembrane potential (ΔΨ) as key parts of their lethal mechanism. Thus, a sense-response system for detecting and mediating adaptive responses to such stresses could impact organism survival; the <jats:named-content xmlns:xlink="http://www.w3.org/1999/xlink" content-type="genus-species" xlink:type="simple">Staphylococcus aureus</jats:named-content> LytSR two-component regulatory system (TCRS) may serve as such a ΔΨ sensor. One well-known target of this system is the <jats:italic>lrgAB</jats:italic> operon, which, along with the related <jats:italic>cidABC</jats:italic> operon, has been shown to be a regulator in the control of programmed cell death and lysis. We used an isogenic set of <jats:named-content xmlns:xlink="http://www.w3.org/1999/xlink" content-type="genus-species" xlink:type="simple">S. aureus</jats:named-content> strains: (i) UAMS-1, (ii) its isogenic Δ <jats:italic>lytS</jats:italic> and Δ <jats:italic>lrgAB</jats:italic> mutants, and (iii) plasmid-complemented Δ <jats:italic>lytSR</jats:italic> and Δ <jats:italic>lrgAB</jats:italic> mutants. The Δ <jats:italic>lytS</jats:italic> strain displayed significantly increased <jats:italic>in vitro</jats:italic> susceptibilities to all HDPs tested (neutrophil-derived human neutrophil peptide 1 [hNP-1], platelet-derived thrombin-induced platelet microbicidal proteins [tPMPs], and the tPMP-mimetic peptide RP-1), as well as to calcium-daptomycin (DAP), a cationic antimicrobial peptide (CAP). In contrast, the Δ <jats:italic>lrgAB</jats:italic> strain exhibited no significant changes in susceptibilities to these cationic peptides, indicating that although <jats:italic>lytSR</jats:italic> positively regulates transcription of <jats:italic>lrgAB</jats:italic> , increased HDP/CAP susceptibilities in the Δ <jats:italic>lytS</jats:italic> mutant were <jats:italic>lrgAB</jats:italic> independent. Further, parental UAMS-1 (but not the Δ <jats:italic>lytS</jats:italic> mutant) became more resistant to hNP-1 and DAP following pretreatment with carbonyl cyanide <jats:italic>m</jats:italic> -chlorophenylhydrazone (CCCP) (a CM-depolarizing agent). Of note, <jats:italic>lytSR</jats:italic> -dependent survival against CAP/HDP killing was not associated with changes in either surface positive charge, expression of <jats:italic>mprF</jats:italic> and <jats:italic>dlt</jats:italic> , or CM fluidity. The Δ <jats:italic>lytS</jats:italic> strain (but not the Δ <jats:italic>lrgAB</jats:italic> mutant) displayed a significant reduction in target tissue survival in an endocarditis model during DAP treatment. Collectively, these results suggest that the <jats:italic>lytSR</jats:italic> TCRS plays an important role in adaptive responses of <jats:named-content xmlns:xlink="http://www.w3.org/1999/xlink" content-type="genus-species" xlink:type="simple">S. aureus</jats:named-content> to CM-perturbing HDPs/CAPs, likely by functioning as a sense-response system for detecting subtle changes in ΔΨ. </jats:p> Role of the LytSR Two-Component Regulatory System in Adaptation to Cationic Antimicrobial Peptides in Staphylococcus aureus Antimicrobial Agents and Chemotherapy |
| spellingShingle | Yang, Soo-Jin, Xiong, Yan Q., Yeaman, Michael R., Bayles, Kenneth W., Abdelhady, Wessam, Bayer, Arnold S., Antimicrobial Agents and Chemotherapy, Role of the LytSR Two-Component Regulatory System in Adaptation to Cationic Antimicrobial Peptides in Staphylococcus aureus, Infectious Diseases, Pharmacology (medical), Pharmacology |
| title | Role of the LytSR Two-Component Regulatory System in Adaptation to Cationic Antimicrobial Peptides in Staphylococcus aureus |
| title_full | Role of the LytSR Two-Component Regulatory System in Adaptation to Cationic Antimicrobial Peptides in Staphylococcus aureus |
| title_fullStr | Role of the LytSR Two-Component Regulatory System in Adaptation to Cationic Antimicrobial Peptides in Staphylococcus aureus |
| title_full_unstemmed | Role of the LytSR Two-Component Regulatory System in Adaptation to Cationic Antimicrobial Peptides in Staphylococcus aureus |
| title_short | Role of the LytSR Two-Component Regulatory System in Adaptation to Cationic Antimicrobial Peptides in Staphylococcus aureus |
| title_sort | role of the lytsr two-component regulatory system in adaptation to cationic antimicrobial peptides in staphylococcus aureus |
| title_unstemmed | Role of the LytSR Two-Component Regulatory System in Adaptation to Cationic Antimicrobial Peptides in Staphylococcus aureus |
| topic | Infectious Diseases, Pharmacology (medical), Pharmacology |
| url | http://dx.doi.org/10.1128/aac.00412-13 |