TY - JOUR
T1 - PrfA activation in Listeria monocytogenes increases the sensitivity to class IIa bacteriocins despite impaired expression of the bacteriocin receptor
AU - Farizano, Juan V.
AU - Masías, Emilse
AU - Hsu, Fong Fu
AU - Salomón, Raúl A.
AU - Freitag, Nancy E.
AU - Hebert, Elvira María
AU - Minahk, Carlos
AU - Saavedra, Lucila
N1 - Funding Information:
J.V.F. and E.M. are recipients of a CONICET fellowship. R.A.S., L.S. and C.M. are career investigators of CONICET. Financial support was provided by Agencia Nacional de Promoción Científica y Tecnológica ( PICT 2012 N°2998 and PICT 2011 N°0175 ), Consejo Nacional de Investigaciones Científicas y Técnicas (Grant PIP 0530 ), Secretaría de Ciencia y Técnica de la Universidad Nacional de Tucumán ( PIUNT 2018 D641/2 ). The Washington University School of Medicine Mass spectrometry facility is supported by US Public Health Service Grants P41-GM103422 , P60-DK-20579 , P30-DK56341 , 4R33HL120760-03 and R01AI130454 .
Funding Information:
J.V.F. and E.M. are recipients of a CONICET fellowship. R.A.S. L.S. and C.M. are career investigators of CONICET. Financial support was provided by Agencia Nacional de Promoción Científica y Tecnológica (PICT 2012 N°2998 and PICT 2011 N°0175), Consejo Nacional de Investigaciones Científicas y Técnicas (Grant PIP 0530), Secretaría de Ciencia y Técnica de la Universidad Nacional de Tucumán (PIUNT 2018 D641/2). The Washington University School of Medicine Mass spectrometry facility is supported by US Public Health Service Grants P41-GM103422, P60-DK-20579, P30-DK56341, 4R33HL120760-03 and R01AI130454.
Publisher Copyright:
© 2019 Elsevier B.V.
PY - 2019/8
Y1 - 2019/8
N2 - Background: The scope of the present work was to characterize the activity of class IIa bacteriocins in Listeria (L.)monocytogenes cells that constitutively express an activated form of PrfA, the virulence master regulator, since bacteriocin sensitivity was only characterized in saprophytic cells so far. The mannose phosphotransferase system (Man-PTS)has been shown to be the class IIa bacteriocin receptor in Listeria; hence, special attention was paid to its expression in virulent bacteria. Methods: L. monocytogenes FBprfA* cells were obtained by transconjugation. Bacterial growth was studied in TSB and glucose containing-minimal medium. Sensitivity to antimicrobial peptides was assessed by killing curves. Membranes of L. monocytogenes FBprfA* cells were characterized using proteomic and lipidomic approaches. Results: The mannose phosphotransferase system (Man-PTS)was downregulated upon expression of PrfA*, and these cells turned out to be more sensitive to enterocin CRL35 and pediocin PA-1, while not to nisin. Proteomic and lipidomic analysis showed differences between wild type (WT)and PrfA* strains. For instance, phosphatidic acid was only detected in PrfA* cells, whereas, there was a significant decline of plasmalogen-phosphatidylglycerol in the same strain. Conclusions: Our results support a model in which Man-PTS acts just as a docking molecule that brings class IIa bacteriocins to the plasma membrane. Furthermore, our results suggest that lipids play a crucial role in the mechanism of action of bacteriocins. General significance: This is the first demonstration of the link between L. monocytogenes virulence and the bacterial sensitivity toward pediocin-like peptides.
AB - Background: The scope of the present work was to characterize the activity of class IIa bacteriocins in Listeria (L.)monocytogenes cells that constitutively express an activated form of PrfA, the virulence master regulator, since bacteriocin sensitivity was only characterized in saprophytic cells so far. The mannose phosphotransferase system (Man-PTS)has been shown to be the class IIa bacteriocin receptor in Listeria; hence, special attention was paid to its expression in virulent bacteria. Methods: L. monocytogenes FBprfA* cells were obtained by transconjugation. Bacterial growth was studied in TSB and glucose containing-minimal medium. Sensitivity to antimicrobial peptides was assessed by killing curves. Membranes of L. monocytogenes FBprfA* cells were characterized using proteomic and lipidomic approaches. Results: The mannose phosphotransferase system (Man-PTS)was downregulated upon expression of PrfA*, and these cells turned out to be more sensitive to enterocin CRL35 and pediocin PA-1, while not to nisin. Proteomic and lipidomic analysis showed differences between wild type (WT)and PrfA* strains. For instance, phosphatidic acid was only detected in PrfA* cells, whereas, there was a significant decline of plasmalogen-phosphatidylglycerol in the same strain. Conclusions: Our results support a model in which Man-PTS acts just as a docking molecule that brings class IIa bacteriocins to the plasma membrane. Furthermore, our results suggest that lipids play a crucial role in the mechanism of action of bacteriocins. General significance: This is the first demonstration of the link between L. monocytogenes virulence and the bacterial sensitivity toward pediocin-like peptides.
KW - Antimicrobial activity
KW - Bacteriocins
KW - Listeria
KW - Virulence
UR - http://www.scopus.com/inward/record.url?scp=85065255185&partnerID=8YFLogxK
U2 - 10.1016/j.bbagen.2019.04.021
DO - 10.1016/j.bbagen.2019.04.021
M3 - Article
C2 - 31059750
AN - SCOPUS:85065255185
SN - 0304-4165
VL - 1863
SP - 1283
EP - 1291
JO - Biochimica et Biophysica Acta - General Subjects
JF - Biochimica et Biophysica Acta - General Subjects
IS - 8
ER -