Comparative Study of Two Plasticins: Specificity, Interfacial Behavior, and Bactericidal Activity Export

@article{citeulike:5770540, abstract = {PMID: 19711984 A comparative study was designed to evaluate the staphylococcidal efficiency of two sequence-related plasticins from the dermaseptin superfamily we screened previously. Their bactericidal activities against Staphylococcus aureus as well as their chemotactic potential were investigated. The impact of the GraS/GraR two-component system involved in regulating resistance to cationic antimicrobial peptides (CAMPs) was evaluated. Membrane disturbing activity was quantified by membrane depolarization assays using the diS-C3 probe and by membrane integrity assays measuring β-galactosidase activity with recombinant strain ST1065 reflecting compromised membranes and cytoplasmic leakage. Interactions of plasticins with membrane models composed of either zwitterionic lipids mimicking the S. aureus membrane of CAMP-resistant strains or anionic lipids mimicking the negative charge-depleted membrane of CAMP-sensitive strains were analyzed by jointed Brewster angle microscopy (BAM), polarization modulation infrared reflection absorption spectroscopy (PM-IRRAS), and differential scanning calorimetry (DSC) to yield detailed information about the macroscopic interfacial organization, in situ conformation, orientation of the peptides at the lipid−solvent interface, and lipid-phase disturbance. We clearly found evidence of distinct interfacial behaviors of plasticins we linked to the distribution of charges along the peptides and structural interconversion properties at the membrane interface. Our results also suggest that amidation might play a key role in GraS/GraR-mediated CAMP sensing at the bacterial surface.}, author = {Joanne, Pierre and Falord, Mélanie and Chesneau, Olivier and Lacombe, Claire and Castano, Sabine and Desbat, Bernard and Auvynet, Constance and Nicolas, Pierre and Msadek, Tarek and El Amri, Chahrazade}, citeulike-article-id = {5770540}, citeulike-linkout-0 = {http://dx.doi.org/10.1021/bi901222p}, citeulike-linkout-1 = {http://pubs.acs.org/doi/abs/10.1021/bi901222p}, day = {13}, doi = {10.1021/bi901222p}, journal = {Biochemistry}, keywords = {antimicrobial-peptide}, month = {October}, number = {40}, pages = {9372--9383}, posted-at = {2009-10-06 15:15:01}, priority = {2}, title = {Comparative Study of Two Plasticins: Specificity, Interfacial Behavior, and Bactericidal Activity}, url = {http://dx.doi.org/10.1021/bi901222p}, volume = {48}, year = {2009} }

TY - JOUR ID - citeulike:5770540 L3 - citeulike-article-id:5770540 N2 - PMID: 19711984 A comparative study was designed to evaluate the staphylococcidal efficiency of two sequence-related plasticins from the dermaseptin superfamily we screened previously. Their bactericidal activities against Staphylococcus aureus as well as their chemotactic potential were investigated. The impact of the GraS/GraR two-component system involved in regulating resistance to cationic antimicrobial peptides (CAMPs) was evaluated. Membrane disturbing activity was quantified by membrane depolarization assays using the diS-C3 probe and by membrane integrity assays measuring β-galactosidase activity with recombinant strain ST1065 reflecting compromised membranes and cytoplasmic leakage. Interactions of plasticins with membrane models composed of either zwitterionic lipids mimicking the S. aureus membrane of CAMP-resistant strains or anionic lipids mimicking the negative charge-depleted membrane of CAMP-sensitive strains were analyzed by jointed Brewster angle microscopy (BAM), polarization modulation infrared reflection absorption spectroscopy (PM-IRRAS), and differential scanning calorimetry (DSC) to yield detailed information about the macroscopic interfacial organization, in situ conformation, orientation of the peptides at the lipid−solvent interface, and lipid-phase disturbance. We clearly found evidence of distinct interfacial behaviors of plasticins we linked to the distribution of charges along the peptides and structural interconversion properties at the membrane interface. Our results also suggest that amidation might play a key role in GraS/GraR-mediated CAMP sensing at the bacterial surface. IS - 40 JF - Biochemistry EP - 9383 TI - Comparative Study of Two Plasticins: Specificity, Interfacial Behavior, and Bactericidal Activity VL - 48 SP - 9372 KW - antimicrobial-peptide AU - Joanne, Pierre AU - Falord, Mélanie AU - Chesneau, Olivier AU - Lacombe, Claire AU - Castano, Sabine AU - Desbat, Bernard AU - Auvynet, Constance AU - Nicolas, Pierre AU - Msadek, Tarek AU - El Amri, Chahrazade PY - 2009/10/13/ UR - http://dx.doi.org/10.1021/bi901222p ER -