A systematic quantitative proteomic examination of multidrug resistance in Acinetobacter baumannii

Chopra, Sidharth; Ramkissoon, Kevin; Anderson, Dave

doi:10.1016/j.jprot.2013.03.008

Cited by 44 publications

(32 citation statements)

References 150 publications

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“…P. aeruginosa bEPS is also effective in counteracting chlorine and monochloramine disinfectants, reducing their availability and prolonging cell life (31). A multidrug-resistant strain of A. baumannii produces bEPS in abundance compared to a drugsensitive strain (32). While the bEPS fraction appears significant for protection inside the biofilm, it was not a significant factor in our ex situ experiments against tobramycin.…”

Section: Fig 2 Addition Of Eps From Acinetobacter Baumannii But Not mentioning

confidence: 81%

Differential Protection from Tobramycin by Extracellular Polymeric Substances from Acinetobacter baumannii and Staphylococcus aureus Biofilms

Davenport

Call

Beyenal

2014

Antimicrob Agents Chemother

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bWe investigated biofilms of two pathogens, Acinetobacter baumannii and Staphylococcus aureus, to characterize mechanisms by which the extracellular polymeric substance (EPS) found in biofilms can protect bacteria against tobramycin exposure. To do so, it is critical to study EPS-antibiotic interactions in a homogeneous environment without mass transfer limitations. Consequently, we developed a method to grow biofilms, harvest EPS, and then augment planktonic cultures with isolated EPS and tobramycin. We demonstrated that planktonic cultures respond differently to being treated with different types of EPS (A. baumannii versus S. aureus) in the presence of tobramycin. By harvesting EPS from the biofilms, we found that A. baumannii EPS acts as a "universal protector" by inhibiting tobramycin activity against bacterial cells regardless of species; S. aureus EPS did not show any protective ability in cell cultures. Adding Mg 2؉ or Ca 2؉ reduced the protective effect of A. baumannii EPS. Finally, when we selectively digested the proteins or DNA of the EPS, we found that the protective ability did not change, suggesting that neither has a significant role in protection. To the best of our knowledge, this is the first study that demonstrates how EPS protects pathogens against antibiotics in a homogeneous system without mass transfer limitations. Our results suggest that EPS protects biofilm communities, in part, by adsorbing antibiotics near the surface. This may limit antibiotic diffusion to the bottom of the biofilms but is not likely to be the only mechanism of protection.

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Section: Fig 2 Addition Of Eps From Acinetobacter Baumannii But Not mentioning

confidence: 81%

Differential Protection from Tobramycin by Extracellular Polymeric Substances from Acinetobacter baumannii and Staphylococcus aureus Biofilms

Davenport

Call

Beyenal

2014

Antimicrob Agents Chemother

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“…P. vivax iRBC proteins and peptides were prepared for analysis using the FASP-I [Pv-Proteome 1] or FASP-II [Pv-Proteome 2] protocols [37], desalted using 100 μl OMIX C18 tips (Agilent, Palo Alto, CA) [Pv-Proteome 1] or 3 M Empore disk cartridges [Pv-Proteome 2], roughly quantitated using absorbance at 280 nm [37] on a Nanodrop spectrometer (Nanodrop, Wilmington, DE), and analyzed by 2D SCX (strong cation exchange)/C18 RP (reversed phase) LC/MS/MS on a Thermo Scientific (San Jose, CA) LTQ-XL ETD Orbitrap mass spectrometer with New Objective (Woburn, MA) PV-550 source [38]. Precursor ions were analyzed in the Orbitrap, and MS/MS spectra were analyzed in the linear ion trap.…”

Section: Methodsmentioning

confidence: 99%

Plasmodium vivax trophozoite-stage proteomes

Anderson

Lapp

Akinyi

et al. 2015

Journal of Proteomics

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Plasmodium vivax is the causative infectious agent of 80–300 million annual cases of malaria. Many aspects of this parasite’s biology remain unknown. To further elucidate the interaction of P. vivax with its Saimiri boliviensis host, we obtained detailed proteomes of infected red blood cells, representing the trophozoite-enriched stage of development. Data from two of three biological replicate proteomes, emphasized here, were analyzed using five search engines, which enhanced identifications and resulted in the most comprehensive P. vivax proteomes to date, with 1375 P. vivax and 3209 S. boliviensis identified proteins. Ribosome subunit proteins were noted for both P. vivax and S. boliviensis, consistent with P. vivax’s known reticulocyte host–cell specificity. A majority of the host and pathogen proteins identified belong to specific functional categories, and several parasite gene families, while 33% of the P. vivax proteins have no reported function. Hemoglobin was significantly oxidized in both proteomes, and additional protein oxidation and nitration was detected in one of the two proteomes. Detailed analyses of these post-translational modifications are presented. The proteins identified here significantly expand the known P. vivax proteome and complexity of available host protein functionality underlying the host–parasite interactive biology, and reveal unsuspected oxidative modifications that may impact protein function. Biological significance Plasmodium vivax malaria is a serious neglected disease, causing an estimated 80 to 300 million cases annually in 95 countries. Infection can result in significant morbidity and possible death. P. vivax, unlike the much better-studied Plasmodium falciparum species, cannot be grown in long-term culture, has a dormant form in the liver called the hypnozoite stage, has a reticulocyte host–cell preference in the blood, and creates caveolae vesicle complexes at the surface of the infected reticulocyte membranes. Studies of stage-specific P. vivax expressed proteomes have been limited in scope and focused mainly on pathogen proteins, thus limiting understanding of the biology of this pathogen and its host interactions. Here three P. vivax proteomes are reported from biological replicates based on purified trophozoite-infected reticulocytes from different Saimiri boliviensis infections (the main non-human primate experimental model for P. vivax biology and pathogenesis). An in-depth analysis of two of the proteomes using 2D LC/MS/MS and multiple search engines identified 1375 pathogen proteins and 3209 host proteins. Numerous functional categories of both host and pathogen proteins were identified, including several known P. vivax protein family members (e.g., PHIST, eTRAMP and VIR), and 33% of protein identifications were classified as hypothetical. Ribosome subunit proteins were noted for both P. vivax and S. boliviensis, consistent with this parasite species’ known reticulocyte host–cell specificity. In two biological replicates analyzed for post-translational modif...

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“…Oxidant pressure caused by the overproduction of ROS could destroy the biological protein and cytomembrane, even change the activity of some enzyme (Marques and Soares 2011). Chopra et al (2013) had compared the proteome of the multidrug resistant strain BAA-1605 with that of the drug-sensitive strain ATCC 17978 by large-scale quantitative proteomics and found that 114 of 1484 proteins were more abundant and 99 were less abundant. Some proteins with twofold or greater abundance were relative to antibiotic-and heavy metal-resistance proteins.…”

Section: Effects Of Zn Concentration and Binary Exposure On Bacterialmentioning

confidence: 99%

Antioxidative responses of Pseudomonas fluorescens YZ2 to simultaneous exposure of Zn and Cefradine

Chen

et al. 2015

Ecotoxicology

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Binary pollution of both heavy metals and antibiotics has received increasing attentions for their joint effects of eco-toxicity and health hazards. To reveal the effects of mixtures of different pollutants on bacterial antioxidant response system, Pseudomonas fluorescens ZY2, a new strain isolated from swine wastewater, was chosen to determinate growth (bacterial density OD600), reactive oxygen species (ROS) concentration, protein concentration and superoxide dismutase (SOD) activity under exposure treatments of Zn, Cefradine or Zn + Cefradine. Bacterial densities of all the treatment groups increased significantly over the incubation time, but those containing pollutant addition were slightly lower than the control at different times of incubation. Both ROS concentration and SOD activity increased first and then decreased (p < 0.01) over time, which was opposite to the protein concentrations (p < 0.01), showing a much significant increase by Cefradine alone. With Zn concentration increasing from 40 to 160 mg/L, the intracellular SOD activity increased as a response to the improvement of ROS (p < 0.05), while the balance between ROS and SOD was broken down due to the disproportionate change of total SOD activity and ROS concentration, the bacterial densities therefore decreased for the weak resistance. With the combined treatment of Zn (200 mg/L) and Cefradine (1 mg/L), though the toxicity of Zn caused a much significant increase of ROS, the bacterial resistance was further improved showing a more significant increase of total SOD activity and the bacterial densities therefore increased bacterial growth. Zn concentration also affected the protein synthesis. Either single or binary stress induced the bacterial resistance by regulating SOD activity to eliminate ROS. All results of the bacterial oxidant stress, SOD response and protein synthesis in the combined treatment groups were more complicated than those in single treatment groups, which depended on the properties of the single treatment as well as the interaction between the two treatments upon bacterial activity. For P. fluorescens ZY2, the mediation of SOD activity to eliminate ROS in response to the combined exposure to Zn and Cefradine was first revealed as one of the co-resistance mechanisms, which is informative to further understanding the risk of antibiotics resistant bacteria to human and environmental health more accurately.

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A systematic quantitative proteomic examination of multidrug resistance in Acinetobacter baumannii

Cited by 44 publications

References 150 publications

Differential Protection from Tobramycin by Extracellular Polymeric Substances from Acinetobacter baumannii and Staphylococcus aureus Biofilms

Differential Protection from Tobramycin by Extracellular Polymeric Substances from Acinetobacter baumannii and Staphylococcus aureus Biofilms

Plasmodium vivax trophozoite-stage proteomes

Antioxidative responses of Pseudomonas fluorescens YZ2 to simultaneous exposure of Zn and Cefradine

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