Pulling the Brakes on Fast and Furious Multiple Drug-Resistant (MDR) Bacteria
Abstract
:1. Introduction
2. Nanoparticles as a Weapon against Antibiotically Resistant Bacteria Extracorporally
2.1. Metal Oxide, Nitric Oxide, and Chitosan NPs
2.2. Nano-Photothermal Therapy of MDR Bacteria
2.3. Silver NPs Bactericidal Effect against Multidrug-Resistant Bacteria
2.4. Aluminum Oxide Nanoparticles
2.5. Silicon NPs
2.6. Gallium Nanoparticles (NPs)
3. Host Defense Peptides (HDPs)
4. Defensins
5. Cathelicidins
6. Antimicrobial Peptides (AMP)
7. Bacteriophage Therapy
8. Immune Stimulation via Bacterial Extracts
9. Vaccination
10. Combination Drug Therapy
10.1. Combination Drug Combination Acting on Diverse Targets in Different Pathways
10.2. Drug Combinations Acting on Diverse Targets in the Same Pathways
10.3. Drug Combination Acting on a Single Target, but in Multiple Dimensions
11. Novel Antibodies against MDR Bacteria
12. Carbon Monoxide-Releasing Molecules (CORMs)
13. Probiotics
14. Quorum Sensing
15. Vaccines vs. Drugs: Who Is Going to Win?
16. How Important Is the Accurate and Rapid Detection of the MDR Bacteria?
17. Conclusions
Author Contributions
Funding
Institutional Review Board Statement
Informed Consent Statement
Data Availability Statement
Conflicts of Interest
References
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Agent | Target Bacteria/Diseases | Mode of Action/Description | Notes (Advantages (a), Limitations (l), Combination Strategy (c)) | Ref. |
---|---|---|---|---|
Nanoparticles | ||||
AuNP with cationic surface chemistry | Gram-positive and Gram-negative bacteria | Interaction with cell membrane → formation of aggregates → bacterial cell lysis; cause protuberance | (a) Unique electronic, sensing, optical, and biochemical properties | [34,35,36,98] |
CuONP | Variety pathogens, including MRSA, E. coli, S. aureus, P. aeruginosa, N. meningitis, B. cereus, S. pyogenes, A. baumannii | ROS → induce oxidative stress | (c) Antibacterial activity enhanced by conjugation with AgNPs (photocatalytic activity attributed to the production of ROS) | [1,38,39,40,99] |
ZnONPs, colloidal ZnO suspension | MRSA, S. agalactiae, MRSE, MSSA, ESBL-producing E. coli and K. pneumoniae, Vibrio cholera, Campylobacter jejuni, E. faecalis, S. epidermidis, and other clinically relevant pathogens | Disorganization and damage of cell, cell membrane after internalization; damage of proteins, lipids, and DNA via oxidative stress | (l) Level of toxicity concentration dependent (c) Antibacterial activity enhanced by conjugation with AgNPs | [1,41,42,43,44,45,46] |
Nitric-oxide-releasing NPs (NONPs) | Antibiotic-resistant and sensitive bacteria, i.e., K. pneumoniae, E. faecalis, S. pyogenes, E. coli, and P. aeruginosa | Formation of cell toxic reactive nitrogen and oxygen intermediates, NO-associated lipid damage, iron depletion, inhibition of DNA repair enzymes | (a) NO is unstable so spontaneously generate reactive intermediates | [47,48,49,50,51,52,53,54] |
Gold nanorods | P. aeruginosa | Conjugated with primary antibodies | (a) Eradicate biofilms (c) 1,2-Distearoyl-sn-glycero-3-phosphorylethanolamine (DSPE) | [60,69] |
S. aureus and Propionibacterium acnes | Local hyperthermia by laser beam excited functionalized gold nanorods | (a) Enhanced reduction of viable bacterial count | [61] | |
AgNPs, colloidal AgNPs | Gram-positive and Gram-negative bacteria; drug-susceptible strains including Streptococcus spp., E. coli, and P. aeruginosa; MRSA, MRSE, (erythromycin-resistant) S. pyogenes, (ampicillin-resistant) E. coli, MDR P. aeruginosa | AgNPs anchor to cell wall leading to increased cell permeability by structural changes → uncontrolled transport through cell membrane; Membrane damage caused by AgNP produced free radicals; released Ag+ ions inactivate enzymes by interacting with thiol groups of enzymes | (a) Bactericidal against Gram-positive as well as Gram-negative bacteria (1) Dose-dependent | [55,74,75,76] |
Biosynthetically produces AgNPs using fungus, yeast, bacteria, and plant extracts | M. tuberculosis, P. aeruginosa, S. pneumoniae, MRSA, K. pneumoniae, MRSE, S. pyogenes, Bacillus spp., E. coli and S. typhi | Inhibit cell wall synthesis, protein synthesis, which is mediated by the 30 s ribosomal subunit, and nucleic acid synthesis | (a) Strong antibacterial efficacy against various MDR pathogens | [81,82,83] |
Aluminum oxide NPs | E. coli, Pseudomonas fluorescence, Staphylococcus aureus, Streptococcus mutans, Proteus vulgaris) | Disruption of bacterial cell wall by producing ROS, Serve as radical scavengers leading to distortion in bacterial cells | (a) Thermodynamically stable over a wide range of temperatures | [88,89,90] |
Ethionamide (ETH)-conjugated SiNPs (silicon) | Multidrug-resistant M. tuberculosis | Enhance solubility and permeability of ETH at different pH-values | (a) Reduction of dosing frequency of ETH for the treatment of multidrug-resistant M. tuberculosis (c) thermally carbonized-porous silicon (TCPSi) loaded with ethionamide (ETH) | [94] |
Gallium (III) nano-formulations | Drug-resistant M. tuberculosis | Targeted drug delivery, Promotion of maturation of phagosome → increased macrophage-mediated killing, Interruption of iron-mediated enzymatic reactions | (a) Active against resistant bacteria like M. tuberculosis, HIV | [96] |
Nano-photothermal therapy | ||||
AuNPs | Gram-positive bacteria, Gram-negative bacteria | Electromagnetic radiation absorbed by the NPs converted into heat → transferred via thermal conduction to bacteria in close proximities | (c) Conjugated with vancomycin or amoxicillin | [62,63,67] |
Au nanorods | Pathogenic E. coli | Generate heat that lyses bacteria | (c) Heat generated by using continuous-wave laser irradiation or near-infrared laser | [29] |
Au nanorods | P. aeruginosa | Nanorod attach to the bacterial cell surface allows the cell to expose to near-infrared radiation | (c) Conjugated with primary antibodies | [1,69] |
Multifunctional popcorn-shaped magnetic iron core-shell gold nanoparticles | Salmonella DT104 | Selective and irreparable cellular-damage | (c) Conjugated with Salmonella DT104 specific antibody | [70] |
Polysiloxane polymers containing embedded methylene blue and AuNPs | MRSA and E. coli | Light-induced production of singlet oxygen and other reactive oxygen species by the methylene blue and gold nanoparticles enhanced activity of methylene blue | (a) Significant reduction of viable cell count (1) Require exposure to light and polymer formation | [1,71,72] |
Category | Agent | Target Bacteria/Diseases | Mode of Action/Description | Notes (Advantages (a), Limitations (l), Combination Strategy (c)) | Status | Ref |
---|---|---|---|---|---|---|
HDP | Brevinin1 HYba1 and brevinin1 HYba2 | Several Gram-positive and Gram-negative bacteria | Hemolytic, cytotoxic and antibacterial activities | (a) Very low hemolysis on human erythrocytes | Hep 3B cancer cell line | [101] |
HDP (Defensin) | 68 fungal defensin-like peptides (fDLPs) | A variety of bacterial, fungal and viral pathogens | (i) Cationic amphipathic peptides having approximately 30 amino acid residues (ii) From five genera named Apophysomyces, Trichosporon, Scedosporium, Beauveria, and Lichtheimia had been reported | (a) Higher antibacterial potential with lower cellular toxicities | In vitro and in vivo | [105] |
Scedosporisin (synthetic defensin) | Gram-positive bacteria, vancomycin-resistant Enterococci, MRSA | Scedosporisin-2 killed bacteria more rapidly as compared to the antibiotic vancomycin | (a) Low cytotoxicity and hemolysis on human | In vitro | [105] | |
HDP (Cathelicidin) | Bactenecin, indolicidin, protegrins,… | S. pyogenes and MRSA, VISA, Listeria | Produced by the immune systems of bovine and porcine | (a) Broad bacterial lytic properties, stability and higher efficacy | In vitro and in vivo | [106] |
Human cathelicidin LL-37 | Antibiofilm activity against S. aureus and E. coli | Human immune system is known to produce only one type of cathelicidin precursor protein, hCAP18 → processed proteolytically to produce mature LL-37 | (1) Exact mechanisms of interaction between LL-37 and immune cells have not been yet clarified | In vitro and in vivo | [107] | |
CATHPb1–6 (six novel cathelicidins identified from Python bivittatu) | S. aureus (MRSA/VRSA) | Involved in modulating macrophages/monocytes; trafficking neutrophils to the site of infection and also enhance their bactericidal functions; increases levels of chemokines and reduces release of proinflammatory cytokines | (a) Provides protection via different administration routes | In vitro and in vivo (mice) | [108] |
Category | Agent | Target Bacteria/Diseases | Mode of Action/Description | Notes (Advantages (a), Limitations (l), Combination Strategy (c)) | Status | Ref. |
---|---|---|---|---|---|---|
ABP | Nisin | Variety of Gram-positive | Cationic peptide | (1) Requires proper optimization of pH | In vitro | [114] |
ABP + HDP | Combination of peptides and defensin proteins | Variety of Gram-positive and Gram-negative bacteria; effective against fungi too | Proteinaceous entities can either be cationic or amphipathic | (a) Not require any specific protein binding sites | In vitro | [113] |
ABP | Antimicrobial peptides KT2 and RT2 | Antibiofilm activity against MDR enterohemorrhagic E. coli O157:H7 | Tryptophan-rich cationic peptides permeabilize bacterial cell membranes → lead to death of cells by causing large damage or small obstructions that disturb transmembrane potential | (a) Not only prevent biofilm formation but also can eliminate mature biofilms (l) Interactions with membrane and each other (c) Combination with other antimicrobial compounds to enhance activity → lower concentration of antimicrobial compounds | In vivo | [100,120] |
Agelaia-MPI and Polybia-MPII | MDR Acinetobacter baumannii, several Gram-positive and Gram-negative bacteria, Mycobacteria as well as fungi | Isolated from wasps; bactericidal activity along with antibiofilm activity | (l) Production costs (l) Peptidases and proteases lead to low stability of peptides in human serum → (c) Increased stability in combination with other molecules (e.g., polyethylene glycol) | In vitro | [129] | |
Ocellatin-PT2–PT6 | Opportunistic pathogen Pseudomonas aeruginosa | Ocellatin-PT3 inhibits proliferation of established biofilms by directly killing bacterial cells | (a) Novel antimicrobial agent(l) Works better in combination BS antibiotics | in vitro | [130] | |
QS + ABP | “RNAIII-inhibiting peptide” (RIP) | Biofilm formation and ailments caused by S. aureus | Inhibition of phosphorylation of “target of RNAIII activating protein” → quorum sensing inhibition, prevention of MDR in bacteria | (a) Inhibits cell adhesion and biofilm formation | In vitro and in vivo (cellulitis) | [135,136] |
Agent | Target Bacteria/Diseases | Mode of Action/Description | Notes (Advantages (a), Limitations (l), Combination Strategy (c)) | Status | Ref |
---|---|---|---|---|---|
Bacteriophages | |||||
ϕMR11, KP DP1, SA DP1, PA DP4, EC DP3 | E. faecalis, S. aureus, Klebsiella, A. baumannii, P. aeruginosa, and Escherichia coli | Phages bind to specific receptors on bacterial cell surface → infects bacterial cells → production of endolysins that damage bacterial cell wall by hydrolyzing four main bonds of peptidoglycan, Rupture of outer membrane via complexes (spanins) (Gram-negative bacteria) | (a) Applied externally and internally; high affinity for specific bacterium (normal flora not attacked) only one administration (replicative nature); can survive in the gastric environment; minimal side effects → ecologically safe; frequency of bacterial resistance to phages significantly lower compared with resistance to antibiotics (l) Not very effective in mixed infections (narrow host range) | In vivo (mice) | [19,169] |
Lytic phage strain (KPP10) | P. aeruginosa | Decreased numbers of viable P. aeruginosa cells in blood, liver, and spleen as well as levels of inflammatory cytokines in blood and liver | (c) Oral administration | Animal models | [153] |
CD140 | Clostridium difficile-induced ileocolitis | Phage administration prophylaxis against infection | (1) Specific against Clostridium difficile | hamster | [148] |
ØCDHM1–ØCDHM6, ØCDHS1, ENB6 and C33, Ø9882, ØA392, and KPP10 | Clostridium difficile, vancomycin-resistant E. faecium, extended-spectrum β-lactamase producing E. coli, imipenem-resistant and MDR P. aeruginosa | Treatment of gut-derived sepsis | (a) Specifically act against bacterial pathogens (a) Do not affect the natural bioflora (a) Safer to use in humans (1) They will be effective only if their favorable conditions exist | Hamsters and mice | [150,154] |
OMKO1 | MDR P. aeruginosa | Outer membrane porin M (OprM) of the multidrug efflux systems MexAB and MexXY as a receptor-binding site | (a) Specifically act against MDR P. aeruginosa (a) Alters efflux pump mechanism to make the bacterium more susceptible to drugs | In vitro | [154] |
PBAB08 and PBAB25 | Acinetobacter baumannii | Reduction of bacterial load, increase in serum IgE with a slight increase of GM-CSF, IL2, IL10, and IL17A | (1) Inoculated in a cocktail and require properly set optimal conditions | mouse | [163] |
Mixture of three phages | Campylobacter jejuni and C. coli | Reduce bacterial colonization | (1) Acquisition phage to resistance | Poultry | [143] |
PlyF307 (phage lysin) | MDR A. baumannii | Lysing of bacterial cells | (a) Inactive against eukaryotic cells | Mouse | [163] |
Cpl-1 (phage endolysin) | Streptococcus pneumoniae | Reduced pulmonary bacterial counts and prevented bacteremia, systemic hypotension, and lactate increase as well as reduction of penicillin-susceptible pneumococci | (1) Specific against pneumococci | Mouse | [164] |
PGHs (phage endolysins) | MRSA | The peptidoglycan hydrolase enzyme targets the conserved regions and can destroy a wide range of mutant cell walls of bacteria | (a) Active against mutant and resistant strains (a) Also can clear static biofilms | In vitro and in Mouse | [165] |
PlyCD (prophage lysin) | C. difficile | PlyCD specifically targets the pathogenic C. difficile while not affecting other commensal bacteria | (c) Phage lysins in combination with antibiotics more effective than antibiotics alone | Ex vivo mouse colon model | [166] |
PlySs2 (phage endolysin) | Streptococcus and Staphylococcus species, such as MRSA | Lytic activity | (a) High therapeutic potential compared to other lysins | Mouse | [167] |
PlyC (phage endolysin) | S. pyogenes | Lysins can cross the epithelial cell membrane to eradicate intracellular infections | (a) Ability to traverse epithelial membranes | model membranes | [168] |
PlyG (phage endolysin) | Bacillus anthracis | Interrupt vegetative cells; major advantage over antibiotics (attacking endospores) | (a) Separate domains to recognize spores and vegetative cells | In vitro | [170] |
Agent | Target Bacteria/Diseases | Mode of Action/Description | Notes (Advantages (a), Limitations (l), Combination Strategy (c)) | In Vitro, In Vivo, Clinical Phase, Animal Model | Ref |
---|---|---|---|---|---|
Vaccines | |||||
Tetra-subunit vaccine | S. aureus | Comprising of two capsular polysaccharides and two virulence-associated proteins (ClfA and MntC) | (c) Diminish the burden of the disease, thereby reducing use of antibiotics | Phase 2b trial | [175] |
Three different vaccines | C. difficile | Constructed on C. difficile toxins A and B | (1) More research is required for proper optimizations of toxin-based vaccines, including development and use of novel adjuvants | Phase 2 and 3 trials | [189] |
OprF/I fusion protein vaccine | P. aeruginosa | Founded on conserved outer membrane protein F/I fusion | (a) Produce rapid immune response in healthy volunteers | Phase 2/3 trials | [175,190] |
Vaccine NDV-3 | Candida | Targeting T cell target protein, Als3 | (a) Also protects from intravenous as well as skin and soft tissue infection with Staphylococcus aureus | Phase 2 trials | [184] |
Antiresistance vaccines | MRSA | Cloned internal region from transpeptidase domain from penicillin-binding protein (PBP2a) as DNA vaccine | (a) More operational against drug-resistant strains by explicitly targeting resistant alleles of a conserved protein or by targeting proteins exclusively present in resistant clusters | Mouse | [186] |
Antiresistance vaccines | Neisseria meningitidis | Vaccination with purified recombinant PBP2 + passive immunization with anti-PBP2 rabbit IgG antibody | (a) This vaccine candidate has a conserved region that is present in all strains of N. meningitidis and targeted by protective antibodies | Mouse | [175,188] |
Combination Drug Therapy | ||||
---|---|---|---|---|
Agent | Target Bacteria/ Diseases | Mode of Action/Description | Notes (Advantages (a), Limitations (l), Combination Strategy (c)) | Ref |
Combination drug combination acting on diverse targets in different pathways | ||||
Rifampicin (R), isoniazid (H), ethambutol (E), and pyrazinamide (Z) | M. tuberculosis | Rifampicin (RNA polymerase inhibitor), isoniazid (enoyl reductase subunit of fatty acid synthase), ethambutol (an inhibitor of arabinosyl transferases involved in cell wall biosynthesis) and pyrazinamide (mechanism of action poorly understood) | (a) Method highly effective since a bacterium may develop resistance by changing one of its targets, the combination drug strategy will still be effective against at least the other two pathways | [147,192,193] |
Drug combinations acting on diverse targets in the same pathways | ||||
Clavulanic acid | Gram-positive bacteria | Degrades the β-lactamase enzyme, allowing the drug to destroy these microorganisms | (c) Use of a β-lactam antibiotic (amoxicillin) and β-lactamase enzyme inhibitor (clavulanic acid) | [187] |
Drug combination acting on a single target, but in multiple dimensions | ||||
Streptogramins | Two active molecules that bind to the adjacent sites in the 50S ribosomal subunit near the peptidyl transferase center | (c) Both of these molecules are used simultaneously; they show 10–100-fold more potency as compared to using a single molecule alone | [194,195,196] |
Agent | Target Bacteria/Diseases | Mode of Action/Description | Notes (Advantages (a), Limitations (l), Combination Strategy (c)) | In Vitro, In Vivo, Clinical Phase, Animal Model | Ref |
---|---|---|---|---|---|
Antibodies | |||||
A1102 (humanized mouse gal-III mAb) | K. pneumoniae ST258 | Passive immunization with A1102 before infection with ST258 → infection prophylaxis | (1) Efficacy and exact role for protection in vivo not understood | In vitro and in vivo in experimental models (mice) | [197] |
O25b-specific mAb ASN-4 | MCR-1-positive colistin-resistant ST131-H30 strain | Oopsonophagocytosis, endotoxin neutralization, and complement-mediated killing | (a) Multiple mechanisms of action | In vitro and in vivo in experimental models (Murine models) | [198] |
MEDI3902 | P. aeruginosa | Bispecific antibody targeting the P. aeruginosa type III secretion (T3S) protein PcrV and Psl exopolysaccharide | (c) In combination with drug therapy (antibiotics) deliver assistance when used alongside antibiotics | In vivo (mice) | [199] |
Agent | Target Bacteria/Diseases | Mode of Action/Description | Notes (Advantages (a), Limitations (l), Combination Strategy (c)) | Status | Ref. |
---|---|---|---|---|---|
Probiotics | |||||
Lactobacillus and Bifidobacterium | E. coli, Salmonella, Helicobacter pylori, Listeria monocytogenes and rotavirus | Lessen occurrence, time period, and/or ruthlessness of antibiotic-linked gastroenteritis → enhancing efficacy of these antibiotics | (c) Simultaneous utilization of probiotics with antibiotics | In vivo | [204] |
Lactobacillus acidophilus strain | P. aeruginosa | Inhibit development of drug-resistant bacteria by secretion of antibacterial chemicals including lactic acid, hydrogen peroxide, diminishing MDRs ability to colonize the body → reducing use of antibiotics | (a) Reduced use of antibiotics and development of MDR by providing protection against intrinsic resistance strains | In vitro | [20,21] |
Lactobacilli | MDR K. pneumoniae | Used in place of antibiotic therapy | (1) Require identification of more strains | In vitro | [205] |
Propionibacterium freudenreichii freudenreichii B3523 (PF) and P. freudenreichii shermanii B4327 (PS)) | MDR Salmonella heidelberg (SH) | Used as an alternative to antibiotics for preventing SH infections | (a) Non-host gastrointestinal tract-derived probiotic | Turkey poults | [206] |
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Khan, A.A.; Manzoor, K.N.; Sultan, A.; Saeed, M.; Rafique, M.; Noushad, S.; Talib, A.; Rentschler, S.; Deigner, H.-P. Pulling the Brakes on Fast and Furious Multiple Drug-Resistant (MDR) Bacteria. Int. J. Mol. Sci. 2021, 22, 859. https://doi.org/10.3390/ijms22020859
Khan AA, Manzoor KN, Sultan A, Saeed M, Rafique M, Noushad S, Talib A, Rentschler S, Deigner H-P. Pulling the Brakes on Fast and Furious Multiple Drug-Resistant (MDR) Bacteria. International Journal of Molecular Sciences. 2021; 22(2):859. https://doi.org/10.3390/ijms22020859
Chicago/Turabian StyleKhan, Abid Ali, Khanzadi Nazneen Manzoor, Aamir Sultan, Maria Saeed, Mahrukh Rafique, Sameen Noushad, Ayesha Talib, Simone Rentschler, and Hans-Peter Deigner. 2021. "Pulling the Brakes on Fast and Furious Multiple Drug-Resistant (MDR) Bacteria" International Journal of Molecular Sciences 22, no. 2: 859. https://doi.org/10.3390/ijms22020859