Effect of antimicrobial peptides on ATPase activity and proton pumping in plasma membrane vesicles obtained from mycobacteria

Santos, Paola; Gordillo, Aldemar; Osses, Luis R.; Salazar, Luz-Mary; Soto, Carlos-Yesid

doi:10.1016/j.peptides.2012.04.018

Cited by 38 publications

(19 citation statements)

References 57 publications

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“…On the other hand, The minimal inhibitory concentration (MIC) of unattached MOF‐199 on E. coli cells was determined using a microplate colorimetric‐based test with resazurin as a bacterial growth indicator . The growth of bacteria was indicated by a change in the color of broth from blue to rose, and the MIC was defined as the lowest MOF‐199 concentration preventing this color change.…”

Section: Methodsmentioning

confidence: 99%

Antibacterial activity against Escherichia coli of Cu‐BTC (MOF‐199) metal‐organic framework immobilized onto cellulosic fibers

Rodríguez

Hinestroza

Ochoa‐Puentes

et al. 2014

J of Applied Polymer Sci

155

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A strong antimicrobial activity against Escherichia coli of Cu‐BTC metal‐organic frameworks immobilized over cellulosic fibers is hereby reported. The in situ synthesis of Cu‐BTC metal‐organic frameworks, aka MOF‐199 or HKUST‐1, onto cellulosic substrates was carried out by exposing carboxymethylated cellulosic substrates to Cu(OAC)2, 1,3,5‐benzenetricarboxylic acid and triethylamine solutions following a very specific order. Using an in vitro model, in accordance to ASTM E2149‐13a, we observed that the cellulose‐MOF system was able to completely eliminate the growth of E. coli on agar plates and liquid cultures. The antibacterial activity of the comprising components of MOF‐199 and the cellulosic substrate was also evaluated and determined to be negligible. Since the method used to synthesize MOF‐199 crystals provides a strong bond between the crystals and the cellulosic substrates, the crystals not detach from the anionic cellulosic fibers allowing the modified textile to be washed and reused hence opening a new avenue to fabricate antibacterial clinical fabrics. © 2014 Wiley Periodicals, Inc. J. Appl. Polym. Sci. 2014, 131, 40815.

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Section: Methodsmentioning

confidence: 99%

Antibacterial activity against Escherichia coli of Cu‐BTC (MOF‐199) metal‐organic framework immobilized onto cellulosic fibers

Rodríguez

Hinestroza

Ochoa‐Puentes

et al. 2014

J of Applied Polymer Sci

155

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“…The pma1 (MSMEG 3926) gene was amplified by PCR from M. smegmatis mc 2 155 (Snapper et al 1990) genomic DNA using the primer pairs pma1 pMV dir/pma1 pMV rev, which introduced PstI and HindIII restriction sites at the 5íand 3íend of the gene, respectively. The obtained amplimer was cloned into the pGEM-T easy vector (Promega Corporation, Madison, WI, USA) to generate the pCAT1 plasmid (Table S1).…”

Section: Cloning and Overexpression Of M Smegmatis Mc 2 155 Pma1mentioning

confidence: 99%

“…The enzymatic reactions were supplemented with Brij-58 to ensure that the majority of vesicles were right-side out (Santos et al 2012). This allows the P-type ATPases to be exposed to the reaction media and adequately stimulated by both Mg 2+ (cofactor) and the specific ions tested.…”

Section: Smegmatis Pma1 Gene Transcription Is Induced By Na + K mentioning

confidence: 99%

Pma1 is an alkali/alkaline earth metal cation ATPase that preferentially transports Na+ and K+ across the Mycobacterium smegmatis plasma membrane

Ayala‐Torres

Novoa‐Aponte

Soto

2015

Microbiological Research

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Mycobacterium smegmatis Pma1 is the orthologue of M. tuberculosis P-type ATPase cation transporter CtpF, which is activated under stress conditions, such as hypoxia, starvation and response to antituberculous and toxic substances. The function of Pma1 in the mycobacterial processes across the plasma membrane has not been characterised. In this work, bioinformatic analyses revealed that Pma1 likely contains potential sites for, Na(+), K(+) and Ca(2+) binding and transport. Accordingly, RT-qPCR experiments showed that M. smegmatis pma1 transcription is stimulated by sub-lethal doses of Na(+), K(+) and Ca(2+); in addition, the ATPase activity of plasma membrane vesicles in recombinant Pma1-expressing M. smegmatis cells is stimulated by treatment with these cations. In contrast, M. smegmatis cells homologously expressing Pma1 displayed tolerance to high doses of Na(+) and K(+) but not to Ca(2+) ions. Consistently, the recombinant protein Km embedded in plasma membrane demonstrated that Ca(2+) has more affinity for Pma1 than Na(+) and K(+) ions; furthermore, the estimation of Vmax/Km suggests that Na(+) and K(+) ions are more efficiently translocated than Ca(2+). Thus, these results strongly suggest that Pma1 is a promiscuous alkali/alkaline earth cation ATPase that preferentially transports Na(+) and/or K(+) across the mycobacterial plasma membrane.

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“…A comparison of the numerous studies of the activity of these peptides against M tuberculosis reveals that lariatin A and nisin A are more active than mCRAMP and LL‐37 . Similarly, lacticin 3147 and nisin A are more active than MIAP against M tuberculosis H37Ra …”

Section: Quest For Novel Drugs: Proteins and Peptidesmentioning

confidence: 99%

“…94,97,123,130 Similarly, lacticin 3147 and nisin A are more active than MIAP against M tuberculosis H37Ra. 127,154 However, maintaining the required level of nisin A in human blood to inhibit mycobacteria is challenging because of the peptide's remark- inhibition of M bovis BCG (an attenuated strain of M bovis used as a vaccine) than Ci-MAM-A24 and LL-37. 100,146,156 In contrast, the class II bacteriocin E50-52 has been shown to possess greater activity against M tuberculosis H37Rv than ecumicin, lassomycin, and lipid II-binding antibiotic teixobactin (Table 4).…”

Section: Natural Peptides Without Disulfide Bondsmentioning

confidence: 99%

A review on anti‐tuberculosis peptides: Impact of peptide structure on anti‐tuberculosis activity

Yathursan

Wiles

Read

et al. 2019

Journal of Peptide Science

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Antibiotic resistance is a major public health problem globally. Particularly concerning amongst drug‐resistant human pathogens is Mycobacterium tuberculosis that causes the deadly infectious tuberculosis (TB) disease. Significant issues associated with current treatment options for drug‐resistant TB and the high rate of mortality from the disease makes the development of novel treatment options against this pathogen an urgent need. Antimicrobial peptides are part of innate immunity in all forms of life and could provide a potential solution against drug‐resistant TB. This review is a critical analysis of antimicrobial peptides that are reported to be active against the M tuberculosis complex exclusively. However, activity on non‐TB strains such as Mycobacterium avium and Mycobacterium intracellulare, whenever available, have been included at appropriate sections for these anti‐TB peptides. Natural and synthetic antimicrobial peptides of diverse sequences, along with their chemical structures, are presented, discussed, and correlated to their observed antimycobacterial activities. Critical analyses of the structure allied to the anti‐mycobacterial activity have allowed us to draw important conclusions and ideas for research and development on these promising molecules to realise their full potential. Even though the review is focussed on peptides, we have briefly summarised the structures and potency of the various small molecule drugs that are available and under development, for TB treatment.

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Effect of antimicrobial peptides on ATPase activity and proton pumping in plasma membrane vesicles obtained from mycobacteria

Cited by 38 publications

References 57 publications

Antibacterial activity against Escherichia coli of Cu‐BTC (MOF‐199) metal‐organic framework immobilized onto cellulosic fibers

Antibacterial activity against Escherichia coli of Cu‐BTC (MOF‐199) metal‐organic framework immobilized onto cellulosic fibers

Pma1 is an alkali/alkaline earth metal cation ATPase that preferentially transports Na+ and K+ across the Mycobacterium smegmatis plasma membrane

A review on anti‐tuberculosis peptides: Impact of peptide structure on anti‐tuberculosis activity

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