Thanatin: An Emerging Host Defense Antimicrobial Peptide with Multiple Modes of Action

Dash, Rachita; Bhattacharjya, Surajit

doi:10.3390/ijms22041522

Cited by 56 publications

(37 citation statements)

References 73 publications

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“…In addition, Tur1A, an AMP found in dolphins, binds to ribosomes, and blocks the translation of mRNA into proteins [28]. Thanatin, an insect-derived AMP targets the bacterial LPS and induces the LPS-mediated aggregation [29]. Tridecaptin blocks ATP synthesis in bacteria and is active on MDR and colistin-resistant Enterobacterales [30].…”

Section: Inhibition Of Intracellular Functionsmentioning

confidence: 99%

Antimicrobial Peptides: A Potent Alternative to Antibiotics

et al. 2021

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Antimicrobial peptides constitute one of the most promising alternatives to antibiotics since they could be used to treat bacterial infections, especially those caused by multidrug-resistant pathogens. Many antimicrobial peptides, with various activity spectra and mechanisms of actions, have been described. This review focuses on their use against ESKAPE bacteria, especially in biofilm treatments, their synergistic activity, and their application as prophylactic agents. Limitations and challenges restricting therapeutic applications are highlighted, and solutions for each challenge are evaluated to analyze whether antimicrobial peptides could replace antibiotics in the near future.

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Section: Inhibition Of Intracellular Functionsmentioning

confidence: 99%

Antimicrobial Peptides: A Potent Alternative to Antibiotics

et al. 2021

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“…The number of amino acid residues within a single disulfide bond affects antibacterial activity ( Lee et al, 2002 ). Collectively, the C-terminal residues of thanatin are more critical for antimicrobial activity than the N-terminal residues ( Dash and Bhattacharjya, 2021 ). Despite studies on the structure and antimicrobial activity of thanatin, the precursor molecules of this peptide have not been identified.…”

Section: Discussionmentioning

confidence: 99%

Multiple Precursor Proteins of Thanatin Isoforms, an Antimicrobial Peptide Associated With the Gut Symbiont of Riptortus pedestris

2022

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Thanatin is an antimicrobial peptide (AMP) generated by insects for defense against bacterial infections. In the present study, we performed cDNA cloning of thanatin and found the presence of multiple precursor proteins from the bean bug, Riptortus pedestris. The cDNA sequences encoded 38 precursor proteins, generating 13 thanatin isoforms. In the phylogenetic analysis, thanatin isoforms were categorized into two groups based on the presence of the membrane attack complex/perforin (MACPF) domain. In insect-bacterial symbiosis, specific substances are produced by the immune system of the host insect and are known to modulate the symbiont’s population. Therefore, to determine the biological function of thanatin isoforms in symbiosis, the expression levels of three AMP genes were compared between aposymbiotic insects and symbiotic R. pedestris. The expression levels of the thanatin genes were significantly increased in the M4 crypt, a symbiotic organ, of symbiotic insects upon systemic bacterial injection. Further, synthetic thanatin isoforms exhibited antibacterial activity against gut-colonized Burkholderia symbionts rather than in vitro-cultured Burkholderia cells. Interestingly, the suppression of thanatin genes significantly increased the population of Burkholderia gut symbionts in the M4 crypt under systemic Escherichia coli K12 injection. Overgrown Burkholderia gut symbionts were observed in the hemolymph of host insects and exhibited insecticidal activity. Taken together, these results suggest that thanatin of R. pedestris is a host-derived symbiotic factor and an AMP that controls the population of gut-colonized Burkholderia symbionts.

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“…However, the mechanisms of inhibitory activities of thanatin against Gram-positive bacteria and fungi are not clearly elucidated. AMPs such as thanatin have revived the hope of developing effecting antimicrobial therapies, either alone or in combination with antibiotics, against extremely drug-resistant bacteria [ 183 ].…”

Section: Reduction Of Antimicrobial Permeability Into Bacterial Cellsmentioning

confidence: 99%

Bacterial Resistance to Antimicrobial Agents

et al. 2021

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Bacterial pathogens as causative agents of infection constitute an alarming concern in the public health sector. In particular, bacteria with resistance to multiple antimicrobial agents can confound chemotherapeutic efficacy towards infectious diseases. Multidrug-resistant bacteria harbor various molecular and cellular mechanisms for antimicrobial resistance. These antimicrobial resistance mechanisms include active antimicrobial efflux, reduced drug entry into cells of pathogens, enzymatic metabolism of antimicrobial agents to inactive products, biofilm formation, altered drug targets, and protection of antimicrobial targets. These microbial systems represent suitable focuses for investigation to establish the means for their circumvention and to reestablish therapeutic effectiveness. This review briefly summarizes the various antimicrobial resistance mechanisms that are harbored within infectious bacteria.

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Thanatin: An Emerging Host Defense Antimicrobial Peptide with Multiple Modes of Action

Cited by 56 publications

References 73 publications

Antimicrobial Peptides: A Potent Alternative to Antibiotics

Antimicrobial Peptides: A Potent Alternative to Antibiotics

Multiple Precursor Proteins of Thanatin Isoforms, an Antimicrobial Peptide Associated With the Gut Symbiont of Riptortus pedestris

Bacterial Resistance to Antimicrobial Agents

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