A fowlicidin-1 analog protects mice from lethal infections induced by methicillin-resistant Staphylococcus aureus

Bommineni, Yugendar R.; Achanta, Mallika; Alexander, Jason; Sunkara, Lakshmi T.; Ritchey, Jerry W.; Zhang, Guolong

doi:10.1016/j.peptides.2010.03.037

Cited by 33 publications

(18 citation statements)

References 25 publications

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“…To compare the relative HDP-inducing efficacy of saturated free fatty acids in pigs, IPEC-J2 cells were treated first with a broad range of doses of different fatty acids with the chain length varying from C1 to C18 for 24 h, and the cytotoxicity was examined as we previously described [35]–[37]. Generally, fatty acids showed an enhanced toxicity as the aliphatic chain length increased (data not shown).…”

Section: Resultsmentioning

confidence: 97%

Induction of Porcine Host Defense Peptide Gene Expression by Short-Chain Fatty Acids and Their Analogs

et al. 2013

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Dietary modulation of the synthesis of endogenous host defense peptides (HDPs) represents a novel antimicrobial approach for disease control and prevention, particularly against antibiotic-resistant infections. However, HDP regulation by dietary compounds such as butyrate is species-dependent. To examine whether butyrate could induce HDP expression in pigs, we evaluated the expressions of a panel of porcine HDPs in IPEC-J2 intestinal epithelial cells, 3D4/31 macrophages, and primary monocytes in response to sodium butyrate treatment by real-time PCR. We revealed that butyrate is a potent inducer of multiple, but not all, HDP genes. Porcine β-defensin 2 (pBD2), pBD3, epididymis protein 2 splicing variant C (pEP2C), and protegrins were induced markedly in response to butyrate, whereas pBD1 expression remained largely unaltered in any cell type. Additionally, a comparison of the HDP-inducing efficacy among saturated free fatty acids of different aliphatic chain lengths revealed that fatty acids containing 3–8 carbons showed an obvious induction of HDP expression in IPEC-J2 cells, with butyrate being the most potent and long-chain fatty acids having only a marginal effect. We further investigated a panel of butyrate analogs for their efficacy in HDP induction, and found glyceryl tributyrate, benzyl butyrate, and 4-phenylbutyrate to be comparable with butyrate. Identification of butyrate and several analogs with a strong capacity to induce HDP gene expression in pigs provides attractive candidates for further evaluation of their potential as novel alternatives to antibiotics in augmenting innate immunity and disease resistance of pigs.

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Section: Resultsmentioning

confidence: 97%

Induction of Porcine Host Defense Peptide Gene Expression by Short-Chain Fatty Acids and Their Analogs

et al. 2013

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“…Since cathelicidins have membrane-perturbing properties which might affect the host’s cell membrane153132333435, first the possible cytotoxicity of the cathelicidins to RAW264.7 cells was assessed. No or very limited cytotoxicity was observed for most cathelicidins.…”

Section: Resultsmentioning

confidence: 99%

“…In addition, cathelicidins have been shown to have therapeutic potential. Overexpression of cathelicidin in a lung xenograft model has been shown to promote P. aeruginosa and S. aureus killing12, while exogenous cathelicidin treatment has been successfully used to inhibit M. haemolytica, E. coli and S. aureus infections131415.…”

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confidence: 99%

Interspecies cathelicidin comparison reveals divergence in antimicrobial activity, TLR modulation, chemokine induction and regulation of phagocytosis

Coorens

Scheenstra

Veldhuizen

et al. 2017

Sci Rep

101

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Cathelicidins are short cationic peptides initially described as antimicrobial peptides, which can also modulate the immune system. Because most findings have been described in the context of human LL-37 or murine CRAMP, or have been investigated under varying conditions, it is unclear which functions are cathelicidin specific and which functions are general cathelicidin properties. This study compares 12 cathelicidins from 6 species under standardized conditions to better understand the conservation of cathelicidin functions. Most tested cathelicidins had strong antimicrobial activity against E. coli and/or MRSA. Interestingly, while more physiological culture conditions limit the antimicrobial activity of almost all cathelicidins against E. coli, activity against MRSA is enhanced. Seven out of 12 cathelicidins were able to neutralize LPS and another 7 cathelicidins were able to neutralize LTA; however, there was no correlation found with LPS neutralization. In contrast, only 4 cathelicidins enhanced DNA-induced TLR9 activation. In conclusion, these results provide new insight in the functional differences of cathelicidins both within and between species. In addition, these results underline the importance not to generalize cathelicidin functions and indicates that caution should be taken in extrapolating results from LL-37- or CRAMP-related studies to other animal settings.

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“…According to the APD [9], more than a dozen of peptides have been expressed in plants to reduce or avoid infection. In addition, lactoferricin, distinctin, ranalexin, halocidin, polybia-MPI, chicken cathelicidin 1 (fowlicidin-1), bacterial mutacin B-Ny266, and bacterial ABP-118 have been tested in mice models [73][74][75][76][77][78][79][80]. Other engineered peptides or AMP mimics that have been evaluated in animal models include D, L-peptides, WLBU2, Pro-rich A3-APO, and acyl-lysyl oligomers [81][82][83][84].…”

Section: Therapeutic Potentials Of Ampsmentioning

confidence: 99%

“…Some of the post-translational strategies, such as C-terminal amidation, cyclization, D-amino acid incorporation, and halogenation, have been adopted in laboratories to enhance peptide stability to proteases. As a consequence, several engineered peptides have been demonstrated to be able to keep animal healthy [73][74][75][76][77][78][79][80][81][82][83][84].…”

Section: Concluding Remarks and Future Directionsmentioning

confidence: 99%

Post-Translational Modifications of Natural Antimicrobial Peptides and Strategies for Peptide Engineering

Wang¹

2011

CBIOT

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Natural antimicrobial peptides (AMPs) are gene-coded defense molecules discovered in all the three life domains: Eubacteria, Archaea, and Eukarya. The latter covers protists, fungi, plants, and animals. It is now recognized that amino acid composition, peptide sequence, and posttranslational modifications determine to a large extent the structure and function of AMPs. This article systematically describes post-translational modifications of natural AMPs annotated in the antimicrobial peptide database (http://aps.unmc.edu/AP). Currently, 1147 out of 1755 AMPs in the database are modified and classified into more than 17 types. Through chemical modifications, the peptides fold into a variety of structural scaffolds that target bacterial surfaces or molecules within cells. Chemical modifications also confer desired functions to a particular peptide. Meanwhile, these modifications modulate other peptide properties such as stability. Elucidation of the relationship between AMP property and chemical modification inspires peptide engineering. Depending on the objective of our design, peptides may be modified in various ways so that the desired features can be enhanced whereas unwanted properties can be minimized. Therefore, peptide design plays an essential role in developing natural AMPs into a new generation of therapeutic molecules.

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A fowlicidin-1 analog protects mice from lethal infections induced by methicillin-resistant Staphylococcus aureus

Cited by 33 publications

References 25 publications

Induction of Porcine Host Defense Peptide Gene Expression by Short-Chain Fatty Acids and Their Analogs

Induction of Porcine Host Defense Peptide Gene Expression by Short-Chain Fatty Acids and Their Analogs

Interspecies cathelicidin comparison reveals divergence in antimicrobial activity, TLR modulation, chemokine induction and regulation of phagocytosis

Post-Translational Modifications of Natural Antimicrobial Peptides and Strategies for Peptide Engineering

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