- Expansion of antibacterial spectrum of xanthorrhizol against Gram-negatives in combination with PMBN and food-grade antimicrobials
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Man Su Kim , Ha-Rim Kim , Haebom Kim , Soo-Keun Choi , Chang-Hwan Kim , Jae-Kwan Hwang , Seung-Hwan Park
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J. Microbiol. 2019;57(5):405-412. Published online February 22, 2019
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DOI: https://doi.org/10.1007/s12275-019-8511-2
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Xanthorrhizol (XTZ), isolated from Curcuma xanthorrhiza,
has potent antifungal and antibacterial activity. It shows
very strong activity against Gram-positive bacteria, such as
Streptococcus mutans and Staphylococcus aureus, but is generally
not active against Gram-negative bacteria. In this study,
we explored the possibility of using a combination strategy
for expanding the antimicrobial spectrum of XTZ against
Gram-negative bacteria. To take advantage of XTZ being a
food-grade material, 10 food-grade or generally recognized
as safe (GRAS) antimicrobial compounds with low toxicities
were selected for combination therapy. In addition, polymyxin
B nonapeptide (PMBN), which is less toxic than polymyxin
B, was also selected as an outer membrane permeabilizer.
The antibacterial activity of various double or triple
combinations with or without XTZ were assayed in vitro
against four Gram-negative bacterial species (Escherichia
coli, Salmonella enterica serovar Typhi, Salmonella enterica
serovar Typhimurium, and Vibrio cholerae), with synergistic
combinations exhibiting clear activity subjected to further
screening. The combinations with the greatest synergism
were XTZ + PMBN + nisin, XTZ + PMBN + carvacrol, and
XTZ + PMBN + thymol. These combinations also showed
potent antimicrobial activity against Shigella spp., Yersinia
enterocolitica, and Acinetobacter baumannii. In time-kill
assays, the three combinations achieved complete killing of
E. coli within 2 h, and S. Typhi and V. cholera within 15 min.
This is the first report on expanding the activity spectrum
of XTZ against Gram-negative bacteria through combination with PMBN and food-grade or GRAS substances, with
the resulting findings being particularly useful for increasing
the industrial and medical applications of XTZ.
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Citations
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- Nucleotide-Binding Oligomerization Domain 2 (Nod2) Is Dispensable for the Innate Immune Responses of Macrophages against Yersinia enterocolitica
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Yu-Jin Jeong , Chang-Hwan Kim , Eun-Jung Song , Min-Jung Kang , Jee-Cheon Kim , Sang-Muk Oh , Kyung-Bok Lee , Jong-Hwan Park
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J. Microbiol. 2012;50(3):489-495. Published online June 30, 2012
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DOI: https://doi.org/10.1007/s12275-012-1534-6
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Nucleotide-binding oligomerization domain 2 (Nod2) is a cytosolic sensor for muramyl dipeptide, a component of bacterial peptidoglycan. In this study, we have examined whether Nod2 mediates the immune response of macrophages against Yersinia enterocolitica. Bone-marrow-derived macrophages (BMDMs) were isolated from WT and Nod2-deficient mice and were infected with various strains of Y. enterocolitica. ELISA showed that the production of IL-6 and TNF-α in BMDMs infected with Y. enterocolitica was not affected by the Nod2 deficiency. iNOS mRNA expression was induced in both WT and Nod2-deficienct BMDMs in response to Y. enterocolitica, beginning 2 h after infection. Nitric oxide (NO) production by Y. enterocolitica did not differ between WT and Nod2-deficient BMDMs. Western blot analysis revealed that Y. enterocolitica induces activation of NF-κB, p38, and ERK MAPK through a Nod2-independent pathway. Neither LDH release by Y. enterocolitica nor the phagocytic activity of the macrophages was altered by Nod2 deficiency. An in vivo experiment showed that bacterial clearance ability and production of IL-6 and KC in serum were comparable in WT and Nod2-deficient mice infected with Y. enterocolitica. These findings suggest that Nod2 may not be critical for initiating the innate immune response of macrophages against Yersinia infection.
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