- Oral administration of Lactobacillus plantarum lysates attenuates the development of atopic dermatitis lesions in mouse models
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Hangeun Kim , Hye Rim Kim , Na-Ra Kim , Bong Jun Jeong , Jong Suk Lee , Soojin Jang , Dae Kyun Chung
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J. Microbiol. 2015;53(1):47-52. Published online December 4, 2014
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DOI: https://doi.org/10.1007/s12275-015-4483-z
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 Abstract
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Lactobacillus plantarum is a well-documented probiotic that
has been used in clinical trials for the regulation of the immune
system and treatment of gastrointestinal diseases. In
this study, we evaluated the effects of L. plantarum cell lysates
on the immune regulation through the in vitro and in vivo
studies. L. plantarum lysates were prepared by sonication
method
, and we observed that the repetition of disruption
step increased indicator components within the bacterial
lysates. Indicator components might affect TNF-α production.
L. plantarum lysates did not induce TNF-α production,
while LPS-induced TNF-α production was dramatically inhibited
in a sonication-dependent manner in THP-1 cells.
Oral administration of L. plantarum lysates effectively attenuated
the horny layer formation and decreased epidermal
thickening in NC/Nga mice skin. The damage to barrier function
after the 8 weeks oral administration was reduced by L.
plantarum lysates as compared to that in the atopic dermatitis
(AD) mice. Further study revealed that L. plantarum lysates
polarized Th1 response via induction of IL-12 and IFN-γ
production and inhibition of IL-4 and IgE production in
NC/Nga mice. Together, our results suggest that L. plantarum
lysates are remarkable material for host homeostasis and it
could be used for the treatment of inflammatory diseases.
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Citations
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- Biocatalytic Properties and Substrate-binding Ability of a Modular GH10 β-1,4-Xylanase from an Insect-symbiotic Bacterium, Streptomyces mexicanus HY-14
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Do Young Kim , Dong-Ha Shin , Sora Jung , Jong Suk Lee , Han-Young Cho , Kyung Sook Bae , Chang-Keun Sung , Young Ha Rhee , Kwang-Hee Son , Ho-Yong Park
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J. Microbiol. 2014;52(10):863-870. Published online October 1, 2014
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DOI: https://doi.org/10.1007/s12275-014-4390-8
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1,055
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18
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Abstract
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The gene (1350-bp) encoding a modular β-1,4-xylanase (XylU),
which consists of an N-terminal catalytic GH10 domain and
a C-terminal carbohydrate-binding module 2 (CBM 2), from
Streptomyces mexicanus HY-14 was cloned and functionally
characterized. The purified His-tagged recombinant enzyme
(rXylU, 44.0 kDa) was capable of efficiently hydrolyze diverse
xylosidic compounds, p-nitrophenyl-cellobioside, and pnitrophenyl-
xylopyranoside when incubated at pH 5.5 and
65°C. Especially, the specific activities (649.8 U/mg and 587.0
U/mg, respectively) of rXylU toward oat spelts xylan and
beechwood xylan were relatively higher than those (<500.0
U/mg) of many other GH10 homologs toward the same
substrates. The results of enzymatic degradation of birchwood
xylan and xylooligosaccharides (xylotriose to xylohexaose)
revealed that rXylU preferentially hydrolyzed the
substrates to xylobiose (>75%) as the primary degradation
product. Moreover, a small amount (4%<) of xylose was detected
as the degradation product of the evaluated xylosidic
substrates, indicating that rXylU was a peculiar GH10 β-1,4-
xylanase with substrate specificity, which was different from
its retaining homologs. A significant reduction of the binding
ability of rXylU caused by deletion of the C-terminal CBM
2 to various insoluble substrates strongly suggested that the
additional domain might considerably contribute to the
enzyme-substrate interaction.
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