- Lactobacillus rhamnosus CCFM1107 treatment ameliorates alcohol-induced liver injury in a mouse model of chronic alcohol feeding
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Fengwei Tian , Feifei Chi , Gang Wang , Xiaoming Liu , Qiuxiang Zhang , Yongquan Chen , Hao Zhang , Wei Chen
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J. Microbiol. 2015;53(12):856-863. Published online December 2, 2015
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DOI: https://doi.org/10.1007/s12275-015-5239-5
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Abstract
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Lactobacillus rhamnosus CCFM1107 was screened for high
antioxidative activity from 55 lactobacilli. The present study
attempted to explore the protective properties of L. rhamnosus
CCFM1107 in alcoholic liver injury. A mouse model
was induced by orally feeding alcohol when simultaneously
treated with L. rhamnosus CCFM1107, the drug Hu-Gan-
Pian (HGP), L. rhamnosus GG (LGG), and L. plantarum
CCFM1112 for 3 months. Biochemical analysis was performed
for both serum and liver homogenate. Detailed intestinal flora
and histological analyses were also carried out. Our results
indicated that the administration of L. rhamnosus CCFM1107
significantly inhibited the increase in the levels of serum aminotransferase
and endotoxin, as well as the levels of triglyceride
(TG) and cholesterol (CHO) in the serum and in the
liver. Glutathione (GSH), glutathione peroxidase (GSH-Px)
and superoxide dismutase (SOD) were elevated while the levels
of malondialdehyde (MDA) were decreased. The enteric dysbiosis
caused by alcohol was restored by increasing the numbers
of both lactobacilli and bifidobacteria and decreasing
the numbers of both enterococci and enterobacter. Histological
analysis confirmed the protective effect of L. rhamnosus
CCFM1107. Compared with the other lactobacilli and to
the drug Hu-Gan-Pian, there is a high chance that L. rhamnosus
CCFM1107 provides protective effects on alcoholic
liver injury by reducing oxidative stress and restoring the
intestinal flora.
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- Defining the N-Linked Glycosylation Site of Hantaan Virus Envelope Glycoproteins Essential for Cell Fusion
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Feng Zheng , Lixian Ma , Lihua Shao , Gang Wang , Fengzhe Chen , Ying Zhang , Song Yang
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J. Microbiol. 2008;46(2):233-233.
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Abstract
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In the article by Zheng et al. that appears in the Journal of Microbiology 2007; 45, 41-47. Page 44, Figure 6(E) should appear as shown below.
- Defining the N-Linked Glycosylation Site of Hantaan Virus Envelope Glycoproteins Essential for Cell Fusion
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Feng Zheng , Lixian Ma , Lihua Shao , Gang Wang , Fengzhe Chen , Ying Zhang , Song Yang
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J. Microbiol. 2007;45(1):41-47.
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DOI: https://doi.org/2493 [pii]
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Abstract
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The Hantaan virus (HTNV) is an enveloped virus that is capable of inducing low pH-dependent cell fusion. We molecularly cloned the viral glycoprotein (GP) and nucleocapsid (NP) cDNA of HTNV and expressed them in Vero E6 cells under the control of a CMV promoter. The viral gene expression was assessed using an indirect immunofluorescence assay and immunoprecipitation. The transfected Vero E6 cells expressing GPs, but not those expressing NP, fused and formed a syncytium following exposure to a low pH. Monoclonal antibodies (MAbs) against envelope GPs inhibited cell fusion, whereas MAbs against NP did not. We also investigated the N-linked glycosylation of HTNV GPs and its role in cell fusion. The envelope GPs of HTNV are modified by N-linked glycosylation at five sites: four sites on G1 (N134, N235, N347, and N399) and one site on G2 (N928). Site-directed mutagenesis was used to construct eight GP gene mutants, including five single N-glycosylation site mutants and three double-site mutants, which were then expressed in Vero E6 cells. The oligosaccharide chain on residue N928 of G2 was found to be crucial for cell fusion after exposure to a low pH. These results suggest that G2 is likely to be the fusion protein of HTNV.
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