Journal Article
- Comparison of anti-influenza virus activity and pharmacokinetics of oseltamivir free base and oseltamivir phosphate
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Jin Soo Shin , Keun Bon Ku , Yejin Jang , Yi-Seul Yoon , Daeho Shin , Oh Seung Kwon , Yun Young Go , Seong Soon Kim , Myoung Ae Bae , Meehyein Kim
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J. Microbiol. 2017;55(12):979-983. Published online December 7, 2017
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DOI: https://doi.org/10.1007/s12275-017-7371-x
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Abstract
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Influenza viruses are major human respiratory pathogens that
cause high morbidity and mortality worldwide. Currently,
prophylactic vaccines and therapeutic antiviral agents are used
to prevent and control influenza virus infection. Oseltamivir
free base (OSV-FB), a modified generic antiviral drug of
Tamiflu (oseltamivir phosphate, OSV-P), was launched in
the Republic of Korea last year. Here, we examine the bioequivalence
of these two compounds by assessing their antiviral
efficacy in infected cells and in a mouse model. It was
observed that both antivirals showed comparable efficacy
against 11 different influenza A and B viruses in vitro. Moreover,
in mice infected with influenza A virus (mouse-adapted
A/Puerto Rico/8/34), they showed a dose-dependent therapeutic
activity and alleviated infection-mediated reductions
in body weight, leading to significantly better survival. There
was histopathological disappearance of virus-induced inflammatory
cell infiltration of the lung after oral treatment with
either antiviral agent (at 10 mg/kg). Pharmacokinetic analysis
also exhibited similar plasma concentrations of the active
drug, oseltamivir carboxylate, metabolised from both OSVB
and OSV-P. This is the first report showing bioequivalence
of OSV-FB to its phosphate salt form in the mouse system.
The free base drug has some beneficial points including simple
drug formulation process and reduced risk of undesirable
cation-phosphate precipitation within solution. The long term
stability of OSV-FB requires further monitoring when it is
provided as a national stock in readiness for an influenza
pandemic.
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Jing Yu, Jian-Ming Liu, Hui-Yi Chen, Wei-Ming Xiong
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Frontiers in Microbiology.2018;[Epub] CrossRef
Research Support, Non-U.S. Gov'ts
- Relationships between the use of Embden Meyerhof pathway (EMP) or Phosphoketolase pathway (PKP) and lactate production capabilities of diverse Lactobacillus reuteri strains
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Grégoire Burgé , Claire Saulou-Bérion , Marwen Moussa , Florent Allais , Violaine Athes , Henry-Eric Spinnler
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J. Microbiol. 2015;53(10):702-710. Published online October 2, 2015
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DOI: https://doi.org/10.1007/s12275-015-5056-x
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Abstract
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The aims of this study is to compare the growth and glucose
metabolism of three Lactobacillus reuteri strains (i.e.
DSM 20016, DSM 17938, and ATCC 53608) which are lactic
acid bacteria of interest used for diverse applications such
as probiotics implying the production of biomass, or for the
production of valuable chemicals (3-hydroxypropionaldehyde,
3-hydroxypropionic acid, 1,3-propanediol). However, the
physiological diversity inside the species, even for basic metabolisms,
like its capacity of acidification or glucose metabolism,
has not been studied yet. In the present work, the
growth and metabolism of three strains representative of
the species diversity have been studied in batch mode. The
strains were compared through characterization of growth
kinetics and evaluation of acidification kinetics, substrate consumption
and product formation. The results showed significant
differences between the three strains which may be
explained, at least in part, by variations in the distribution
of carbon source between two glycolytic pathways during the
bacterial growth: the phosphoketolase or heterolactic pathway
(PKP) and the Embden-Meyerhof pathway (EMP). It was
also shown that, in the context of obtaining a large amount
of biomass, DSM 20016 and DSM 17938 strains were the
most effective in terms of growth kinetics. The DSM 17938
strain, which shows the more significant metabolic shift from
EMP to PKP when the pH decreases, is more effective for
lactate production.
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- Kinetic Evaluation of Products Inhibition to Succinic Acid Producers Escherichia coli NZN111, AFP111, BL21, and Actinobacillus succinogenes 130ZT
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Qiang Li , Dan Wang , Yong Wu , Maohua Yang , Wangliang Li , Jianmin Xing , Zhiguo Su
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J. Microbiol. 2010;48(3):290-296. Published online June 23, 2010
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DOI: https://doi.org/10.1007/s12275-010-9262-2
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64
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Abstract
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Succinic acid is one of the platform compounds and its production via natural feedstocks has drawn worldwide concerns. To evaluate the inhibitory effects of fermentation products on the growth of Actinobacillus succinogenes 130ZT and Escherichia coli NZN111, AFP111, BL21, fermentations with addition of individual products in medium were carried out. The cell growth was inhibited when the concentrations of formate, acetate, lactate, and succinate were at range of 8.8-17.6 g/L, 10-40 g/L, 9-18 g/L, and 10-80 g/L, respectively. For these two species of bacteria, E. coli was more resistant to acid products than A. succinogenes,
while both endured succinate rather than by-products. As a result of end product inhibition, succinate production yield by A. succinogenes decreased from 1.11 to 0.49 g/g glucose. Logistic and Monod mathematical models were presented to simulate the inhibition kinetics. The Logistic model was found more suitable for
describing the overall synergistic inhibitory effects.
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- Physiological characterization of kinetics and action mechanism of vibrio hemolysin
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Choe, Young Chool , Jeong, Ga Jin
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J. Microbiol. 1995;33(4):289-294.
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Abstract
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The action mechanism of hemolysin rendering virulency of Vibrio anguilarum has not clarified as yet, even though there were several possible factors explained. We have studied hemolytic kinetics performed by hemolysin from V. anguillarum strain V7 as well as binding of hemolysin to RBC membrane. Maximal rate of hemolysis and duration of lag phase were directly and inversly correlated to the concentration of hemolysin used. Hemolysin molecules are known to bind consumptively with proper diameter, while other protectants with smaller diameter could not. In conclusion, hemolysin should bind irreversibly to RBC membrane exert hemolysis distorting osmotic pressure. The binding could be hindered by spatial structure of the RBC surfacem which might be caused by sialic acid.