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- Structural Insights into the Lipopolysaccharide Transport (Lpt) System as a Novel Antibiotic Target.
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Yurim Yoon, Saemee Song
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J. Microbiol. 2024;62(4):261-275. Published online May 31, 2024
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DOI: https://doi.org/10.1007/s12275-024-00137-w
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Abstract
- Lipopolysaccharide (LPS) is a critical component of the extracellular leaflet within the bacterial outer membrane, forming an effective physical barrier against environmental threats in Gram-negative bacteria. After LPS is synthesized and matured in the bacterial cytoplasm and the inner membrane (IM), LPS is inserted into the outer membrane (OM) through the ATP-driven LPS transport (Lpt) pathway, which is an energy-intensive process. A trans-envelope complex that contains seven Lpt proteins (LptA-LptG) is crucial for extracting LPS from the IM and transporting it across the periplasm to the OM. The last step in LPS transport involves the mediation of the LptDE complex, facilitating the insertion of LPS into the outer leaflet of the OM. As the Lpt system plays an essential role in maintaining the impermeability of the OM via LPS decoration, the interactions between these interconnected subunits, which are meticulously regulated, may be potential targets for the development of new antibiotics to combat multidrug-resistant Gram-negative bacteria. In this review, we aimed to provide an overview of current research concerning the structural interactions within the Lpt system and their implications to clarify the function and regulation of LPS transport in the overall process of OM biogenesis.
Additionally, we explored studies on the development of therapeutic inhibitors of LPS transport, the factors that limit success, and future prospects.
Journal Articles
- [Protocol] Development of DNA aptamers specific for small therapeutic peptides using a modified SELEX method
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Jaemin Lee , Minkyung Ryu , Dayeong Bae , Hong-Man Kim , Seong-il Eyun , Jeehyeon Bae , Kangseok Lee
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J. Microbiol. 2022;60(7):659-667. Published online June 22, 2022
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DOI: https://doi.org/10.1007/s12275-022-2235-4
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Citations
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Abstract
- Aptamers are short single-stranded DNA or RNA oligonucleotides
capable of binding with high affinity and specificity
to target molecules. Because of their durability and ease of synthesis,
aptamers are used in a wide range of biomedical fields,
including the diagnosis of diseases and targeted delivery of
therapeutic agents. The aptamers were selected using a process
called systematic evolution of ligands by exponential enrichment
(SELEX), which has been improved for various research
purposes since its development in 1990. In this protocol,
we describe a modified SELEX method that rapidly produces
high aptamer screening yields using two types of magnetic
beads. Using this method, we isolated an aptamer that
specifically binds to an antimicrobial peptide. We suggest that
by conjugating a small therapeutic-specific aptamer to a gold
nanoparticle-based delivery system, which enhances the stability
and intracellular delivery of peptides, aptamers selected
by our method can be used for the development of therapeutic
agents utilizing small therapeutic peptides.
- Function of Rhs proteins in porcine extraintestinal pathogenic Escherichia coli PCN033
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Wenjia Lu , Jia Tan , Hao Lu , Gaoyan Wang , Wenqi Dong , Chenchen Wang , Xiaodan Li , Chen Tan
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J. Microbiol. 2021;59(9):854-860. Published online August 12, 2021
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DOI: https://doi.org/10.1007/s12275-021-1189-2
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Abstract
- Extraintestinal pathogenic Escherichia coli (ExPEC) is an important
zoonotic pathogen that places severe burdens on public
health and animal husbandry. There are many pathogenic
factors in E. coli. The type VI secretion system (T6SS) is a
nano-microbial weapon that can assemble quickly and inject
toxic effectors into recipient cells when danger is encountered.
T6SSs are encoded in the genomes of approximately
25% of sequenced Gram-negative bacteria. When these bacteria
come into contact with eukaryotic cells or prokaryotic
microbes, the T6SS assembles and secretes associated effectors.
In the porcine ExPEC strain PCN033, we identified four
classic rearrangement hotspot (Rhs) genes. We determined
the functions of the four Rhs proteins through mutant construction
and protein expression. Animal infection experiments
showed that the Δrhs-1CT, Δrhs-2CT, Δrhs-3CT, and
Δrhs-4CT caused a significant decrease in the multiplication
ability of PCN033 in vivo. Cell infection experiments showed
that the Rhs protein is involved in anti-phagocytosis activities
and bacterial adhesion and invasion abilities. The results
of this study demonstrated that rhs1, rhs3, and rh4 plays an
important role in the interaction between PCN033 and host
cell. Rhs2 has contribution to cell and mice infection. This
study helps to elucidate the pathogenic mechanism governing
PCN033 and may help to establish a foundation for further
research seeking to identify potential T6SS effectors.
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