Bacterial infections in humans and animals caused by multidrug-resistant (MDR) pathogens pose a serious threat to public health. New antibacterial targets are extremely urgent to solve the dilemma of cross-resistance. Phospholipids are critical components in bacterial envelopes and involve diverse crucial processes to maintain homeostasis and modulate metabolism. Targeting phospholipids and their synthesis pathways has been largely overlooked because conventional membrane-targeted substances are non-specific with cytotoxicity. In this review, we first introduce the structure and physiological function of phospholipids in bacteria. Subsequently, we describe the chemical diversity of novel ligands targeting phospholipids, structure-activity relationships (SAR), modes of action (MOA), and pharmacological effects. Finally, we prospect the advantage of bacterial phospholipids as promising antibacterial targets. In conclusion, these findings will shed light on discovering and developing new antibacterial drugs to combat MDR bacteria-associated infections.
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http://dx.doi.org/10.1016/j.plipres.2024.101307 | DOI Listing |
Curr Microbiol
December 2024
Yunnan Institute of Microbiology, School of Life Sciences, Yunnan University, Kunming, Yunnan, 650091, People's Republic of China.
A novel bacteria strain, designated YIM B02787, was isolated from rhizosphere soil of Ageratina adenophora, in Yunnan, southwest China. The strain was aerobic, Gram-stain-negative, rod-shaped and motile with one polar flagellum. Growth occurred at 4-45 °C (optimum, 20-30 °C) and pH 6.
View Article and Find Full Text PDFMethods Mol Biol
December 2024
Department of Biochemistry and Molecular Biology, The University of Texas Health Science Center, McGovern Medical School, Houston, TX, USA.
Phospholipid translocation occurs ubiquitously in biological membranes and primarily is protein catalyzed. Lipid flippases mediate the net translocation of specific phospholipids from one leaflet of a membrane to the other. In the inner (cytoplasmic) membrane (IM) of Gram-negative bacteria, lysophospholipid translocase (LplT) and cytosolic bifunctional acyl-acyl carrier protein (ACP) synthetase/2-acylglycerolphosphoethanolamine acyltransferase (Aas) form a glycerophospholipid regeneration system, which is capable of facilitating rapid retrograde translocation of lyso forms of phosphatidylethanolamine (PE), phosphatidylglycerol (PG), and cardiolipin (CL) but not exogenous (host-derived) phosphatidylcholine (PC) across the IM of Gram-negative diderm (two-membraned) bacteria in consequential order lyso-PE = lyso-PG > > lysophosphatidic acid (lyso-PA) >> lyso-PC.
View Article and Find Full Text PDFSci Adv
December 2024
Department of Chemistry, Gwangju Institute of Science and Technology, Gwangju 61005, Republic of Korea.
Phosphatidylserine synthase (PssA) is essential in the biosynthesis of phosphatidylethanolamine, a major phospholipid of bacterial membranes. A peripheral membrane protein PssA can associate with the cellular membrane in its active state or exist in the cytosol in an inactive form. The membrane-bound enzyme acts on cytidine diphosphate diacylglycerol (CDP-DG) to form cytidine monophosphate and a covalent intermediate, which is subsequently targeted by serine to produce phosphatidylserine.
View Article and Find Full Text PDFInt J Syst Evol Microbiol
December 2024
Department of Bio & Environmental Technology, College of Natural Science, Seoul Women's University, Seoul 01797, Republic of Korea.
Three Gram-negative, aerobic and non-motile bacterial strains, BT552, BT553 and KR1UV-12, were isolated from soil samples in Gwangju-si and Gangneung-si, the Republic of Korea. Phylogenetic analysis based on 16S rRNA gene sequence showed that strains BT552, BT553 and KR1UV-12 clustered to a distinct clade within the family (order , class ). The strains exhibited the highest genetic similarity with representatives of the genus ; moreover, strains BT552 and BT553 tightly clustered with DAPP-PG 224 (98.
View Article and Find Full Text PDFInt J Mol Sci
November 2024
Department of Physical Chemistry and Biophysics, Faculty of Pharmacy, Wroclaw Medical University, Borowska 211A, 50-556 Wrocław, Poland.
is one of the most common dermatological diseases and is strongly connected with the pathological growth of the . More than half of the cultures of this bacterium are resistant to antibiotics, resulting in the proposal of the use of antibacterial peptides as an alternative to traditional antibiotics. Ascorbic acid (AA) and its antioxidant properties may ally in acne therapy.
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