Infectious diseases pose a significant threat to both human and animal populations. Intracellular bacteria are a group of pathogens that invade and survive within the interior of eukaryotic cells, which in turn protect them from antibacterial drugs and the host immune system. Limited penetration of antibacterials into host cells results in insufficient bacterial clearance and treatment failure. Bacteriophages have, over the decades, been proved to play an important role in combating bacterial infections (phage therapy), making them an important alternative to classical antibiotic strategies today. Phages have been found to be effective at killing various species of extracellular bacteria, but little is still known about how phages control intracellular infections. With advances in phage genomics and mechanisms of delivery and cell uptake, the development of phage-based antibacterial strategies to address the treatment of intracellular bacteria has general potential. In this review, we present the current state of knowledge regarding the application of bacteriophages against intracellular bacteria. We cover phage deployment against the most common intracellular pathogens with special attention to therapeutic and preventive strategies.
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http://dx.doi.org/10.1080/1040841X.2021.1960481 | DOI Listing |
PLoS One
January 2025
Institute of Medical Microbiology and Hospital Hygiene, Heinrich Heine University Düsseldorf, Düsseldorf, Germany.
Guanylate binding proteins (GBPs) are large interferon-inducible GTPases, executing essential host defense activities against Toxoplasma gondii, an invasive intracellular apicomplexan protozoan parasite of global importance. T. gondii establishes a parasitophorous vacuole (PV) which shields the parasite from the host's intracellular defense mechanisms.
View Article and Find Full Text PDFProc Natl Acad Sci U S A
January 2025
Department of Chemical Engineering, Stanford University, Stanford, CA 94305.
The crowded bacterial cytoplasm is composed of biomolecules that span several orders of magnitude in size and electrical charge. This complexity has been proposed as the source of the rich spatial organization and apparent anomalous diffusion of intracellular components, although this has not been tested directly. Here, we use biplane microscopy to track the 3D motion of self-assembled bacterial genetically encoded multimeric nanoparticles (bGEMs) with tunable size (20 to 50 nm) and charge (-3,240 to +2,700 e) in live cells.
View Article and Find Full Text PDFJ Integr Plant Biol
January 2025
Key Laboratory of Photobiology, Institute of Botany, the Chinese Academy of Sciences, Beijing, 100093, China.
Plants, algae and photosynthetic bacteria convert light into chemical energy by means of photosynthesis, thus providing food and energy for most organisms on Earth. Photosynthetic pigments, including chlorophylls (Chls) and carotenoids, are essential components that absorb the light energy necessary to drive electron transport in photosynthesis. The biosynthesis of Chl shares several steps in common with the biosynthesis of other tetrapyrroles, including siroheme, heme and phycobilins.
View Article and Find Full Text PDFBiol Cell
January 2025
INBIOP (Instituto de Biociencias de la Patagonia), Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET), Facultad de Ciencias Naturales y Ciencias de la Salud, Universidad Nacional de la Patagonia San Juan Bosco, Comodoro Rivadavia, Chubut, Argentina.
Actinobacteria belonging to Mycobacterium and Rhodococcus genera are able to synthesize and intracellularly accumulate variable amounts of triacylglycerols (TAG) in the form of lipid droplets (LDs). The lipid storage capacity of LDs in cells is controlled by the balance between lipogenesis and lipolysis. The growth of LDs in bacterial cells may be directly promoted by TAG biosynthesis, whereas TAG degradation might result in the reduction of LD sizes and lipid storage capacity.
View Article and Find Full Text PDFPrep Biochem Biotechnol
January 2025
Department of Pharmaceutical Biotechnology, Faculty of Pharmacy, Tabriz University of Medical Sciences, Tabriz, Iran.
L-asparaginase (asparagine amidohydrolase) contributes to 40% of the total enzyme demands worldwide and is one-third of the global requirement as an anti-cancerous drug in treating acute lymphocytic leukemia (ALL), a type of leukemia. This protein breaks down L-asparagine into aspartic acid and ammonia those involved in ALL, rely on for growth and survival. Both non-recombinant and recombinant L-asparaginase can be produced by bacteria when a suitable substrate and method (solid-state fermentation (SSF) or submerged fermentation (SmF) which are techniques to grow microorganisms under controlled conditions), is provided.
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