Arginine Metabolism in Bacterial Pathogenesis and Cancer Therapy

Lifeng Xiong, Jade L L Teng, Michael G Botelho, Regina C Lo, Susanna K P Lau, Patrick C Y Woo, Lifeng Xiong, Jade L L Teng, Michael G Botelho, Regina C Lo, Susanna K P Lau, Patrick C Y Woo

Abstract

Antibacterial resistance to infectious diseases is a significant global concern for health care organizations; along with aging populations and increasing cancer rates, it represents a great burden for government healthcare systems. Therefore, the development of therapies against bacterial infection and cancer is an important strategy for healthcare research. Pathogenic bacteria and cancer have developed a broad range of sophisticated strategies to survive or propagate inside a host and cause infection or spread disease. Bacteria can employ their own metabolism pathways to obtain nutrients from the host cells in order to survive. Similarly, cancer cells can dysregulate normal human cell metabolic pathways so that they can grow and spread. One common feature of the adaption and disruption of metabolic pathways observed in bacterial and cancer cell growth is amino acid pathways; these have recently been targeted as a novel approach to manage bacterial infections and cancer therapy. In particular, arginine metabolism has been illustrated to be important not only for bacterial pathogenesis but also for cancer therapy. Therefore, greater insights into arginine metabolism of pathogenic bacteria and cancer cells would provide possible targets for controlling of bacterial infection and cancer treatment. This review will summarize the recent progress on the relationship of arginine metabolism with bacterial pathogenesis and cancer therapy, with a particular focus on arginase and arginine deiminase pathways of arginine catabolism.

Keywords: arginase; arginine deiminase; arginine metabolism; bacterial pathogenesis; cancer therapy.

Figures

Figure 1
Figure 1
Simplified model for bacterial arginine catabolism by arginase and ADI pathways. In bacteria, arginine could be catalyzed by the arginase pathway (in blue) and/or the ADI pathway (in light salmon). For the arginase pathway, arginine is converted into urea and ornithine, which is subsequently catalyzed into glutamate. The ADI pathway catabolizes arginine to ornithine with the byproducts of ammonia, CO2 and ATP. The produced ornithine could be transported outside and exchange one molecule of arginine in the cell by the arginine–ornithine antiporter (ArcD) located in the bacterial membrane. Arginine may also be transported by some unknown transporters, which are shown by the question mark. RocD: ornithine aminotransferase; RocF: arginase; RocA: Δ-pyrroline-5-carboxylate dehydrogenase; ArcC: carbamate kinase; ArcA: arginine deiminase; ArcB: ornithine carbamoyltransferase; Pi: inorganic phosphate.
Figure 2
Figure 2
Proposed model for intracellular killing of bacteria by phagocyte and bacterial defense strategies against phagocytosis. Bacteria could be engulfed by a phagocyte into the phagosome (1), followed by fusion with a lysozyme to form a phagolysosome (2), being killed by varied strategies like pH decrease, enzymes (solid blue oval) release (2a), and production of antimicrobial NO by iNOS (2b). We propose that the bacteria containing ADI pathway genes may employ this pathway to defend these killing strategies in the following ways: firstly, the production of ammonia could probably raise the cytoplasmic pH, thereby inhibiting the formation of phagolysosome (3); secondly, the ADI pathway competes with iNOS for the common substrate (arginine), thereby reducing NO production (4); thirdly, arginine depletion would also activate the autophagy and/or apoptosis pathways, like that in cancer cells (Figure 3), to induce programmed cell death and release bacteria (5).
Figure 3
Figure 3
Schematic representation of argininosuccinate synthetase (ASS)-negative cell death induced by arginine deprivation. In ASS-negative cells, arginine cannot synthesize so arginine depletion by ADI or arginase would induce a quick response of cell autophagy by the mammalian Target of Rapamycin (mTOR) or MEK-ERK pathway. Autophagy could recycle limited arginine and prevent apoptosis as a survival response in the short term. Instead, in long-term arginine deprivation, autophagy would contribute to caspase-independent (CASP-IND) cell death and caspase dependent (CASP-DEP) apoptosis could also happen. The dashed lines ( and ) means the reactions are dependent on the availability of enzymes (panel A) or the reactions have not yet confirmed by experiments (panel B). MEK: mitogen-activated protein kinase, also known as extracellular signal-regulated kinase kinase; ERK: extracellular signal-regulated kinase.

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