Role of Sphingomyelinase in Infectious Diseases Caused by Bacillus cereus

Oda, Masataka; Hashimoto, Manabu; Takahashi, Masaya; Ohmae, Yuka; Seike, Soshi; Kato, Ryoko; Fujita, Aoi; Tsuge, Hideaki; Nagahama, Masahiro; Ochi, Sadayuki; Sasahara, Teppei; Hayashi, Shunji; Hirai, Yoshikazu; Sakùrai, Jun

doi:10.1371/journal.pone.0038054

Cited by 57 publications

(67 citation statements)

References 44 publications

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“…cereus is an opportunistic pathogen that causes endophthalmitis, pneumonia, and septicemia, as well as food poisoning (33). B. cereus SMase C induces colon epithelial cell death, kills silkworms, and contributes to the virulence of B. cereus in a Galleria mellonella larval infection model (34,35).…”

Section: Sphingomyelinase Csmentioning

confidence: 99%

Bacterial Sphingomyelinases and Phospholipases as Virulence Factors

Flores-Dı́az

Monturiol-Gross

Naylor

et al. 2016

Microbiol Mol Biol Rev

164

143

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SUMMARYBacterial sphingomyelinases and phospholipases are a heterogeneous group of esterases which are usually surface associated or secreted by a wide variety of Gram-positive and Gram-negative bacteria. These enzymes hydrolyze sphingomyelin and glycerophospholipids, respectively, generating products identical to the ones produced by eukaryotic enzymes which play crucial roles in distinct physiological processes, including membrane dynamics, cellular signaling, migration, growth, and death. Several bacterial sphingomyelinases and phospholipases are essential for virulence of extracellular, facultative, or obligate intracellular pathogens, as these enzymes contribute to phagosomal escape or phagosomal maturation avoidance, favoring tissue colonization, infection establishment and progression, or immune response evasion. This work presents a classification proposal for bacterial sphingomyelinases and phospholipases that considers not only their enzymatic activities but also their structural aspects. An overview of the main physiopathological activities is provided for each enzyme type, as are examples in which inactivation of a sphingomyelinase- or a phospholipase-encoding gene impairs the virulence of a pathogen. The identification of sphingomyelinases and phospholipases important for bacterial pathogenesis and the development of inhibitors for these enzymes could generate candidate vaccines and therapeutic agents, which will diminish the impacts of the associated human and animal diseases.

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Section: Sphingomyelinase Csmentioning

confidence: 99%

Bacterial Sphingomyelinases and Phospholipases as Virulence Factors

Flores-Dı́az

Monturiol-Gross

Naylor

et al. 2016

Microbiol Mol Biol Rev

164

143

View full text Add to dashboard Cite

show abstract

“…SMases C were also shown to play an important role in bacterial virulence, e.g. for Bacillus cereus (Oda et al, 2014(Oda et al, , 2012, Staphylococcus aureus (Hayashida et al, 2009;Huseby et al, 2010;Katayama et al, 2013) or Listeria ivanovii (Gonzalez-Zorn et al, 1999). The SMase C inhibitor SMY-540 exhibits a strong inhibitory effect against B. cereus and significantly reduces lethality of B. cereusinfected mice (Oda et al, 2014).…”

Section: Phospholipases As Targets For Chemotherapeuticsmentioning

confidence: 99%

Phospholipases during membrane dynamics in malaria parasites

Flammersfeld

Lang

Flieger

et al. 2018

International Journal of Medical Microbiology

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A B S T R A C TPlasmodium parasites, the causative agents of malaria, display a well-regulated lipid metabolism required to ensure their survival in the human host as well as in the mosquito vector. The fine-tuning of lipid metabolic pathways is particularly important for the parasites during the rapid erythrocytic infection cycles, and thus enzymes involved in lipid metabolic processes represent prime targets for malaria chemotherapeutics. While plasmodial enzymes involved in lipid synthesis and acquisition have been studied in the past, to date not much is known about the roles of phospholipases for proliferation and transmission of the malaria parasite. These phospholipid-hydrolyzing esterases are crucial for membrane dynamics during host cell infection and egress by the parasite as well as for replication and cell signaling, and thus they are considered important virulence factors. In this review, we provide a comprehensive bioinformatic analysis of plasmodial phospholipases identified to date. We further summarize previous findings on the lipid metabolism of Plasmodium, highlight the roles of phospholipases during parasite life-cycle progression, and discuss the plasmodial phospholipases as potential targets for malaria therapy.

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“…We reported that administration of anti-Bc-SMase antibody and immunization against Bc-SMase prevented death caused by the clinical isolate (JMU-06B-35) which is the Bc-SMase high expression strain 1 . The administration of B. cereus (JMU-06B-35) results in the death of mice within 10 h. To investigate the therapeutic potential of SMY-540 against B. cereus infection, we tested the effect of SMY-540 on the mortality rate of mice that had been administered a B. cereus (JMU-06B-35).…”

Section: Docking Simulation Analysis Of Bc-smase and Smy-540mentioning

confidence: 99%

“…The hydrolysis of SM to form ceramide in the membrane of macrophages treated with Bc-SMase causes a decrease in membrane fluidity and interferes with phagocytosis 1 . Bc-SMase also engages in hemolytic activity 2,3 .…”

Section: Introductionmentioning

confidence: 99%

“…In addition, Bc-SMase belongs to a family of Mg 2þ -dependent neutral SMase that includes SMase produced by Staphylococcus aureus, and Listeria ivanovii 8 . Recently, we determined that Bc-SMase plays a crucial role in bacterial evasion of the immune response during the early stages of infections 1 . In addition, Tajima et al 9 reported that sphingomyelinase from Staphylococcus aureus suppresses TNFa-induced IL-8 synthesis in endothelial cells and the transmigration of neutrophils.…”

Section: Introductionmentioning

confidence: 99%

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