Glycan region of GPI anchored-protein is required for cytocidal oligomerization of an anticancer parasporin-2, Cry46Aa1 protein, from Bacillus thuringiensis strain A1547

Abe, Yoshiharu; Inoue, Hiroshi; Ashida, Hisashi; Maeda, Yusuke; Kinoshita, Taroh; Kitada, Sakae

doi:10.1016/j.jip.2016.11.008

Cited by 10 publications

(11 citation statements)

References 36 publications

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“…subsequently forms a membrane embedded oligomer that forms pore and induces permeability of the plasma membrane leading to cell death (Abe et al, 2017). Other PS proteins also kill cells by pore formation.…”

Section: Bacillus Thuringiensismentioning

confidence: 99%

“…Inhibit tumor growth, cell cycle arrest, apoptosis and metastasis arrest (Wu et al, 2017) Levan Increase oxidative stress and apoptosis (Queiroz et al, 2017) L-asparaginase Causes nutritional de ciencies and inhibit protein synthesis resulting in apoptosis (Shrivastava et al, 2016) Ieodoglucomide B Inhibit tumor cell growth (Tareq et al, 2013) Bacillistatins 1 and 2 Inhibit tumor cell growth (Pettit, Arce, Chapuis, & Macdonald, 2015) Mixirins A, B and C Inhibit tumor cell growth (Harris & Pierpoint, 2012) Parasporin 1 Activates apoptotic signaling pathway by binding with Beclin 1 receptor and increase Ca 2+ in ux (Katayama et al, 2007) Parasporin 2 Permeabilize plasma membrane through GPIanchored protein (Abe et al, 2017) Parasporin 3 Pore formation (Ito et al, 2004) Parasporin 4 Cholesterol independent pore formation (Yamashita et al, 2005) Parasporin 6 Swelling of cells and vacuoles formation…”

Section: Surfactinmentioning

confidence: 99%

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Bacillus spp.: Attractive Sources of Anti-cancer and Anti-proliferative Biomolecules

Ferdous¹,

Shishir²,

Khan³

et al. 2018

Microb. Bioacts.

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Cancer treatment remains as an expensive process due to the cost of sophisticated infrastructure development as well as its maintenance with skilled personnel. At the same time, the success rate is not very inspiring since non-specific target oriented medication could cause other health complexities leading to death. Research for alternative therapies aimed at minimizing the side effects of treatments and increasing the survival rates of patients includes routine explorations for anticancer agents from numerous sources (e.g. microbes, plants and nanoparticles). Anticancer activities of several bacterial components especially from Bacillus spp. were reported in many scientific reports. For economic production of these agents, potential strains from this genus could be feasible and sustainable for their long and successful utilization in industries. The review is therefore, focused on describing the available anticancer and anti-proliferative agents reported worldwide from Bacillus spp.

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Section: Bacillus Thuringiensismentioning

confidence: 99%

Section: Surfactinmentioning

confidence: 99%

Bacillus spp.: Attractive Sources of Anti-cancer and Anti-proliferative Biomolecules

Ferdous¹,

Shishir²,

Khan³

et al. 2018

Microb. Bioacts.

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“…Oligomerization has been studied in several wild type and mutant toxins such as Cry1Aa, Cry1Ab, Cry1Ac, Cry1Ca, Cry1Da, Cry1Ea, Cry1Fa, Cry2Ab, Cry3Aa, Cry3Ba, Cry3Ca, Cry4Ba, Cry11Aa and Cry46Aa1 [15,[17][18][19][20][21][22][23][24][25]. Oligomerization has also been detected in other Bt toxins such as Cyt [26] and Vip [27].…”

Section: Introductionmentioning

confidence: 99%

Study of the Bacillus thuringiensis Cry1Ia Protein Oligomerization Promoted by Midgut Brush Border Membrane Vesicles of Lepidopteran and Coleopteran Insects, or Cultured Insect Cells

Khorramnejad

Domínguez-Arrizabalaga

Caballero

et al. 2020

Toxins

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Bacillus thuringiensis (Bt) produces insecticidal proteins that are either secreted during the vegetative growth phase or accumulated in the crystal inclusions (Cry proteins) in the stationary phase. Cry1I proteins share the three domain (3D) structure typical of crystal proteins but are secreted to the media early in the stationary growth phase. In the generally accepted mode of action of 3D Cry proteins (sequential binding model), the formation of an oligomer (tetramer) has been described as a major step, necessary for pore formation and subsequent toxicity. To know if this could be extended to Cry1I proteins, the formation of Cry1Ia oligomers was studied by Western blot, after the incubation of trypsin activated Cry1Ia with insect brush border membrane vesicles (BBMV) or insect cultured cells, using Cry1Ab as control. Our results showed that Cry1Ia oligomers were observed only after incubation with susceptible coleopteran BBMV, but not following incubation with susceptible lepidopteran BBMV or non-susceptible Sf21 insect cells, while Cry1Ab oligomers were persistently detected after incubation with all insect tissues tested, regardless of its host susceptibility. The data suggested oligomerization may not necessarily be a requirement for the toxicity of Cry1I proteins.

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“…In 2009, Akiba et al [134] proposed that PS2 toxins were able to produce oligomers that induce membrane pores and cell death by bind to lipid rafts. In 2017, Abe et al reported that GPI was an essential co-receptor to PS2 parasporins toxic activity [135]. The action mechanism of PS2 family members is apparent by activating apoptosis, which is associated to an increase in the tumor suppressor gene PAR-4 expression and through inhibition of the PI3K/AKT pathway [136].…”

Section: Ps2 Familymentioning

confidence: 99%

The Cytocidal Spectrum of Bacillus thuringiensis Toxins: From Insects to Human Cancer Cells

Mendoza‐Almanza

Esparza-Ibarra

Ayala-Lujan

et al. 2020

Toxins

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Bacillus thuringiensis (Bt) is a ubiquitous bacterium in soils, insect cadavers, phylloplane, water, and stored grain, that produces several proteins, each one toxic to different biological targets such as insects, nematodes, mites, protozoa, and mammalian cells. Most Bt toxins identify their particular target through the recognition of specific cell membrane receptors. Cry proteins are the best-known toxins from Bt and a great amount of research has been published. Cry are cytotoxic to insect larvae that affect important crops recognizing specific cell membrane receptors such as cadherin, aminopeptidase-N, and alkaline phosphatase. Furthermore, some Cry toxins such as Cry4A, Cry4B, and Cry11A act synergistically with Cyt toxins against dipteran larvae vectors of human disease. Research developed with Cry proteins revealed that these toxins also could kill human cancer cells through the interaction with specific receptors. Parasporins are a small group of patented toxins that may or may not have insecticidal activity. These proteins could kill a wide variety of mammalian cancer cells by recognizing specific membrane receptors, just like Cry toxins do. Surface layer proteins (SLP), unlike the other proteins produced by Bt, are also produced by most bacteria and archaebacteria. It was recently demonstrated that SLP produced by Bt could interact with membrane receptors of insect and human cancer cells to kill them. Cyt toxins have a structure that is mostly unrelated to Cry toxins; thereby, other mechanisms of action have been reported to them. These toxins affect mainly mosquitoes that are vectors of human diseases like Anopheles spp (malaria), Aedes spp (dengue, zika, and chikungunya), and Culex spp (Nile fever and Rift Valley fever), respectively. In addition to the Cry, Cyt, and parasporins toxins produced during spore formation as inclusion bodies, Bt strains also produce Vip (Vegetative insecticidal toxins) and Sip (Secreted insecticidal proteins) toxins with insecticidal activity during their vegetative growth phase.

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Glycan region of GPI anchored-protein is required for cytocidal oligomerization of an anticancer parasporin-2, Cry46Aa1 protein, from Bacillus thuringiensis strain A1547

Cited by 10 publications

References 36 publications

Bacillus spp.: Attractive Sources of Anti-cancer and Anti-proliferative Biomolecules

Bacillus spp.: Attractive Sources of Anti-cancer and Anti-proliferative Biomolecules

Study of the Bacillus thuringiensis Cry1Ia Protein Oligomerization Promoted by Midgut Brush Border Membrane Vesicles of Lepidopteran and Coleopteran Insects, or Cultured Insect Cells

The Cytocidal Spectrum of Bacillus thuringiensis Toxins: From Insects to Human Cancer Cells

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