2006
DOI: 10.1128/jb.00787-06
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The Cytotoxic Fimbrial Structural Subunit of Xenorhabdus nematophila Is a Pore-Forming Toxin

Abstract: We have purified a fimbrial shaft protein (MrxA) of Xenorhabdus nematophila. The soluble monomeric protein lysed larval hemocytes of Helicoverpa armigera. Osmotic protection of the cells with polyethylene glycol suggested that the 17-kDa MrxA subunit makes pores in the target cell membrane. The internal diameter of the pores was estimated to be >2.9 nm. Electron microscopy confirmed the formation of pores by the fimbrial subunit. MrxA protein oligomerized in the presence of liposomes. Electrophysiological stud… Show more

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Cited by 24 publications
(18 citation statements)
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“…The ⌬cpxR1 mutant strain has altered production of several exoenzymes with known or suspected roles in X. nematophila virulence for insects and bioconversion of the insect carcass, including increased hemolysin (8,74) and protease (9) secreted activities, as well as increased transcripts of genes encoding these activities (Table 3). Of particular note is the finding that the ⌬cpxR1 mutant exhibited an increase in expression of mrxA (Table 3) encoding a pilin subunit (32) with pore-forming toxin activity (3). MrxA is present in X. nematophila outer membrane vesicles (OMVs) that are toxic to insects.…”
Section: Role Of X Nematophila Cpxr In Host Interactionsmentioning
confidence: 99%
“…The ⌬cpxR1 mutant strain has altered production of several exoenzymes with known or suspected roles in X. nematophila virulence for insects and bioconversion of the insect carcass, including increased hemolysin (8,74) and protease (9) secreted activities, as well as increased transcripts of genes encoding these activities (Table 3). Of particular note is the finding that the ⌬cpxR1 mutant exhibited an increase in expression of mrxA (Table 3) encoding a pilin subunit (32) with pore-forming toxin activity (3). MrxA is present in X. nematophila outer membrane vesicles (OMVs) that are toxic to insects.…”
Section: Role Of X Nematophila Cpxr In Host Interactionsmentioning
confidence: 99%
“…Oral administration of purified Pit protein results in an inhibition of growth with the larvae of Spodoptera litura and H. armigera, but did not kill the insects; however the injectable activity of the toxin was much greater. In Xenorhabdus the type 1 fimbrial protein, MrxA, recently implicated in nematode colonisation was previously identified as a putative pore-forming toxin which targets hemocytes thus preventing phagocytosis [59,60]. The same group also identified an insecticidal pilin subunit associated with outer membrane vesicles (OMVs) which appear to bleb from X. nematophilus [123,124].…”
Section: A Host Of Other Insecticidal Toxinsmentioning
confidence: 99%
“…Three phenethylamide compounds, purified from the culture broth of X. nematophila have demonstrable cytotoxicity towards hemocytes and may induce apoptosis by activating cytochrome c-dependent caspase-3 [57,58]. In addition a type 1 fimbrial protein, MrxA, has been shown to be toxic to cultured hemocytes and is able to form pores in cell membranes [59,60]. Bacteria unable to produce this protein showed reduced hemocyte toxicity in the larval hemocoel during early stage of infection and delayed larval mortality [60].…”
Section: Evasion Of the Cellular Responsementioning
confidence: 99%
“…MrxA was shown to be associated with outer membrane vesicles (OMVs) that exhibited oral toxicity toward the lepidopteran Helicoverpa armigera (25). Purified MrxA exhibited cytotoxic properties and recombinant MrxA displayed oral toxicity and functioned as a pore-forming toxin on targeted insect hemocytes (5,26).…”
mentioning
confidence: 99%