The type II signal peptidase of Legionella pneumophila

Buck, Emmy De; Meyen, Eef; Maes, Liesbeth; Vranckx, Leen; Mellaert, Lieve Van; Anné, Jozef; Lammertyn, Elke

doi:10.1016/j.resmic.2006.06.003

Cited by 9 publications

(4 citation statements)

References 24 publications

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“…In addition, the biosynthetic pathway of LimB might also provide an alternative strategy for therapeutic intervention during chronic Q fever; specifically, lipoprotein secretion could conceivably be inhibited by drugs like globomycin. Globomycin, a cyclic pentapeptide antibiotic, has been shown to inhibit secretion of lipoproteins in a wide variety of pathogens by inhibiting Lsp function (Geukens et al, 2006;Kiho et al, 2004;Rahman et al, 2007). Further investigation of LimB and other surfaceexposed metal-binding proteins of Coxiella is expected to yield clues regarding the poorly characterized pathogenesis of this highly infectious agent.…”

Section: Discussionmentioning

confidence: 99%

A unique Coxiella burnetii lipoprotein involved in metal binding (LimB)

2011

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Coxiella burnetii is the bacterial agent of Q fever in humans. Here, we describe a unique, 7.2 kDa, surface-exposed lipoprotein involved in metal binding which we have termed LimB. LimB was initially identified as a potential metal-binding protein on far-Western (FW) blots containing whole-cell lysate proteins when probed with nickel-coated horseradish peroxidase (Ni-HRP) and developed with a chemiluminescent HRP substrate. The corresponding identity of LimB as CBU1224a was established by matrix-assisted laser desorption ionization-tandem time-offlight mass spectrometry. BLAST analyses with CBU1224a showed no significant similarity to sequences outside strains of C. burnetii. Additional in silico analyses revealed a putative 20 residue signal sequence with the carboxyl end demarcated by a potential lipobox (LSGC) whose Cys residue is predicted to serve as the N-terminal, lipidated Cys of mature LimB. The second residue of mature LimB is predicted to be Ala, an uncharged envelope localization residue. These features suggest that CBU1224a is synthesized as a prolipoprotein which is subsequently lipidated, secreted and anchored in the outer membrane. Mature LimB is predicted to contain 45 aa, of which there are 10 His and 5 Cys; both amino acids are frequently involved in binding transition metal cations. Recombinant LimB (rLimB) was generated and its Ni-HRP-binding activity demonstrated on FW blots. Ni-HRP binding by rLimB was inhibited by .95 % on FW blots done in the presence of EDTA, imidazole, Ni 2+ or Zn 2+ , and roughly halved in the presence of Co 2+ or Fe 3+ . The limB gene was maximally expressed at 3-7 days post-infection in Coxiellainfected Vero cells, coinciding with exponential phase growth. Two isoforms of LimB were detected on FW and Western blots, including a smaller (~7.2 kDa) species that was the predominant form in small cell variants and a larger isoform (~8.7 kDa) in large cell variants. LimB is Sarkosyl-insoluble, like many omps. The predicted surface location of LimB was verified by immunoelectron and immunofluorescence microscopy using anti-rLimB antibodies. Overall, the results suggest that LimB is a unique Coxiella lipoprotein that serves as a surface receptor for divalent metal cations and may play a role in acquiring at least one of these metals during intracellular growth.

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Section: Discussionmentioning

confidence: 99%

A unique Coxiella burnetii lipoprotein involved in metal binding (LimB)

2011

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“…Based on RT-PCR experiments, it was shown that the lepB and lspA genes are also transcribed when bacteria grow intracellularly in host cells. The functionality of LepB and LspA was demonstrated and LepB was found to be essential for viability, as is the case for other Gram-negative bacteria (Lammertyn et al, 2004;Geukens et al, 2006). It has also been suggested that LspA plays a role in the pathogenicity of L. pneumophila because in silico-predicted lipoproteins seem to be particularly involved in protein secretion and motility (Geukens et al, 2006).…”

Section: Protein Transport Across the Inner Membranementioning

confidence: 97%

The role of protein secretion systems in the virulence of the intracellular pathogen Legionella pneumophila

2007

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“…The signal peptidase II encoded by lspA gene induced in P. temperata belongs to a class of aspartyl proteases. Since the product of lspA has been suggested as an important virulence factor operating via maturation of several lipoproteins [ 60 ], we postulate that the product of lspA may play a pathological role in P. temperata by cleaving some core proteins and thus influencing bacterial life cycle in the insect host.…”

Section: Discussionmentioning

confidence: 99%

Comparative in vivo gene expression of the closely related bacteria Photorhabdus temperata and Xenorhabdus koppenhoeferi upon infection of the same insect host, Rhizotrogus majalis

Sreevatsan

Grewal

2009

BMC Genomics

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Background: Photorhabdus and Xenorhabdus are Gram-negative, phylogenetically related, enterobacteria, forming mutualism with the entomopathogenic nematodes Heterorhabditis and Steinernema, respectively. The mutualistic bacteria living in the intestines of the nematode infective juveniles are pathogenic to the insect upon release by the nematodes into the insect hemolymph. Such a switch needs activation of genes that promote bacterial virulence. We studied in vivo gene expression in Photorhabdus temperata and Xenorhabdus koppenhoeferi upon infection of the white grub Rhizotrogus majalis using selective capture of transcribed sequences technique.

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The type II signal peptidase of Legionella pneumophila

Cited by 9 publications

References 24 publications

A unique Coxiella burnetii lipoprotein involved in metal binding (LimB)

A unique Coxiella burnetii lipoprotein involved in metal binding (LimB)

The role of protein secretion systems in the virulence of the intracellular pathogen Legionella pneumophila

Comparative in vivo gene expression of the closely related bacteria Photorhabdus temperata and Xenorhabdus koppenhoeferi upon infection of the same insect host, Rhizotrogus majalis

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