Plasma‐activated carbon nanotube‐based high sensitivity immunosensors for monitoring Legionella pneumophila by direct detection of maltose binding protein peptidoglycan‐associated lipoprotein (MBP‐PAL)

Modulation of Rab GTPase function by a protein phosphocholine transferase

Authors: Shaeri Mukherjee, Xiaoyun Liu, Kohei Arasaki, Justin McDonough, Jorge E. Galán & Craig R. RoyThe intracellular pathogen Legionella pneumophila modulates the activity of host GTPases to direct the transport and assembly of the membrane-bound compartment in which it resides. In vitro studies have indicated that the Legionella protein DrrA post-translationally modifies the GTPase Rab1 by a process called AMPylation. Here we used mass spectrometry to investigate post-translational modifications to Rab1 that occur during infection of host cells by Legionella. Consistent with in vitro studies, DrrA-mediated AMPylation of a conserved tyrosine residue in the switch II region of Rab1 was detected during infection. In addition, a modification to an adjacent serine residue in Rab1 ...

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Protein expression, crystallization and preliminary X-ray crystallographic studies of LidA from Legionella pneumophila

LidA, a translocated substrate of the Legionella pneumophila Dot/Icm type IV secretion system, is associated with maintenance of bacterial integrity and interferes with the early secretory pathway. However, the precise mechanism of LidA in these processes remains elusive. To further investigate the structure and function of LidA, the full-length protein was successfully expressed in Escherichia coli and purified. LidA was crystallized using sitting-drop vapour diffusion and diffracted to a resolution of 2.75 Å. The crystal belonged to space group P212121, with unit-cell parameters a = 57.5, b = 64.5, c = 167.3 Å, a = ß = ? = 90°. There is one molecule per asymmetric unit. (Source: Acta Crystallographica Section F)

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Protein expression, crystallization and preliminary X-ray crystallographic studies of LidA from Legionella pneumophila

Abstract: LidA, a translocated substrate of the Legionella pneumophila Dot/Icm type IV secretion system, is associated with maintenance of bacterial integrity and interferes with the early secretory pathway. However, the precise mechanism of LidA in these processes remains elusive. To further investigate the structure and function of LidA, the full-length protein was successfully expressed in Escherichia coli and purified. LidA was crystallized using sitting-drop vapour diffusion and diffracted to a resolution of 2.75 Å. The crystal belonged to space group P212121, with unit-cell parameters a = 57.5, b = 64.5, c = 167.3 Å,  =  =  = 90°. There is one molecule per asymmetric unit.

Keywords: LidA; Legionella pneumophila; Dot/Icm type IV secretion system.

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