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. 2012 Mar;80(3):1243–1251. doi: 10.1128/IAI.05994-11

Fig 3.

Fig 3

Hcp1 secretion rather than Hcp2 secretion is dependent on the T6SS in E. coli RS218. (A) Hcp2 is undetected in supernatant from strain RS218. The Hcp2 secretion pathway was demonstrated by Western blotting with Hcp2 and Crp antibodies using the supernatants of E. coli strains RS218 and ΔT6SS. Crp is a cytoplasmic protein marker. (B) Hcp1 is secreted by the T6SS of RS218. Hcp1 secretion was demonstrated by Western blotting with Hcp1 and Crp antibodies using the supernatants from E. coli strains RS218, ΔT6SS, Δhcps, ΔevfC, and pAC-evfC/ΔevfC. Crp is a cytoplasmic protein marker. (C) β-Lactamase activity detection in the supernatants of various strains. pCX-hcp1/ΔT6SS, pCX-hcp2/RS218, and pCX-hcp2/ΔT6SS showed negligible β-lactamase activity, indicating no secretion, while pCX-hcp1/RS218 exhibited considerable β-lactamase activity, supporting Hcp1 secretion. The represented Bla activity data (means ± SD) represent the results from duplicate samples of two independent experiments. ***, P < 0.001. OD 486, optical density at 486 nm.