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Results: 8

1.
FIG 7 

FIG 7 . From: Structural and Functional Analysis of the Pore-Forming Toxin NetB from Clostridium perfringens.

Oligomerization of NetB and its derivatives. The purified recombinant NetB derivatives indicated (750 ng) were separated by electrophoresis in 8% SDS-PAGE and Western blotted with polyclonal rabbit anti-NetB antiserum. The locations of size standards are indicated by the arrows on the left.

Xu-Xia Yan, et al. mBio. 2013 Jan-Feb;4(1):e00019-13.
2.
FIG 6 

FIG 6 . From: Structural and Functional Analysis of the Pore-Forming Toxin NetB from Clostridium perfringens.

Cartoon representation of NetB indicating the location of the random and site-directed mutations. The side chains of the mutated residues are labeled and shown in stick and semitransparent sphere representation. The amino latch domain is shown in magenta, the β-sandwich domain is shown in blue, the rim domain is shown in red, and the prestem region is shown in gold.

Xu-Xia Yan, et al. mBio. 2013 Jan-Feb;4(1):e00019-13.
3.
FIG 3 

FIG 3 . From: Structural and Functional Analysis of the Pore-Forming Toxin NetB from Clostridium perfringens.

Western blot analysis of the random NetB substitution derivatives. Culture supernatants of late-logarithmic-phase TPG (described in the supplemental material) cultures of C. perfringens strains producing the NetB derivatives indicated were subjected to 12% SDS-PAGE, transferred to a nitrocellulose membrane, and Western blotted with polyclonal rabbit anti-NetB antiserum. NC, negative control; WT, wild-type strain.

Xu-Xia Yan, et al. mBio. 2013 Jan-Feb;4(1):e00019-13.
4.
FIG 4 

FIG 4 . From: Structural and Functional Analysis of the Pore-Forming Toxin NetB from Clostridium perfringens.

Quantitative analysis of hemolytic activity of NetB. Purified NetB was serially diluted 2-fold in microtiter trays and incubated at 37°C for 30 min with RBC from the eight species indicated. The release of hemoglobin was measured by the increase in optical density at 415 nm, corrected for the buffer-only negative controls. Standard deviations for triplicate experiments were calculated.

Xu-Xia Yan, et al. mBio. 2013 Jan-Feb;4(1):e00019-13.
5.
FIG 5 

FIG 5 . From: Structural and Functional Analysis of the Pore-Forming Toxin NetB from Clostridium perfringens.

Quantitative hemolytic activities of substitution-containing NetB derivatives on chicken and duck RBC. The purified recombinant NetB proteins indicated were serially diluted 2-fold in microtiter trays and incubated at 37°C for 30 min with either chicken (A) or duck (B) RBC. The release of hemoglobin was measured by the increase in optical density at 415 nm, corrected for the buffer-only negative controls. Standard deviations for triplicate experiments were calculated.

Xu-Xia Yan, et al. mBio. 2013 Jan-Feb;4(1):e00019-13.
6.
FIG 2 

FIG 2 . From: Structural and Functional Analysis of the Pore-Forming Toxin NetB from Clostridium perfringens.

Structural comparison of the rim domain of NetB with HlgB and LukF-PV. Ribbon and surface representation of the rim domains of NetB (A), leukocidin F (HlgB) from S. aureus (PDB ID 2LKF [18]) (B), and Panton-Valentine leukocidin F (Luk-PV) from S. aureus (1PVL [54]) (C). The phosphocholine head group (PC) and morpholineethanesulfonic acid (MES) molecules, which crystallized with HlgB and LukF-PV, respectively, are shown in ball-and-stick representation. The residues forming the phospholipid or equivalent MES binding site are shown in stick representation. The equivalent residues in NetB are also shown in stick representation. Carbon atoms are shown in green (NetB), purple (HlgB), and pink (LukF-PV). Nitrogen atoms are shown in blue, oxygen atoms are shown in red, and sulfur atoms are shown in yellow. The format of the figure is partly based on Fig. 4 of reference 19.

Xu-Xia Yan, et al. mBio. 2013 Jan-Feb;4(1):e00019-13.
7.
FIG 8 

FIG 8 . From: Structural and Functional Analysis of the Pore-Forming Toxin NetB from Clostridium perfringens.

NetB in planar lipid bilayers. (A) Representative single-channel events recorded after addition of NetB (2 µg) to a PE-PS bilayer bathed in 0.1 M KCl and held at +40 mV. (B and C) Expanded time scales of two sections of panel A. Note the variation in closed levels in panel B and the small “flickery” events of 50 to 90 pS in panel C. (D) Distribution of mean conductance values obtained for NetB. (E) Effect of ion replacement on mean conductance values.

Xu-Xia Yan, et al. mBio. 2013 Jan-Feb;4(1):e00019-13.
8.
FIG 1 

FIG 1 . From: Structural and Functional Analysis of the Pore-Forming Toxin NetB from Clostridium perfringens.

The 1.8-Å crystal structure of NetB. (A) Cartoon representation of the overall fold of NetB. The amino latch domain is shown in magenta, the β-sandwich domain is shown in blue, the rim domain is shown in red, and the prestem region is shown in gold. The N- and C-terminal residues are labeled. Residues 162 to 175 were not observed in the crystal structure. (B) Structural comparison of NetB (gray) with delta-toxin from C. perfringens (blue) (PDB ID 2YGT). (C) Structural comparison of NetB (gray) with leukocidin F (HlgB) from S. aureus (orange) (PDB ID 2LKF [18]). (D) Cartoon representation of the rim domain of NetB. The side chains of exposed aromatic residues are shown in stick representation and labeled. Carbon atoms are colored red, oxygen atoms are colored yellow, and nitrogen atoms are colored blue. (E) Electron density of the NetB rim domain contoured at 1 sigma (1.8-Å-resolution data). The ethylene glycol molecule that crystallized with NetB is shown in stick representation, and surrounding electron density is colored green. Residues predicted to be involved in membrane recognition are shown in stick representation. Carbon atoms are red, oxygen atoms are yellow, and nitrogen atoms are blue.

Xu-Xia Yan, et al. mBio. 2013 Jan-Feb;4(1):e00019-13.

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