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- はすな ねぎたや
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![T1r T1r1 T1r3 T1r2 T1r3 [1] T1r T1r 500 LBD 1 LBD T1rLBD [2] T1r T1r2a T1r3 LBD [3] T1r2a/T1r3](/docs-images/104/162747886/images/1-0.jpg "L- [4] T1r2a/T1r3LBD M~ M T1rLBD FRET FRET T1rLBD [3] 1 T1r 2 T1r2a/T1r3 X [3] 28 75 March")
1 T1r T1r1 T1r3 T1r2 T1r3 [1] T1r T1r 500 LBD 1 LBD T1rLBD [2] T1r T1r2a T1r3 LBD [3] T1r2a/T1r3 L- [4] T1r2a/T1r3LBD M~ M T1rLBD FRET FRET T1rLBD [3] 1 T1r 2 T1r2a/T1r3 X [3] March 2017
![al. Cell 139, 234 (2009). [2] Ashikawa et al. Prot. Sci. 20, 1720 (2011).](/docs-images/104/162747886/images/2-1.jpg "[3] Nango et al. Sci. Rep. 6, 25745 (2016). 1998 2012 6 [4] Oike et al. J. Neurosci.")
2 T1rLBD imsaxst1r2a/t1r3lbd X 1 T1r2a/T1r3LBD Å Å Å 112 Å [3] T1rLBD 3 T1r2a/T1r3LBD LBD imsaxs 3T1rLBD [1] Yarmolinsky et al. Cell 139, 234 (2009). [2] Ashikawa et al. Prot. Sci. 20, 1720 (2011). [3] Nango et al. Sci. Rep. 6, (2016) [4] Oike et al. J. Neurosci. 27, 5584 (2007). 75 March
![Enterohemorrhagic Escherichia coli EHEC 1996 4,000 1(a) [1] EHEC 3 8 6 7 HUS [2] EHEC 1982 O157 [1,2,3] 1984 2 5 EHEC O157 [3]](/docs-images/104/162747886/images/3-0.jpg "EHEC EHEC EHEC O H [2] O157:H7 1(b) EHEC Stx A StxA B StxB StxB Gb3 Stx StxA [4] StxB 5 2a Stx 2 Stx1 Stx2StxB 169 70 345")
![350StxB 1 3 [4,5] 15 2a StxB [4,6,7] Stx1B Stx2B MMAtet [7] 4 MAMMARRRRA2b StxB StxB [8] Gb3 [5,9,10,11] X (a) (b) 5000 4000](/docs-images/104/162747886/images/3-1.jpg "3000 2000 1000 0 1 (a) 2006-2015 (b) O157:H7 http://www.nih.go.jp/niid/ja/ehec-m/2055-bac1/related/710-ehec-o157sem.")
3 Enterohemorrhagic Escherichia coli EHEC ,000 1(a) [1] EHEC HUS [2] EHEC 1982 O157 [1,2,3] EHEC O157 [3] EHEC EHEC EHEC O H [2] O157:H7 1(b) EHEC Stx A StxA B StxB StxB Gb3 Stx StxA [4] StxB 5 2a Stx 2 Stx1 Stx2StxB StxB 1 3 [4,5] 15 2a StxB [4,6,7] Stx1B Stx2B MMAtet [7] 4 MAMMARRRRA2b StxB StxB [8] Gb3 [5,9,10,11] X (a) (b) (a) (b) O157:H March 2017
![MD Stx1 B Stx1B MMAtet (a) 2 (a) Stx1B (b) MMAtetStx1B 3 MMAtet M A R (b) MD Generalized-Ensemble Molecular Biophysics GEMB [12]](/docs-images/104/162747886/images/4-0.jpg "(a) (b) Stx1B PDB 1BOS 2 StxB MMAtet AMBER99SB TIP3P 3 10ns(a) 150ns(b)Stx1B-MMAtet Stx1B MMA-tet space-fi ll ball-and-stick Stx1B")
![3 MMAtet1 Stx1BStx1B 4 Stx1B 2 Stx1B 2 Stx1BStx1A 4 StxB [4] 4 4 MMAtet Stx1B Stx1B 3 Stx2BMD Stx1B-MMAtet 3 10ns 3a 150ns3b Stx1](/docs-images/104/162747886/images/4-2.jpg "Stx1B MMAtet MMAtet i Stx1B k d ik S ik S ik =1/d ik 4a Arm1 Stx1B Stx1B Arm4 Stx1B 5 Stx1B 5 MMAtet 4b 3 4 MMAtet Stx1B 75 March")
4 MD Stx1 B Stx1B MMAtet (a) 2 (a) Stx1B (b) MMAtetStx1B 3 MMAtet M A R (b) MD Generalized-Ensemble Molecular Biophysics GEMB [12] (a) (b) Stx1B PDB 1BOS 2 StxB MMAtet AMBER99SB TIP3P 3 10ns(a) 150ns(b)Stx1B-MMAtet Stx1B MMA-tet space-fi ll ball-and-stick Stx1B 3 MMAtet1 Stx1BStx1B 4 Stx1B 2 Stx1B 2 Stx1BStx1A 4 StxB [4] 4 4 MMAtet Stx1B Stx1B 3 Stx2BMD Stx1B-MMAtet 3 10ns 3a 150ns3b Stx1 Stx1B MMAtet MMAtet i Stx1B k d ik S ik S ik =1/d ik 4a Arm1 Stx1B Stx1B Arm4 Stx1B 5 Stx1B 5 MMAtet 4b 3 4 MMAtet Stx1B 75 March
![Arm1 Stx1B W34 N35 D18 Arm2 4 N55 H58 G61 G62 D17 D18 F30 StxB MMAtet N55 H58 [6] MD StxB (a) MD EHEC (b) W34 G62 [7] 4 (a) S ik MMAtet k 5 MMAtet MAMMARRRRA (b) Stx1B 5 MMAtet 140-150nsMMAtet Stx1B](/docs-images/104/162747886/images/5-0.jpg "1 1 69 1988 1999 IBM 2001 2002 2004 [1], IASR 37, 85-86 (2016). [2], http://www1.mhlw.go.jp/o-157/o157q_a. [3] No.1 (1997). [4] 53, 44-51 (2008). [5] H. Ling et al.")
![, Structure of the Shiga-like Toxin I B-Pentamer Complexed with an Analogue of Its Receptor Gb3. Biochemistry 37, 1777-88 (1998). [6] K. Nishikawa, M. Watanabe, E. Kita, K. Igai, K. Omata, M.B. Yaffe, and Y.](/docs-images/104/162747886/images/5-1.jpg "Natori, A multivalent peptide library approach identifies a novel Shiga toxin inhibitor that induces aberrant cellular transport of the toxin, The FASEB Journal, 20: 2597-9, 2006. [7] K. Tsutsuki, M.")
![Fraser et al., Structure of Shiga Toxin Type 2 (Stx2) from Escherichia coli O157:H7, J. Biol. Chem. 279, 27511 27517 (2004). [9] P.I. Kitov et al.](/docs-images/104/162747886/images/5-3.jpg ", Shiga-like toxins are neutralized by tailored multivalent carbohydrate ligands, Nature 403, 669-672 (2000). [10] J.M. Jacobson et al.")
5 Arm1 Stx1B W34 N35 D18 Arm2 4 N55 H58 G61 G62 D17 D18 F30 StxB MMAtet N55 H58 [6] MD StxB (a) MD EHEC (b) W34 G62 [7] 4 (a) S ik MMAtet k 5 MMAtet MAMMARRRRA (b) Stx1B 5 MMAtet nsMMAtet Stx1B IBM [1], IASR 37, (2016). [2], [3] No.1 (1997). [4] 53, (2008). [5] H. Ling et al., Structure of the Shiga-like Toxin I B-Pentamer Complexed with an Analogue of Its Receptor Gb3. Biochemistry 37, (1998). [6] K. Nishikawa, M. Watanabe, E. Kita, K. Igai, K. Omata, M.B. Yaffe, and Y. Natori, A multivalent peptide library approach identifies a novel Shiga toxin inhibitor that induces aberrant cellular transport of the toxin, The FASEB Journal, 20: , [7] K. Tsutsuki, M. Watanabe-Takahashi, Y. Takenaka, E. Kita, and K. Nishikawa, Identification of a Peptide-Based Neutralizer That Potently InhibitsBoth Shiga Toxins 1 and 2 by Targeting Specific Receptor-Binding Regions, Infect. Immun. 81, (2013). [8] M.E. Fraser et al., Structure of Shiga Toxin Type 2 (Stx2) from Escherichia coli O157:H7, J. Biol. Chem. 279, (2004). [9] P.I. Kitov et al., Shiga-like toxins are neutralized by tailored multivalent carbohydrate ligands, Nature 403, (2000). [10] J.M. Jacobson et al., The crystal structure of Shiga toxin type 2 with bound disaccharide guides the design of a heterobifunctional toxin inhibitor, The J. Biol. Chem. 289, (2014). [11] M.E. Fraser et al., Binding of adenine to Stx2, the protein toxin from Escherichia coli O157:H7, Acta Cryst. F62, (2006). [12] H. Okumura, Temperature and pressure denaturation of chignolin: Folding and unfolding simulation by multibaric-multithermal molecular dynamics method, Proteins, 80: , March 2017
![2 d d [1] 1 KCP d8 2 1 dz 2 * dyz dzx * dxy * z HOMO-LUMO [Pt 2 (piam) 2 (NH 3 ) 4 ]X 2 piam = pivalamidate X = Pt II,II 2 * HOMO [Rh 2 (O 2 CCF 3 ) 4 ] Rh II,II 2 * LUMO 2 1 [Rh 2 (O 2 CCF 3 ) 4 ] 2](/docs-images/104/162747886/images/6-0.jpg "[Pt 2 (piam) 2 (NH 3 ) 4 ] Pt Pt Rh Rh Pt Pt [2] 2a 1 z VB CB [Rh 2 (O 2 CCF 3 ) 4 ] * 1 VB CB E 1 2.67 2.23 ev * CB E 2 1.85 ev E 3 1.")
6 2 d d [1] 1 KCP d8 2 1 dz 2 * dyz dzx * dxy * z HOMO-LUMO [Pt 2 (piam) 2 (NH 3 ) 4 ]X 2 piam = pivalamidate X = Pt II,II 2 * HOMO [Rh 2 (O 2 CCF 3 ) 4 ] Rh II,II 2 * LUMO 2 1 [Rh 2 (O 2 CCF 3 ) 4 ] 2 [Pt 2 (piam) 2 (NH 3 ) 4 ] Pt Pt Rh Rh Pt Pt [2] 2a 1 z VB CB [Rh 2 (O 2 CCF 3 ) 4 ] * 1 VB CB E ev * CB E ev E ev [Rh 2 (O 2 CCF 3 ) 4 ] [Rh 2 (O 2 CCH 3 ) 4 ] [Rh 2 (NHCOCH 3 ) 4 ] Pt Pt Rh Rh Pt Pt 2 3 [2,3] 2b 2c1 3 E 1 E 2 E a) 1 b) 2 c) 3 d) 4 75 March
![E 1 1 0.3 ev 3 * HOMO 1 3 [Ru 2 (O 2 CCH 3 ) 4 ] * 2 [Rh 2 (O 2 CCH 3 ) 4 ] * LUMO[Ru 2 (O 2 CCH 3 ) 4 ] [Pt 2 (piam) 2 (NH 3 ) 4 ]X 2 4 X Pt Pt Ru Ru Pt Pt 2 4 Rh Ru [4] 2d E 1 3.43 ev 3 4 300 K T 0.](/docs-images/104/162747886/images/7-1.jpg "95 cm 3 Kmol 1 Pt Pt Ru Ru Pt Pt 2 [Ru 2 ] * 2 Ru T 2 K 0.07 cm 3 Kmol 1 [Ru 2 ] [Ru 2 ] 1.")
7 E ev 3 * HOMO 1 3 [Ru 2 (O 2 CCH 3 ) 4 ] * 2 [Rh 2 (O 2 CCH 3 ) 4 ] * LUMO[Ru 2 (O 2 CCH 3 ) 4 ] [Pt 2 (piam) 2 (NH 3 ) 4 ]X 2 4 X Pt Pt Ru Ru Pt Pt 2 4 Rh Ru [4] 2d E ev K T 0.95 cm 3 Kmol 1 Pt Pt Ru Ru Pt Pt 2 [Ru 2 ] * 2 Ru T 2 K 0.07 cm 3 Kmol 1 [Ru 2 ] [Ru 2 ] 1.4 cm 1 d d 2 SQUID Quantum Design MPMS K : T : : [1],, 2016, 51, [2] K. Uemura, M. Ebihara, Inorg. Chem., 2011, 50, [3] K. Uemura, T. Kanbara, M. Ebihara, Inorg. Chem., 2014, 53, [4] K. Uemura, N. Uesugi, A. Matsuyama, M. Ebihara, H. Yoshikawa, K. Awaga, Inorg. Chem., 2016, 55, March 2017
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Key words: E. coli O 157: H7, fosfomycin, verotoxin, mouse infection
Key words: E. coli O 157: H7, fosfomycin, verotoxin, mouse infection Table 1. Bacterial cell counts in feces of mice infected with Esclwrichia coli O 157: H7 NK2 before and during oral dosing with fosfomycin