Function of the Escherichia coli msbB Gene, a Multicopy Suppressor of htrB Knockouts, in the Acylation of Lipid A

Clementz, Tony; Zhou, Zhimin; Raetz, Christian R. H.

doi:10.1074/jbc.272.16.10353

Cited by 198 publications

(261 citation statements)

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“…The msbB gene of Salmonellae is responsible for the terminal myristoylation of lipid A. 43,44 Disruption of the msbB gene in Salmonellae results in stable mutants that lower TNF induction. Introducing msbB2 mutations into Salmonella strain YS72 (hyperinvasive, purI2, xyl2), previously used for tumor targeting, has demonstrated that introduction of these mutations does not interfere with the ability of the Salmonellae to target tumors.…”

Section: Discussionmentioning

confidence: 99%

Plasmid-based Survivin shRNA and GRIM-19 carried by attenuated Salmonella suppresses tumor cell growth

Liu

Zhang²,

Guo³

et al. 2012

Asian J Androl

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Persistent activation of Survivin and its overexpression contribute to the formation, progression and metastasis of several different tumor types. Therefore, Survivin is an ideal target for RNA interference mediated-growth inhibition. Blockade of Survivin using specific short hairpin RNAs (shRNA) can significantly reduce prostate tumor growth. RNA interference does not fully ablate target gene expression, owing to the idiosyncrasies associated with shRNAs and their targets. To enhance the therapeutic efficacy of Survivin-specific shRNA, we employed a combinatorial expression of Survivin-specific shRNA and gene associated with retinoid-interferon-induced mortality-19 (GRIM-19). Then, the GRIM-19 coding sequences and Survivin-specific shRNAs were used to create a dual expression plasmid vector and were carried by an attenuated strain of Salmonella enteric serovar typhimurium (S. typhimurium) to treat prostate cancer in vitro and in vivo. We found that the co-expressed Survivin-specific shRNA and GRIM-19 synergistically and more effectively inhibited prostate tumor proliferation and survival, when compared with treatment with either single agent alone in vitro and in vivo. This study has provided a novel cancer gene therapeutic approach for prostate cancer.

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Section: Discussionmentioning

confidence: 99%

Plasmid-based Survivin shRNA and GRIM-19 carried by attenuated Salmonella suppresses tumor cell growth

Liu

Zhang²,

Guo³

et al. 2012

Asian J Androl

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“…Important enzymes of Kdo metabolism are CMP-Kdo synthetase (CKS), determined by the kdsB gene [4][5][6], and Kdo transferase, determined by the kdtA gene [7,8]. CKS catalyzes the activation of Kdo according to: CTP + Kdo M-~g~+CMP-Kdo + PPi, whereas Kdo transferase participates in the synthesis of the lipid A moiety of lipopolysaccharide.…”

Section: Introduction 2 Materials and Methodsmentioning

confidence: 99%

The three‐dimensional structure of capsule‐specific CMP: 2‐keto‐3‐deoxy‐manno‐octonic acid synthetase from Escherichia coli

1996

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CMP-Kdo synthetases from Gram-negative bacteria activate Kdo for incorporation into lipo-and capsule-polysaccharities. Here we report the crystal structure of the capsulespecific synthetase from E. coli at 2.3 A resolution. The enzyme is a dimer of 2 x 245 amino acid residues assuming C2 symmetry. It contains a central predominantly parallel [~-sheet with surrounding helices. The chain fold is novel; it is remotely related to a double Rossmaun fold. A large pocket at the carboxyl terminal ends of the central ~-strands most likely accommodates the catalytic center. A putative phosphate binding site at the loop between the first ~strand and the following helix is indicated by a bound iridium hexachloride anion.Key words: Capsular polysaccharide; CMP-Kdo synthetase (Escherichia coli); X-ray analysis; Crystal structure; Saccharide activation which 44% are identical with L-CKS. The kinetic data of the two isozymes differ distinctly [16].The rapid spread of antibiotic resistance among bacterial strains and the fact that Kdo is absent from mammalian cells [17] make K-CKS an attractive target molecule for drug design as an anti-infective measure. Cloning of the kpsU gene from the K5 antigen gene cluster [16] permitted structural analysis of this enzyme. Here, we describe the overexpression, purification, crystallization and X-ray structure determination of K-CKS. To our knowledge this is the first actually presented structure of a sugar-activating enzyme. A short note announcing an L-CKS crystal structure has been given earlier [18]. The AMP-transferring enzyme kanamycin nucleotidyltransferase [19] and the sugar phosphate-transferring enzyme galactose-l-phosphate uridylyltransferase [20] use similar substrates, but they do not activate sugars and they differ structurally from K-CKS.

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“…Growth of 32 P i -Labeled Cells-Cells were grown and labeled using the methods described previously (19,29). In general, labeling of the glycerophospholipids and lipid A was achieved by dilution of overnight cultures with 125 ml of pre-warmed fresh LB broth containing appropriate antibiotics to yield A 550 ϭ 0.05.…”

Section: Figmentioning

confidence: 99%

“…Two multicopy suppressors of htrB mutations (designated msbA and msbB) were also reported (20,21). The msbB gene displays sequence homology to htrB (20,22) and encodes a distinct acyltransferase (16,19) (Fig. 2) that can substitute for htrB at 42°C, when overexpressed on high copy plasmids.…”

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Function of Escherichia coli MsbA, an Essential ABC Family Transporter, in Lipid A and Phospholipid Biosynthesis

Zhou¹,

White²,

Polissi³

et al. 1998

Journal of Biological Chemistry

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Function of the Escherichia coli msbB Gene, a Multicopy Suppressor of htrB Knockouts, in the Acylation of Lipid A

Abstract: Overexpression of the

Cited by 198 publications

References 31 publications

Plasmid-based Survivin shRNA and GRIM-19 carried by attenuated Salmonella suppresses tumor cell growth

Plasmid-based Survivin shRNA and GRIM-19 carried by attenuated Salmonella suppresses tumor cell growth

The three‐dimensional structure of capsule‐specific CMP: 2‐keto‐3‐deoxy‐manno‐octonic acid synthetase from Escherichia coli

Function of Escherichia coli MsbA, an Essential ABC Family Transporter, in Lipid A and Phospholipid Biosynthesis

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