LPS profiles of <i>hpyAVIBM</i> deletion mutant and wild-type strains.

<p>Lane 1: wild-type strain AM5, lane 2: <i>hpyAVIBM</i> deletion mutant AM5 complemented with <i>hpyAVIBM</i> from strain 26695, lane 3: <i>hpyAVIBM</i> deletion mutant. * highlights the bands different between wild type and mutant.</p

Motility assay.

<p>The photograph shows a BHI 7% FBS soft agar plate after 4 days of incubation. (<b>A</b>) SS1 (<b>B</b>) AM5 (<b>C</b>) Graph showing relative change in the diameter of mutant vs wild-type strain.</p

Natural transformation efficiency of <i>H. pylori</i> strains AM5 and SS1 and their respective <i>hpyAVIBM</i> deletion mutant strains.

<p>Values are calculated as transformants/cfu/mg DNA. P<0.0001.</p

Western blotting for CagA and VacA protein levels in <i>H. pylori</i> strainsAM5 and AM5Δ<i>hpyAVIBM</i>.

<p>Western blotting for CagA and VacA protein levels in <i>H. pylori</i> strainsAM5 and AM5Δ<i>hpyAVIBM</i>.</p

Survival of a pathogen in host depends upon its ability to modulate the balance between virulence and avirulence.

<p>Survival of a pathogen in host depends upon its ability to modulate the balance between virulence and avirulence.</p

Comparative transcriptomics of <i>H. pylori</i> wild type vs <i>hpyAVIBM</i> deletion mutant of strains AM5 and SS1.

<p>The genes listed are either down- or up-regulated in the <i>hpyAVIBM deletion</i> mutant of <i>H. pylori</i> strains AM5 and SS1. The identity of each gene is indicated by the Locus name as annotated in the <i>H. pylori</i> strain 26695 genome. The average ratio presented is the mean of mutant/wt ratio. P value <0.005.</p><p>ND: not determined.</p><p>- : not significant.</p

<i>hpyAVIBM</i> deletion enhances IL-8 production in AGS cell lines.

<p>(1) <i>H. pylori</i> strain AM5/SS1 (2) <i>H. pylori</i> strain AM5<i>ΔhpyAVIBM/</i>SS1<i>ΔhpyAVIBM</i> (3) <i>hpyAVIBM</i> deletion mutant AM5/SS1 complemented with <i>hpyAVIBM</i> from strain 26695.</p

Electrophoretic mobility shift analyses for the determination of the binding affinity of the wt R

<p><b>Copyright information:</b></p><p>Taken from "R.KpnI, an HNH superfamily REase, exhibits differential discrimination at non-canonical sequences in the presence of Ca and Mg"</p><p></p><p>Nucleic Acids Research 2007;35(8):2777-2786.</p><p>Published online 11 Apr 2007</p><p>PMCID:PMC1885652.</p><p>© 2007 The Author(s)</p>KpnI and mutant H149A in the presence of Ca. () and () Gel shift showing the native gel (inset) with duplex II and III. The wt R.KpnI was titrated over the concentration range from 0 to 256 nM, and the concentration of the DNA was 25 pM. The intensity of the shifted DNA band are expressed as% bound. (), () and () are the gel shifts showing the native gels (inset) with duplex I, II and III respectively using mutant H149A. The average values of the three different experiments were plotted in the graph

Sequences of the oligonucleotides used in this study.

<p>Sequences of the oligonucleotides used in this study.</p

Surface plasmon resonance analysis of HpDprA mutants interaction with DNA.

<p>Different concentrations of <b>(A)</b>HpDprA^R48A/R49Aand <b>(C)</b>HpDprA^{R48A/R49A/K133A} were injected on the single stranded DNA surface in standard buffer containing 150 mM NaCl. Both sample injection and buffer injection were carried out as described in materials and methods. Representative sensorgrams illustrating changes in the response units (the y—axis) as a function of time (the x-axis) are shown. Similarly, binding sensorgrams were obtained for the interaction of dsDNA with <b>(B)</b>HpDprA^R48A/R49Aand <b>(D)</b>HpDprA^{R48A/R49A/K133A}. The concentrations of soluble analytes and affinity constant (K_d) values are indicated in the inset to the figures. The K_d values are determined as described in materials and methods.</p