Publications
243 results found
Rana RR, Simpson P, Zhang M, et al., 2011, <i>Yersinia pestis</i> TIR-domain protein forms dimers that interact with the human adaptor protein MyD88, MICROBIAL PATHOGENESIS, Vol: 51, Pages: 89-95, ISSN: 0882-4010
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- Citations: 30
Sheppard C, Camara B, Shadrin A, et al., 2011, Inhibition of <i>Escherichia coli</i> RNAp by T7 Gp2 Protein: Role of Negatively Charged Strip of Amino Acid Residues in Gp2, JOURNAL OF MOLECULAR BIOLOGY, Vol: 407, Pages: 623-632, ISSN: 0022-2836
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- Citations: 9
Yang Y, Berry AA, Lee W-C, et al., 2011, Complete <SUP>1</SUP>H, <SUP>13</SUP>C and <SUP>15</SUP>N NMR assignments for donor-strand complemented AafA, the major pilin of aggregative adherence fimbriae (AAF/II) from enteroaggregative E. coli, BIOMOLECULAR NMR ASSIGNMENTS, Vol: 5, Pages: 1-5, ISSN: 1874-2718
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- Citations: 2
Yang Y, Garnett JA, Matthews S, 2011, Crystallization and initial crystallographic analysis of AafA: the major adhesive subunit of the enteroaggregative <i>Escherichia coli</i> AAF/II pilus, ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, Vol: 67, Pages: 454-456
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- Citations: 4
Moore B, Miles AJ, Guerra-Giraldez C, et al., 2011, Structural Basis of Molecular Recognition of the <i>Leishmania</i> Small Hydrophilic Endoplasmic Reticulum-associated Protein (SHERP) at Membrane Surfaces, JOURNAL OF BIOLOGICAL CHEMISTRY, Vol: 286, Pages: 9246-9256
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- Citations: 7
Garnett JA, Ramboarina S, Lee W-C, et al., 2011, Crystallization and initial crystallographic analysis of the <i>Streptococcus parasanguinis</i> FW213 Fap1-NR<sub>α</sub> adhesive domain at pH 5.0, ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, Vol: 67, Pages: 274-276
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- Citations: 2
Woermann ME, Corrigan RM, Simpson PJ, et al., 2011, Enzymatic activities and functional interdependencies of <i>Bacillus subtilis</i> lipoteichoic acid synthesis enzymes, MOLECULAR MICROBIOLOGY, Vol: 79, Pages: 566-583, ISSN: 0950-382X
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- Citations: 53
Salgado PS, Taylor JD, Cota E, et al., 2011, Extending the usability of the phasing power of diselenide bonds: SeCys SAD phasing of CsgC using a non-auxotrophic strain, ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, Vol: 67, Pages: 8-13, ISSN: 2059-7983
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- Citations: 15
Ramboarina S, Garnett JA, Zhou M, et al., 2010, Structural Insights into Serine-rich Fimbriae from Gram-positive Bacteria, JOURNAL OF BIOLOGICAL CHEMISTRY, Vol: 285, Pages: 32446-32457, ISSN: 0021-9258
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- Citations: 42
Yan R, Simpson PJ, Matthews SJ, et al., 2010, Backbone <SUP>1</SUP>H, <SUP>15</SUP>N, <SUP>13</SUP>C and Ile, Leu, Val methyl chemical shift assignments for the 33.5 kDa N-terminal domain of Candida albicans ALS1, BIOMOLECULAR NMR ASSIGNMENTS, Vol: 4, Pages: 187-190, ISSN: 1874-2718
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- Citations: 8
Friedrich N, Matthews S, Soldati-Favre D, 2010, Sialic acids: Key determinants for invasion by the Apicomplexa, INTERNATIONAL JOURNAL FOR PARASITOLOGY, Vol: 40, Pages: 1145-1154, ISSN: 0020-7519
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- Citations: 14
Bergeron JRC, Huthoff H, Veselkov DA, et al., 2010, The SOCS-Box of HIV-1 Vif Interacts with ElonginBC by Induced-Folding to Recruit Its Cul5-Containing Ubiquitin Ligase Complex, PLOS PATHOGENS, Vol: 6, ISSN: 1553-7366
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- Citations: 67
Arbeloa A, Garnett J, Lillington J, et al., 2010, EspM2 is a RhoA guanine nucleotide exchange factor, Cellular Microbiology, Vol: 12, Pages: 654-664, ISSN: 1462-5814
We investigated how the type III secretion system WxxxE effectors EspM2 of enterohaemorrhagic Escherichia coli, which triggers stress fibre formation, and SifA of Salmonella enterica serovar Typhimurium, which is involved in intracellular survival, modulate Rho GTPases. We identified a direct interaction between EspM2 or SifA and nucleotide‐free RhoA. Nuclear Magnetic Resonance Spectroscopy revealed that EspM2 has a similar fold to SifA and the guanine nucleotide exchange factor (GEF) effector SopE. EspM2 induced nucleotide exchange in RhoA but not in Rac1 or H‐Ras, while SifA induced nucleotide exchange in none of them. Mutating W70 of the WxxxE motif or L118 and I127 residues, which surround the catalytic loop, affected the stability of EspM2. Substitution of Q124, located within the catalytic loop of EspM2, with alanine, greatly attenuated the RhoA GEF activity in vitro and the ability of EspM2 to induce stress fibres upon ectopic expression. These results suggest that binding of SifA to RhoA does not trigger nucleotide exchange while EspM2 is a unique Rho GTPase GEF.
Camara B, Liu M, Reynolds J, et al., 2010, T7 phage protein Gp2 inhibits the <i>Escherichia coli</i> RNA polymerase by antagonizing stable DNA strand separation near the transcription start site, PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, Vol: 107, Pages: 2247-2252, ISSN: 0027-8424
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- Citations: 53
Friedrich N, Santos JM, Liu Y, et al., 2010, Members of a novel protein family containing microneme adhesive repeat domains act as sialic acid-binding lectins during host cell invasion by apicomplexan parasites, J.Biol.Chem., Vol: 285, Pages: 2064-2076
Numerous intracellular pathogens exploit cell surface glycoconjugates for host cell recognition and entry. Unlike bacteria and viruses, Toxoplasma gondii and other parasites of the phylum Apicomplexa actively invade host cells, and this process critically depends on adhesins (microneme proteins) released onto the parasite surface from intracellular organelles called micronemes (MIC). The microneme adhesive repeat (MAR) domain of T. gondii MIC1 (TgMIC1) recognizes sialic acid (Sia), a key determinant on the host cell surface for invasion by this pathogen. By complementation and invasion assays, we demonstrate that TgMIC1 is one important player in Sia-dependent invasion and that another novel Sia-binding lectin, designated TgMIC13, is also involved. Using BLAST searches, we identify a family of MAR-containing proteins in enteroparasitic coccidians, a subclass of apicomplexans, including T. gondii, suggesting that all these parasites exploit sialylated glycoconjugates on host cells as determinants for enteric invasion. Furthermore, this protein family might provide a basis for the broad host cell range observed for coccidians that form tissue cysts during chronic infection. Carbohydrate microarray analyses, corroborated by structural considerations, show that TgMIC13, TgMIC1, and its homologue Neospora caninum MIC1 (NcMIC1) share a preference for alpha2-3- over alpha2-6-linked sialyl-N-acetyllactosamine sequences. However, the three lectins also display differences in binding preferences. Intense binding of TgMIC13 to alpha2-9-linked disialyl sequence reported on embryonal cells and relatively strong binding to 4-O-acetylated-Sia found on gut epithelium and binding of NcMIC1 to 6'sulfo-sialyl Lewis(x) might have implications for tissue tropism
Lai L, Simpson P, Bumstead J, et al., 2009, Complete NMR assignments for the second microneme adhesive repeat (MAR) domain from Eimeria tenella microneme protein EtMIC3, BIOMOLECULAR NMR ASSIGNMENTS, Vol: 3, Pages: 175-177, ISSN: 1874-2718
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- Citations: 8
Allman SA, Jensen HH, Vijayakrishnan B, et al., 2009, Potent fluoro-oligosaccharide probes of adhesion in Toxoplasmosis, Chembiochem., Vol: 10, Pages: 2522-2529
Unnatural, NMR- and MRI-active fluorinated sugar probes, designed and synthesised to bind to the pathogenic protein TgMIC1 from Toxoplasma gondii, were found to display binding potency equal to and above that of the natural ligand. Dissection of the binding mechanism and modes, including the first X-ray crystal structures of a fluoro-oligosaccharide bound to a lectin, demonstrate that it is possible to create effective fluorinated probe ligands for the study of, and perhaps intervention in, sugar-protein binding events
Liu Y, Garnett JA, Leon E, et al., 2009, Detailed insights from microarray and crystallographic studies into carbohydrate recognition by microneme protein 1 (MIC1) of Toxoplasma gondii, Protein Sci., Vol: 18, Pages: 1935-1947
The intracellular protozoan Toxoplasma gondii is among the most widespread parasites. The broad host cell range of the parasite can be explained by carbohydrate microarray screening analyses that have demonstrated the ability of the T. gondii adhesive protein, TgMIC1, to bind to a wide spectrum of sialyl oligosaccharide ligands. Here, we investigate by further microarray analyses in a dose-response format the differential binding of TgMIC1 to 2-3- and 2-6-linked sialyl carbohydrates. Interestingly, two novel synthetic fluorinated analogs of 3'SiaLacNAc(1-4) and 3'SiaLacNAc(1-3) were identified as highly potent ligands. To understand the structural basis of the carbohydrate binding specificity of TgMIC1, we have determined the crystal structures of TgMIC1 micronemal adhesive repeat (MAR)-region (TgMIC1-MARR) in complex with five sialyl-N-acetyllactosamine analogs. These crystal structures have revealed a specific, water-mediated hydrogen bond network that accounts for the preferential binding of TgMIC1-MARR to arrayed 2-3-linked sialyl oligosaccharides and the high potency of the fluorinated analogs. Furthermore, we provide strong evidence for the first observation of a C--F...H--O hydrogen bond within a lectin-carbohydrate complex. Finally, detailed comparison with other oligosaccharide-protein complexes in the Protein Data Bank (PDB) reveals a new family of sialic-acid binding sites from lectins in parasites, bacteria, and viruses
Xu Y, Liu M, Simpson PJ, et al., 2009, Automated Assignment in Selectively Methyl-Labeled Proteins, JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, Vol: 131, Pages: 9480-+, ISSN: 0002-7863
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- Citations: 27
Liu B, Sawmynaden K, Marchant J, et al., 2009, Complete resonance assignments for the MIC2 associated protein from <i>Toxoplasma gondii</i>, BIOMOLECULAR NMR ASSIGNMENTS, Vol: 3, Pages: 81-83, ISSN: 1874-2718
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- Citations: 2
Sawmynaden K, Saouros S, Marchant J, et al., 2008, Complete NMR assignments for the second EGF domain of MIC6 from <i>Toxoplasma gondii</i> and re-assignment in complex with the galectin-like domain of MIC1, BIOMOLECULAR NMR ASSIGNMENTS, Vol: 2, Pages: 187-189, ISSN: 1874-2718
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- Citations: 1
Saouros S, Sawmynaden K, Marchant J, et al., 2008, Complete resonance assignment of the galectin-like domain of MIC1 from <i>Toxoplasma gondii</i> in complex with the second EGF domain from MIC6 and the backbone assignment in complex with the third EGF domain, BIOMOLECULAR NMR ASSIGNMENTS, Vol: 2, Pages: 175-177, ISSN: 1874-2718
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- Citations: 2
Marchant J, Sawmynaden K, Saouros S, et al., 2008, Complete resonance assignment of the first and second apple domains of MIC4 from <i>Toxoplasma gondii</i>, using a new NMRView-based assignment aid, BIOMOLECULAR NMR ASSIGNMENTS, Vol: 2, Pages: 119-121, ISSN: 1874-2718
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- Citations: 30
Sawmynaden K, Saouros S, Friedrich N, et al., 2008, Structural insights into microneme protein assembly reveal a new mode of EGF domain recognition, EMBO REPORTS, Vol: 9, Pages: 1149-1155, ISSN: 1469-221X
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- Citations: 25
Bleijlevens B, Shivarattan T, Flashman E, et al., 2008, Dynamic states of the DNA repair enzyme AlkB regulate product release, EMBO REPORTS, Vol: 9, Pages: 872-877, ISSN: 1469-221X
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- Citations: 52
Yeung HO, Kloppsteck P, Niwa H, et al., 2008, Insights into adaptor binding to the AAA protein p97, BIOCHEMICAL SOCIETY TRANSACTIONS, Vol: 36, Pages: 62-67, ISSN: 0300-5127
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- Citations: 107
Korotkova N, Yang Y, Le Trong I, et al., 2008, Binding of Dr adhesins of <i>Escherichia coli</i> to carcinoembryonic antigen triggers receptor dissociation, MOLECULAR MICROBIOLOGY, Vol: 67, Pages: 420-434, ISSN: 0950-382X
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- Citations: 53
Isaacson RL, Simpson PJ, Liu M, et al., 2007, A new labeling method for methyl transverse relaxation-optimized spectroscopy NMR spectra of alanine residues, JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, Vol: 129, Pages: 15428-+, ISSN: 0002-7863
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- Citations: 89
Monie TP, Perrin AJ, Birtley JR, et al., 2007, Structural insights into the transcriptional and translational roles of Ebp1, EMBO JOURNAL, Vol: 26, Pages: 3936-3944, ISSN: 0261-4189
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- Citations: 79
Isaacson RL, Pye VE, Simpson P, et al., 2007, Detailed structural insights into the p97-Npl4-Ufd1 interface, JOURNAL OF BIOLOGICAL CHEMISTRY, Vol: 282, Pages: 21361-21369
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- Citations: 55
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