Publications
53 results found
Zhang P, Wang Z, Zhao S, et al., 2019, <SUP>1</SUP>H, <SUP>13</SUP>C and <SUP>15</SUP>N NMR assignments of Bacillus subtilis bacteriophage SPO1 protein Gp46, BIOMOLECULAR NMR ASSIGNMENTS, Vol: 13, Pages: 245-247, ISSN: 1874-2718
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- Citations: 3
Zhao S, Zhang K, Jiang S, et al., 2019, Resonance assignments of sigma factor S binding protein Crl from Escherichia coli, BIOMOLECULAR NMR ASSIGNMENTS, Vol: 13, Pages: 223-226, ISSN: 1874-2718
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- Citations: 2
Darvill N, Blake T, Rouse S, et al., 2018, Structural basis of phosphatidic acid sensing by APH in apicomplexan parasites, Structure, Vol: 26, Pages: 1059-1071.e6, ISSN: 0969-2126
Plasmodium falciparum and Toxoplasma gondii are obligate intracellular parasites that belong to the phylum of Apicomplexa and cause major human diseases. Their access to an intracellular lifestyle is reliant on the coordinated release of proteins from the specialized apical organelles called micronemes and rhoptries. A specific phosphatidic acid effector, the acylated pleckstrin homology domain-containing protein (APH) plays a central role in microneme exocytosis and thus is essential for motility, cell entry, and egress. TgAPH is acylated on the surface of the micronemes and recruited to phosphatidic acid (PA)-enriched membranes. Here, we dissect the atomic details of APH PA-sensing hub and its functional interaction with phospholipid membranes. We unravel the key determinant of PA recognition for the first time and show that APH inserts into and clusters multiple phosphate head-groups at the bilayer binding surface.
Liu B, Wang Z, Lan L, et al., 2018, A rapid colorimetric method to visualize protein interactions, Chemistry - A European Journal, Vol: 24, Pages: 6727-6731, ISSN: 0947-6539
As key molecules in most biological pathways, proteins physically contact one or more biomolecules in a highly specific manner. Several driving forces (i.e., electrostatic and hydrophobic) facilitate such interactions and a variety of methods have been developed to monitor these processes both in vivo and in vitro. In this work, a new method is reported for the detection of protein interactions by visualizing a color change of a cyanine compound, a supramolecule complex of 3,3-di-(3-sulfopropyl)-4,5,4',5'-dibenzo-9-methyl-thiacarbocyanine triethylammonium salt (MTC). Nuclear magnetic resonance (NMR) studies suggest that the hydrophobic nature of the protein surfaces drives MTC into different types of aggregates with distinct colors. When proteins interact with other biomolecules, the hydrophobic surface of the complex differs, resulting in a shift in the form of MTC aggregation, which results in a color change. As a result, this in vitro method has the potential to become a rapid tool for the confirmation of protein-biomolecule interactions, without the requirements for sophisticated instrumentation or approaches.
Tabib-Salazar A, Liu B, Declan B, et al., 2018, T7 phage factor required for managing RpoS in Escherichia coli, Proceedings of the National Academy of Sciences, Vol: 115, Pages: E5353-E5362, ISSN: 0027-8424
T7 development in Escherichia coli requires the inhibition of the housekeepingform of the bacterial RNA polymerase (RNAP), Eσ70, by two T7 proteins: Gp2and Gp5.7. While the biological role of Gp2 is well understood, that of Gp5.7remains to be fully deciphered. Here, we present results from functional andstructural analyses to reveal that Gp5.7 primarily serves to inhibit EσS, thepredominant form of the RNAP in the stationary phase of growth, whichaccumulates in exponentially growing E. coli as a consequence of buildup ofguanosine pentaphosphate ((p)ppGpp) during T7 development. We furtherdemonstrate a requirement of Gp5.7 for T7 development in E. coli cells in thestationary phase of growth. Our finding represents a paradigm for how somelytic phages have evolved distinct mechanisms to inhibit the bacterialtranscription machinery to facilitate phage development in bacteria in theexponential and stationary phases of growth.
Zhang P, Yang X, He Y, et al., 2017, Preparation, characterization and toxicity evaluation of amphotericin B loaded MPEG-PCL micelles and its application for buccal tablets, APPLIED MICROBIOLOGY AND BIOTECHNOLOGY, Vol: 101, Pages: 7357-7370, ISSN: 0175-7598
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- Citations: 10
Tabib-Salazar A, Liu B, Shadrin A, et al., 2017, Full shut-off of Escherichia coli RNA-polymerase by T7 phage requires a small phage-encoded DNA-binding protein, Nucleic Acids Research, Vol: 45, Pages: 7697-7707, ISSN: 1362-4962
Infection of Escherichia coli by the T7 phage leads to rapid and selective inhibition of the bacterial RNA polymerase (RNAP) by the 7 kDa T7 protein Gp2. We describe the identification and functional and structural characterisation of a novel 7 kDa T7 protein, Gp5.7, which adopts a winged helix-turn-helix-like structure and specifically represses transcription initiation from host RNAP-dependent promoters on the phage genome via a mechanism that involves interaction with DNA and the bacterial RNAP. Whereas Gp2 is indispensable for T7 growth in E. coli, we show that Gp5.7 is required for optimal infection outcome. Our findings provide novel insights into how phages fine-tune the activity of the host transcription machinery to ensure both successful and efficient phage progeny development.
Jønsson R, Liu B, Struve C, et al., 2016, Structural and functional studies of Escherichia coli Aggregative Adherence Fimbriae (AAF/V) reveal a deficiency in extracellular matrix binding, BBA Protein and Proteomics, Vol: 1865, Pages: 304-311, ISSN: 1570-9639
Enteroaggregative Escherichia coli (EAEC) is an emerging cause of acute and persistent diarrhea worldwide. The pathogenesis of different EAEC stains is complicated, however, the early essential step begins with attachment of EAEC to intestinal mucosa via aggregative adherence fimbriae (AAFs). Currently, five different variants have been identified, which all share a degree of similarity in the gene organization of their operons and sequences. Here, we report the solution structure of Agg5A from the AAF/V variant. While preserving the major structural features shared by all AAF members, only Agg5A possesses an inserted helix at the beginning of the donor strand, which together with altered surface electrostatics, renders the protein unable to interact with fibronectin. Hence, here we characterize the first AAF variant with a binding mode that varies from previously described AAFs
Liang X, Liu B, Zhu F, et al., 2016, A distinct sortase SrtB anchors and processes a streptococcal adhesin AbpA with a novel structural property., Scientific Reports, Vol: 6, ISSN: 2045-2322
Surface display of proteins by sortases in Gram-positive bacteria is crucial for bacterial fitness and virulence. We found a unique gene locus encoding an amylase-binding adhesin AbpA and a sortase B in oral streptococci. AbpA possesses a new distinct C-terminal cell wall sorting signal. We demonstrated that this C-terminal motif is required for anchoring AbpA to cell wall. In vitro and in vivo studies revealed that SrtB has dual functions, anchoring AbpA to the cell wall and processing AbpA into a ladder profile. Solution structure of AbpA determined by NMR reveals a novel structure comprising a small globular α/β domain and an extended coiled-coil heliacal domain. Structural and biochemical studies identified key residues that are crucial for amylase binding. Taken together, our studies document a unique sortase/adhesion substrate system in streptococci adapted to the oral environment rich in salivary amylase.
Liu B, Zhu F, Wu H, et al., 2015, NMR assignment of the amylase-binding protein A from <i>Streptococcus parasanguinis</i>, BIOMOLECULAR NMR ASSIGNMENTS, Vol: 9, Pages: 173-175, ISSN: 1874-2718
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- Citations: 1
Huynh M-H, Liu B, Henry M, et al., 2015, Structural Basis of <i>Toxoplasma gondii</i> MIC2-associated Protein Interaction with MIC2, JOURNAL OF BIOLOGICAL CHEMISTRY, Vol: 290, Pages: 1432-1441
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- Citations: 17
Berry AA, Yang Y, Pakharukova N, et al., 2014, Structural Insight into Host Recognition by Aggregative Adherence Fimbriae of Enteroaggregative <i>Escherichia coli</i>, PLOS PATHOGENS, Vol: 10, ISSN: 1553-7366
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- Citations: 31
Liu B, Shadrin A, Sheppard C, et al., 2014, A bacteriophage transcription regulator inhibits bacterial transcription initiation by Sigma-factor displacement, Nucleic Acids Research, Vol: 42, Pages: 4294-4305, ISSN: 0305-1048
Bacteriophages (phages) appropriate essential processes of bacterial hosts to benefit their own development. The multisubunit bacterial RNA polymerase (RNAp) enzyme, which catalyses DNA transcription, is targeted by phage-encoded transcription regulators that selectively modulate its activity. Here, we describe the structural and mechanistic basis for the inhibition of bacterial RNAp by the transcription regulator P7 encoded by Xanthomonas oryzae phage Xp10. We reveal that P7 uses a two-step mechanism to simultaneously interact with the catalytic β and β’ subunits of the bacterial RNAp and inhibits transcription initiation by inducing the displacement of the σ70-factor on initial engagement of RNAp with promoter DNA. The new mode of interaction with and inhibition mechanism of bacterial RNAp by P7 underscore the remarkable variety of mechanisms evolved by phages to interfere with host transcription.
Liu B, Shadrin A, Sheppard C, et al., 2014, The sabotage of the bacterial transcription machinery by a small bacteriophage protein., Bacteriophage, Vol: 4, ISSN: 2159-7073
Many bacteriophages produce small proteins that specifically interfere with the bacterial host transcription machinery and thus contribute to the acquisition of the bacterial cell by the bacteriophage. We recently described how a small protein, called P7, produced by the Xp10 bacteriophage inhibits bacterial transcription initiation by causing the dissociation of the promoter specificity sigma factor subunit from the host RNA polymerase holoenzyme. In this addendum to the original publication, we present the highlights of that research.
Wang K, Liu T, Lin R, et al., 2014, Preparation and <i>in vitro</i> release of buccal tablets of naringenin-loaded MPEG-PCL nanoparticles, RSC ADVANCES, Vol: 4, Pages: 33672-33679, ISSN: 2046-2069
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- Citations: 25
Muniz-Feliciano L, Van Grol J, Portillo J-AC, et al., 2013, <i>Toxoplasma gondii</i>-Induced Activation of EGFR Prevents Autophagy Protein-Mediated Killing of the Parasite, PLOS PATHOGENS, Vol: 9, ISSN: 1553-7366
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- Citations: 86
Tabib-Salazar A, Liu B, Doughty P, et al., 2013, The actinobacterial transcription factor RbpA binds to the principal sigma subunit of RNA polymerase, NUCLEIC ACIDS RESEARCH, Vol: 41, Pages: 5679-5691, ISSN: 0305-1048
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- Citations: 39
Liu B, Tabib-Salazar A, Doughty P, et al., 2013, The actinobacterial transcription factor RbpA binds to the principal sigma subunit of RNA polymerase
James E, Liu M, Sheppard C, et al., 2012, Structural and Mechanistic Basis for the Inhibition of <i>Escherichia coli</i> RNA Polymerase by T7 Gp2, MOLECULAR CELL, Vol: 47, Pages: 755-766, ISSN: 1097-2765
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- Citations: 34
Liu B, Garnett JA, Lee W-C, et al., 2012, Promoting crystallisation of the <i>Salmonella enteritidis</i> fimbriae 14 pilin SefD using deuterium oxide, BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, Vol: 421, Pages: 208-213, ISSN: 0006-291X
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- Citations: 3
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
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
Saouros S, Blumenschein TMA, Sawmynaden K, et al., 2007, High-level bacterial expression and purification of apicomplexan micronemal proteins for structural studies, PROTEIN AND PEPTIDE LETTERS, Vol: 14, Pages: 411-415, ISSN: 0929-8665
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- Citations: 10
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