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Journal articles on the topic 'TbpB'

Author: Grafiati

Published: 4 June 2021

Last updated: 12 February 2022

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1

BOULTON, Ian C., Andrew R. GORRINGE, Nigel ALLISON, et al. "Transferrin-binding protein B isolated from Neisseria meningitidis discriminates between apo and diferric human transferrin." Biochemical Journal 334, no. 1 (1998): 269–73. http://dx.doi.org/10.1042/bj3340269.

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Neisseria meningitidis utilization of human serum transferrin (hTF)-bound iron is an important pathogenicity determinant. The efficiency of this system would clearly be increased through preferential binding of diferric hTF over the iron-free form. To characterize this process, functionally active meningococcal transferrin-binding protein A (TbpA) and TbpB have been purified from N. meningitidis using a novel purification procedure. The association of isolated Tbps and Tbps in the presence of hTF was investigated by gel filtration. Co-purified TbpA+B formed a complex of molecular mass 300 kDa

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2

BOULTON, Ian C., Andrew R. GORRINGE, Beatrice GORINSKY, et al. "Purified meningococcal transferrin-binding protein B interacts with a secondary, strain-specific, binding site in the N-terminal lobe of human transferrin." Biochemical Journal 339, no. 1 (1999): 143–49. http://dx.doi.org/10.1042/bj3390143.

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Neisseria meningitidis, grown in iron-limited conditions, produces two transferrin-binding proteins (TbpA and TbpB) that independently and specifically bind human serum transferrin (hTF) but not bovine serum transferrin (bTF). We have used surface plasmon resonance to characterize the interaction between individual TbpA and TbpB and a series of full-length human–bovine chimaeric transferrins (hbTFs) under conditions of variable saturation with iron. A comparative analysis of hTF and hbTF chimaera-binding data confirmed that the major features involved in Tbp binding are located in the C-termin

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3

Stokes, Russell H., Jonathan S. Oakhill, Christopher L. Joannou, Andrew R. Gorringe, and Robert W. Evans. "Meningococcal Transferrin-Binding Proteins A and B Show Cooperation in Their Binding Kinetics for Human Transferrin." Infection and Immunity 73, no. 2 (2005): 944–52. http://dx.doi.org/10.1128/iai.73.2.944-952.2005.

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ABSTRACT Neisseria meningitidis, a causative agent of bacterial meningitis and septicemia, obtains transferrin-bound iron by expressing two outer membrane-located transferrin-binding proteins, TbpA and TbpB. A novel system was developed to investigate the interaction between Tbps and human transferrin. Copurified TbpA-TbpB, recombined TbpA-TbpB, and individual TbpA and TbpB were reconstituted into liposomes and fused onto an HPA chip (BIAcore). All preparations formed stable monolayers, which, with the exception of TbpB, could be regenerated by removing bound transferrin. The ligand binding pr

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4

West, David, Karen Reddin, Mary Matheson, et al. "Recombinant Neisseria meningitidis Transferrin Binding Protein A Protects against Experimental Meningococcal Infection." Infection and Immunity 69, no. 3 (2001): 1561–67. http://dx.doi.org/10.1128/iai.69.3.1561-1567.2001.

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ABSTRACT To better characterize the vaccine potential of Neisseria meningitidis transferrin binding proteins (Tbps), we have overexpressed TbpA and TbpB from Neisseria meningitidisisolate K454 in Escherichia coli. The ability to bind human transferrin was retained by both recombinant proteins, enabling purification by affinity chromotography. The recombinant Tbps were evaluated individually and in combination in a mouse intraperitoneal-infection model to determine their ability to protect against meningococcal infection and to induce cross-reactive and bactericidal antibodies. For the first ti

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5

Renauld-Mongénie, Geneviève, David Poncet, Michèle Mignon, et al. "Role of Transferrin Receptor from a Neisseria meningitidis tbpB Isotype II Strain in Human Transferrin Binding and Virulence." Infection and Immunity 72, no. 6 (2004): 3461–70. http://dx.doi.org/10.1128/iai.72.6.3461-3470.2004.

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ABSTRACT Neisseria meningitidis acquires iron through the action of the transferrin (Tf) receptor, which is composed of the Tf-binding proteins A and B (TbpA and TbpB). Meningococci can be classified into isotype I and II strains depending on whether they harbor a type I or II form of TbpB. Both types of TbpB have been shown to differ in their genomic, biochemical, and antigenic properties. Here we present a comparative study of isogenic mutants deficient in either or both Tbps from the isotype I strain B16B6 and isotype II strain M982. We show that TbpA is essential in both strains for iron u

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6

Ronpirin, Chalinee, Ann E. Jerse, and Cynthia Nau Cornelissen. "Gonococcal Genes Encoding Transferrin-Binding Proteins A and B Are Arranged in a Bicistronic Operon but Are Subject to Differential Expression." Infection and Immunity 69, no. 10 (2001): 6336–47. http://dx.doi.org/10.1128/iai.69.10.6336-6347.2001.

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ABSTRACT Neisseria gonorrhoeae is capable of utilizing host iron-binding proteins, such as transferrin, lactoferrin, and hemoglobin, as the sole source of iron. The receptor involved in transferrin iron acquisition is composed of two distinct transferrin-binding proteins, TbpA and TbpB. The genes that encode these proteins are linked on the chromosome in the ordertbpB-tbpA but are separated by an inverted repeat of unknown function. In this study, we sought to understand the transcriptional organization and regulation of thetbp genes, using a combination of lacZtranscriptional fusion analysis

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7

Silva, Leslie P., Rong-hua Yu, Charles Calmettes, et al. "Steric and allosteric factors prevent simultaneous binding of transferrin-binding proteins A and B to transferrin." Biochemical Journal 444, no. 2 (2012): 189–97. http://dx.doi.org/10.1042/bj20112133.

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The ability to acquire iron directly from host Tf (transferrin) is an adaptation common to important bacterial pathogens belonging to the Pasteurellaceae, Moraxellaceae and Neisseriaceae families. A surface receptor comprising an integral outer membrane protein, TbpA (Tf-binding protein A), and a surface-exposed lipoprotein, TbpB (Tf-binding protein B), mediates the iron acquisition process. TbpB is thought to extend from the cell surface for capture of Tf to initiate the process and deliver Tf to TbpA. TbpA functions as a gated channel for the passage of iron into the periplasm. In the presen

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8

Menéndez, Tamara, Mairet Pérez, and Anabel Alvarez. "Antigenic and genetic characterization of a putative hybrid transferrin-binding protein B fromNeisseria meningitidis." Canadian Journal of Microbiology 45, no. 12 (1999): 1050–54. http://dx.doi.org/10.1139/w99-100.

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The transferrin-binding protein Bs (TbpBs) from the bacterium Neisseria meningitidis have been divided into two families according to genetic and antigenic features. TbpB from meningococcal strain B385 showed a molecular mass similar to that exhibited by TbpBs belonging to the high molecular mass family of TbpBs. TbpB was recognized by immunoassay using a specific serum directed against the TbpB of the reference strain for this family (strain M982). It was also recognized by a serum elicited against the TbpB of the reference strain for the low molecular mass family (strain B16B6). The tbpB gen

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9

Myers, Lisa E., Yan-ping Yang, Run-pan Du, et al. "The Transferrin Binding Protein B of Moraxella catarrhalis Elicits Bactericidal Antibodies and Is a Potential Vaccine Antigen." Infection and Immunity 66, no. 9 (1998): 4183–92. http://dx.doi.org/10.1128/iai.66.9.4183-4192.1998.

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ABSTRACT The transferrin binding protein genes (tbpA andtbpB) from two strains of Moraxella catarrhalis have been cloned and sequenced. The genomic organization of the M. catarrhalistransferrin binding protein genes is unique among known bacteria in that tbpA precedes tbpB and there is a third gene located between them. The deduced sequences of the M. catarrhalis TbpA proteins from two strains were 98% identical, while those of the TbpB proteins from the same strains were 63% identical and 70% similar. The third gene, tentatively called orf3, encodes a protein of approximately 58 kDa that is 9

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10

Ostberg, Karen L., Amanda J. DeRocco, Shreni D. Mistry, Mary Kathryne Dickinson, and Cynthia Nau Cornelissen. "Conserved Regions of Gonococcal TbpB Are Critical for Surface Exposure and Transferrin Iron Utilization." Infection and Immunity 81, no. 9 (2013): 3442–50. http://dx.doi.org/10.1128/iai.00280-13.

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ABSTRACTThe transferrin-binding proteins TbpA and TbpB enableNeisseria gonorrhoeaeto obtain iron from human transferrin. The lipoprotein TbpB facilitates, but is not strictly required for, TbpA-mediated iron acquisition. The goal of the current study was to determine the contribution of two conserved regions within TbpB to the function of this protein. Using site-directed mutagenesis, the first mutation we constructed replaced the lipobox (LSAC) of TbpB with a signal I peptidase cleavage site (LAAA), while the second mutation deleted a conserved stretch of glycine residues immediately downstre

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11

Luke, Nicole R., and Anthony A. Campagnari. "Construction and Characterization ofMoraxella catarrhalis Mutants Defective in Expression of Transferrin Receptors." Infection and Immunity 67, no. 11 (1999): 5815–19. http://dx.doi.org/10.1128/iai.67.11.5815-5819.1999.

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ABSTRACT We have previously reported the construction of an isogenic mutant defective in expression of OmpB1, the TbpB homologue, inMoraxella catarrhalis 7169. In this report, we have extended these studies by constructing and characterizing two new isogenic mutants in this clinical isolate. One mutant is defective in expression of TbpA, and the other mutant is defective in expression of both TbpA and TbpB. These isogenic mutants were confirmed by using PCR analysis, sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and sequencing. In vitro growth studies, comparing all three mutants,

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12

OAKHILL, Jonathan S., Christopher L. JOANNOU, Susan K. BUCHANAN, Andrew R. GORRINGE, and Robert W. EVANS. "Expression and purification of functional recombinant meningococcal transferrin-binding protein A." Biochemical Journal 364, no. 3 (2002): 613–16. http://dx.doi.org/10.1042/bj20020500.

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Pathogenic bacteria of the genus Neisseria have a siderophore-independent iron-uptake system reliant on a direct interaction between the bacterial cell and human transferrin (hTf), a serum protein. In the meningococcus, this uptake system is dependent on two surface-exposed, transferrin-binding proteins (Tbps), TbpA and TbpB. TbpA is highly conserved among meningococcal strains, and is thought to be a porin-like integral protein that functions as a gated channel for the passage of iron into the periplasm. TbpB is more variable in size, lipidated and fully surface-exposed. Given its location on

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13

Lee, Inkyoung, and Robert L. Davies. "Evidence for a common gene pool and frequent recombinational exchange of the tbpBA operon in Mannheimia haemolytica, Mannheimia glucosida and Bibersteinia trehalosi." Microbiology 157, no. 1 (2011): 123–35. http://dx.doi.org/10.1099/mic.0.041236-0.

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The tbpBA operon was sequenced in 42 representative isolates of Mannheimia haemolytica (32), Mannheimia glucosida (6) and Bibersteinia trehalosi (4). A total of 27 tbpB and 20 tbpA alleles were identified whilst the tbpBA operon was represented by 28 unique alleles that could be assigned to seven classes. There were 1566 (34.8 % variation) polymorphic nucleotide sites and 482 (32.1 % variation) variable inferred amino acid positions among the 42 tbpBA sequences. The tbpBA operons of serotype A2 M. haemolytica isolates are, with one exception, substantially more diverse than those of the other

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14

Yu, Rong-hua, Robert A. Bonnah, Samuel Ainsworth, and Anthony B. Schryvers. "Analysis of the Immunological Responses to Transferrin and Lactoferrin Receptor Proteins fromMoraxella catarrhalis." Infection and Immunity 67, no. 8 (1999): 3793–99. http://dx.doi.org/10.1128/iai.67.8.3793-3799.1999.

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ABSTRACT Moraxella catarrhalis expresses surface receptor proteins that specifically bind host transferrin (Tf) and lactoferrin (Lf) in the first step of the iron acquisition pathway. Acute- and convalescent-phase antisera from a series of patients with M. catarrhalis pulmonary infections were tested against Tf and Lf receptor proteins purified from the corresponding isolates. After the purified proteins had been separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and Western blotting, we observed strong reactivity against Tf-binding protein B (TbpB; also called OMP1) and Lf

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15

DeRocco, Amanda J., and Cynthia Nau Cornelissen. "Identification of Transferrin-Binding Domains in TbpB Expressed by Neisseria gonorrhoeae." Infection and Immunity 75, no. 7 (2007): 3220–32. http://dx.doi.org/10.1128/iai.00072-07.

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ABSTRACT The transferrin iron acquisition system of Neisseria gonorrhoeae is necessary for iron uptake from transferrin in the human host and requires the participation of two distinct proteins: TbpA and TbpB. TbpA is a TonB-dependent outer membrane transporter responsible for the transport of iron into the cell. TbpB is a lipid-modified protein, for which a precise role in receptor function has not yet been elucidated. These receptor complex proteins show promise as vaccine candidates; therefore, it is important to identify surface-exposed regions of the proteins required for wild-type functi

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16

Li, Ren Feng, Xiang Qin Tian, Kun Zhao, Jin Qing Jiang, and San Hu Wang. "Web-Based Bioinformatics Analysis of TbpB from Actinobacillus pleuropneumonie L20 Strain." Advanced Materials Research 466-467 (February 2012): 256–61. http://dx.doi.org/10.4028/www.scientific.net/amr.466-467.256.

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The transferring(Tf) receptor from Actinobacillus pleuropneumoniae (App) is comprised of a surface exposed lipoprotein, Tf-binding protein B (TbpB), and an integral outer-membrane protein, Tf-binding protein A (TbpA), both of which are essential for survival in the host, and TbpB is required for the iron acquisition process in vivo. In this study. We analyzed the salient features of the TbpB gene and encoded protein of App L20 strain by bioinformatics tools and highlighted its important biological characterization, which. providing insights into the mechanism of Tf binding and the role of TbpB

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17

Bonnah, Robert A., and Anthony B. Schryvers. "Preparation and Characterization of Neisseria meningitidis Mutants Deficient in Production of the Human Lactoferrin-Binding Proteins LbpA and LbpB." Journal of Bacteriology 180, no. 12 (1998): 3080–90. http://dx.doi.org/10.1128/jb.180.12.3080-3090.1998.

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ABSTRACT Pathogenic members of the family Neisseriaceae produce specific receptors facilitating iron acquisition from transferrin (Tf) and lactoferrin (Lf) of their mammalian host. Tf receptors are composed of two outer membrane proteins, Tf-binding proteins A and B (TbpA and TbpB; formerly designated Tbp1 and Tbp2, respectively). Although only a single Lf-binding protein, LbpA (formerly designated Lbp1), had previously been recognized, we recently identified additional bacterial Lf-binding proteins in the human pathogens Neisseria meningitidis and Moraxella catarrhalis and the bovine pathogen

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18

Noto, Jennifer M., and Cynthia Nau Cornelissen. "Identification of TbpA Residues Required for Transferrin-Iron Utilization by Neisseria gonorrhoeae." Infection and Immunity 76, no. 5 (2008): 1960–69. http://dx.doi.org/10.1128/iai.00020-08.

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ABSTRACT Neisseria gonorrhoeae requires iron for survival in the human host and therefore expresses high-affinity receptors for iron acquisition from host iron-binding proteins. The gonococcal transferrin-iron uptake system is composed of two transferrin binding proteins, TbpA and TbpB. TbpA is a TonB-dependent, outer membrane transporter critical for iron acquisition, while TbpB is a surface-exposed lipoprotein that increases the efficiency of iron uptake. The precise mechanism by which TbpA mediates iron acquisition has not been elucidated; however, the process is distinct from those of char

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Price, Gregory A., Michael W. Russell, and Cynthia Nau Cornelissen. "Intranasal Administration of Recombinant Neisseria gonorrhoeae Transferrin Binding Proteins A and B Conjugated to the Cholera Toxin B Subunit Induces Systemic and Vaginal Antibodies in Mice." Infection and Immunity 73, no. 7 (2005): 3945–53. http://dx.doi.org/10.1128/iai.73.7.3945-3953.2005.

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ABSTRACT The transferrin binding proteins (TbpA and TbpB) comprise the gonococcal transferrin receptor and are considered potential antigens for inclusion in a vaccine against Neisseria gonorrhoeae. Intranasal (IN) immunization has shown promise in development of immunity against sexually transmitted disease pathogens, in part due to the induction of antigen-specific genital tract immunoglobulin A (IgA) and IgG. Conjugation of antigens to the highly immunogenic cholera toxin B subunit (Ctb) enhances antibody responses in the serum and mucosal secretions following IN vaccination. In the current

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Yost-Daljev, Mary Kate, and Cynthia Nau Cornelissen. "Determination of Surface-Exposed, Functional Domains of Gonococcal Transferrin-Binding Protein A." Infection and Immunity 72, no. 3 (2004): 1775–85. http://dx.doi.org/10.1128/iai.72.3.1775-1785.2004.

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ABSTRACT The gonococcal transferrin receptor is composed of two distinct proteins, TbpA and TbpB. TbpA is a member of the TonB-dependent family of integral outer membrane transporters, while TbpB is lipid modified and thought to be peripherally surface exposed. We previously proposed a hypothetical topology model for gonococcal TbpA that was based upon computer predictions and similarity with other TonB-dependent transporters for which crystal structures have been determined. In the present study, the hemagglutinin epitope was inserted into TbpA to probe the surface topology of this protein an

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Lin, Wei, Didier Dalmazzone, Walter Fürst, Anthony Delahaye, Laurence Fournaison, and Pascal Clain. "Thermodynamic properties of semiclathrate hydrates formed from the TBAB+TBPB+water and CO2+TBAB+TBPB+water systems." Fluid Phase Equilibria 372 (June 2014): 63–68. http://dx.doi.org/10.1016/j.fluid.2014.03.026.

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22

Agarwal, Sarika, Carol A. King, Ellen K. Klein, et al. "The Gonococcal Fur-Regulated tbpA and tbpB Genes Are Expressed during Natural Mucosal Gonococcal Infection." Infection and Immunity 73, no. 7 (2005): 4281–87. http://dx.doi.org/10.1128/iai.73.7.4281-4287.2005.

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ABSTRACT Iron is limiting in the human host, and bacterial pathogens respond to this environment by regulating gene expression through the ferric uptake regulator protein (Fur). In vitro studies have demonstrated that Neisseria gonorrhoeae controls the expression of several critical genes through an iron- and Fur-mediated mechanism. While most in vitro experiments are designed to determine the response of N. gonorrhoeae to an exogenous iron concentration of zero, these organisms are unlikely to be exposed to such severe limitations of iron in vivo. To determine if N. gonorrhoeae expresses iron

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23

Lehmann, A. K., A. R. Gorringe, K. M. Reddin, K. West, I. Smith, and A. Halstensen. "Human Opsonins Induced during Meningococcal Disease Recognize Transferrin Binding Protein Complexes." Infection and Immunity 67, no. 12 (1999): 6526–32. http://dx.doi.org/10.1128/iai.67.12.6526-6532.1999.

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ABSTRACT Patient serum opsonins against transferrin binding protein A+B (TbpA+B) complexes from two Neisseria meningitidis strains (K454 and B16B6, with 85- and 68-kDa TbpB, respectively) were quantified by a functional phagocytosis and oxidative burst assay. TbpA+B complexes adsorbed to fluorescent beads were opsonized with individual acute and convalescent sera from 40 patients infected by a variety of meningococcal strains. Flow cytometric quantitation of leukocyte phagocytosis products (PP) demonstrated that disease-induced serum opsonins recognized TbpA+B, and the highest anti-TbpA+B seru

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Rokbi, Bachra, Geneviève Renauld-Mongenie, Michèle Mignon, et al. "Allelic Diversity of the Two Transferrin Binding Protein B Gene Isotypes among a Collection of Neisseria meningitidisStrains Representative of Serogroup B Disease: Implication for the Composition of a Recombinant TbpB-Based Vaccine." Infection and Immunity 68, no. 9 (2000): 4938–47. http://dx.doi.org/10.1128/iai.68.9.4938-4947.2000.

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ABSTRACT The distribution of the two isotypes of tbpB in a collection of 108 serogroup B meningococcal strains belonging to the four major clonal groups associated with epidemic and hyperendemic disease (the ET-37 complex, the ET-5 complex, lineage III, and cluster A4) was determined. Isotype I strains (with a 1.8-kbtbpB gene) was less represented than isotype II strains (19.4 versus 80.6%). Isotype I was restricted to the ET-37 complex strains, while isotype II was found in all four clonal complexes. The extent of the allelic diversity of tbpB in these two groups was studied by PCR restrictio

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Kenney, Christopher D., and Cynthia Nau Cornelissen. "Demonstration and Characterization of a Specific Interaction between Gonococcal Transferrin Binding Protein A and TonB." Journal of Bacteriology 184, no. 22 (2002): 6138–45. http://dx.doi.org/10.1128/jb.184.22.6138-6145.2002.

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ABSTRACT Iron scavenging by Neisseria gonorrhoeae is accomplished by the expression of receptors that are specific for host iron-binding proteins, such as transferrin and lactoferrin. Efficient transferrin-iron acquisition is dependent on the combined action of two proteins, designated TbpA and TbpB. TbpA is a TonB-dependent outer membrane receptor, whereas TbpB is lipid modified and serves to increase the efficiency of transferrin-iron uptake. Both proteins, together or separately, can be isolated from the gonococcal outer membrane by using affinity chromatography techniques. In the present s

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Litt, David J., Helen M. Palmer, and S. Peter Borriello. "Neisseria meningitidis Expressing Transferrin Binding Proteins of Actinobacillus pleuropneumoniae Can Utilize Porcine Transferrin for Growth." Infection and Immunity 68, no. 2 (2000): 550–57. http://dx.doi.org/10.1128/iai.68.2.550-557.2000.

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ABSTRACT Homologous recombination was used to generate a number of mutants of serogroup B Neisseria meningitidis B16B6 with the following characteristics: (i) an inability to bind human or porcine transferrin because of loss of both transferrin binding proteins (Tbp) A and B [strain B16B6(Strr)/tbpA−B−] and (ii) an ability to bind porcine transferrin but not human transferrin [strain B16B6(Strr)/tbpAapBap] due to replacement of the meningococcal Tbp with the Tbp ofActinobacillus pleuropneumoniae. During construction of the B16B6(Strr)/tbpAapBap strain, transformants expressing only TbpA or Tbp

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Reichlen, Matthew J., Katsuhiko S. Murakami, and James G. Ferry. "Functional Analysis of the Three TATA Binding Protein Homologs in Methanosarcina acetivorans." Journal of Bacteriology 192, no. 6 (2010): 1511–17. http://dx.doi.org/10.1128/jb.01165-09.

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ABSTRACT The roles of three TATA binding protein (TBP) homologs (TBP1, TBP2, and TBP3) in the archaeon Methanosarcina acetivorans were investigated by using genetic and molecular approaches. Although tbp2 and tbp3 deletion mutants were readily obtained, a tbp1 mutant was not obtained, and the growth of a conditional tbp1 expression strain was tetracycline dependent, indicating that TBP1 is essential. Transcripts of tbp1 were 20-fold more abundant than transcripts of tbp2 and 100- to 200-fold more abundant than transcripts of tbp3, suggesting that TBP1 is the primary TBP utilized during growth.

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Cash, Devin R., Nicholas Noinaj, Susan K. Buchanan, and Cynthia Nau Cornelissen. "Beyond the Crystal Structure: Insight into the Function and Vaccine Potential of TbpA Expressed by Neisseria gonorrhoeae." Infection and Immunity 83, no. 11 (2015): 4438–49. http://dx.doi.org/10.1128/iai.00762-15.

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ABSTRACTNeisseria gonorrhoeae, the causative agent of the sexually transmitted infection gonorrhea, is not preventable by vaccination and is rapidly developing resistance to antibiotics. However, the transferrin (Tf) receptor system, composed of TbpA and TbpB, is an ideal target for novel therapeutics and vaccine development. Using a three-dimensional structure of gonococcal TbpA, we investigated two hypotheses, i.e., that loop-derived antibodies can interrupt ligand-receptor interactions in the native bacterium and that the loop 3 helix is a critical functional domain. Preliminary loop-derive

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Ekins, Andrew, Fariborz Bahrami, Ada Sijercic, Deborah Maret, and Donald F. Niven. "Haemophilus somnus Possesses Two Systems for Acquisition of Transferrin-Bound Iron." Journal of Bacteriology 186, no. 13 (2004): 4407–11. http://dx.doi.org/10.1128/jb.186.13.4407-4411.2004.

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ABSTRACT Haemophilus somnus strain 649 was found to acquire iron from ovine, bovine, and goat transferrins (Tfs). Expression of Tf receptors, as evaluated by solid-phase binding assays, required the organisms to be grown under iron-restricted conditions in the presence of Tf. Competition binding assays revealed the presence of two distinct Tf-binding receptor systems, one specific for bovine Tf and the other capable of binding all three ruminant Tfs. Affinity isolation procedures using total membranes yielded three putative bovine Tf-binding polypeptides and one putative ovine and goat Tf-bind

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Sims, Kurtis L., and Anthony B. Schryvers. "Peptide-Peptide Interactions between Human Transferrin and Transferrin-Binding Protein B from Moraxellacatarrhalis." Journal of Bacteriology 185, no. 8 (2003): 2603–10. http://dx.doi.org/10.1128/jb.185.8.2603-2610.2003.

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ABSTRACT Transferrin-binding protein B (TbpB) is one component of a bipartite receptor in several gram-negative bacterial species that binds host transferrin and mediates the uptake of iron for growth. Transferrin and TbpB are both bilobed proteins, and the interaction between these proteins seems to involve similar lobe-lobe interactions. Synthetic overlapping peptide libraries representing the N lobe of TbpB from Moraxella catarrhalis were prepared and probed with labeled human transferrin. Transferrin-binding peptides were localized to six different regions of the TbpB N lobe, and reciproca

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Masri, Heather P., and Cynthia Nau Cornelissen. "Specific Ligand Binding Attributable to Individual Epitopes of Gonococcal Transferrin Binding Protein A." Infection and Immunity 70, no. 2 (2002): 732–40. http://dx.doi.org/10.1128/iai.70.2.732-740.2002.

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ABSTRACT The gonococcal transferrin receptor complex comprises two iron-regulated proteins, TbpA and TbpB. TbpA is essential for transferrin-iron uptake and is a TonB-dependent integral outer membrane protein. TbpB is thought to increase the efficiency of iron uptake from transferrin and is lipid modified and surface exposed. To evaluate the structure-function relationships in one of the components of the receptor, TbpA, we created constructs that fused individual putative loops of TbpA with amino-terminal affinity tags. The recombinant proteins were then overexpressed in Escherichia coli, and

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Thomas, Christopher E., Weiyan Zhu, Cornelius N. Van Dam, Nancy L. Davis, Robert E. Johnston, and P. Frederick Sparling. "Vaccination of Mice with Gonococcal TbpB Expressed In Vivo from Venezuelan Equine Encephalitis Viral Replicon Particles." Infection and Immunity 74, no. 3 (2006): 1612–20. http://dx.doi.org/10.1128/iai.74.3.1612-1620.2006.

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ABSTRACT We investigated the immunogenicity of gonococcal transferrin binding protein B (TbpB) expressed with and without a eukaryotic secretion signal from a nonpropagating Venezuelan equine encephalitis virus replicon particle (VRP) delivery system. TbpB was successfully expressed in baby hamster kidney (BHK) cells, and the presence of the eukaryotic secretion signal not only apparently increased the protein's expression but also allowed for extracellular localization and glycosylation. Mice immunized with VRPs produced significant amounts of serum antibody although less than the amounts pro

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Mistretta, Noëlle, Bruno Guy, Yves Bérard, et al. "Improvement of Immunogenicity of Meningococcal Lipooligosaccharide by Coformulation with Lipidated Transferrin-Binding Protein B in Liposomes: Implications for Vaccine Development." Clinical and Vaccine Immunology 19, no. 5 (2012): 711–22. http://dx.doi.org/10.1128/cvi.05683-11.

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ABSTRACTAmong various meningococcal antigens, lipooligosaccharide (LOS) and recombinant lipidated transferrin-binding protein B (rlip-TbpB) are considered to be putative vaccine candidates against group BNeisseria meningitidis. In the present work, we report the development of a new liposome-based vaccine formulation containing both rlip-TbpB and L8 LOS. The endotoxic activity of the liposomal LOS was evaluatedin vitrousing theLimulusAmebocyte Lysate assay and compared to the endotoxic activity of free LOS. Above a 250:1 lipid/LOS molar ratio, liposomes were shown to effectively detoxify the L

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Lv, Jia Yu, Shuiai Wei, Wang Hua Chen, Gu Feng Chen, Li Ping Chen, and Ying Tao Tian. "Thermal Kinetic Analysis of Tert-butyl Peroxybenzoate under Dynamic and Adiabatic Conditions." Advanced Materials Research 550-553 (July 2012): 2782–85. http://dx.doi.org/10.4028/www.scientific.net/amr.550-553.2782.

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This study demonstrates the thermal actions of tert-butyl peroxybenzoate (TBPB) which is widely used in the plastic and rubber industries. The thermodynamic and kinetic analysis were performed on the basis of dynamic and adiabatic calorimetric applications which had been accepted as good assistants for investigating materials’ thermal decomposition. In essence, TBPB is reactive and exothermically unstable. Differential scanning calorimetry (DSC) and accelerating rate calorimeter (ARC) were employed to supply basic data and safety index. Experiments were taken under different scanning rates as

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Tonpitak, Walaiporn, Svenja Thiede, Winfried Oswald, Nina Baltes, and Gerald-F. Gerlach. "Actinobacillus pleuropneumoniae Iron Transport: a Set of exbBD Genes Is Transcriptionally Linked to the tbpB Gene and Required for Utilization of Transferrin-Bound Iron." Infection and Immunity 68, no. 3 (2000): 1164–70. http://dx.doi.org/10.1128/iai.68.3.1164-1170.2000.

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ABSTRACT Upon iron restriction, Actinobacillus pleuropneumoniaehas been shown to express the transferrin-binding proteins TbpB and TbpA, both of which have been implied to be important virulence factors. In order to identify additional iron-regulated proteins, we cloned and analyzed the region upstream of the transferrin-binding protein genes in an A. pleuropneumoniae serotype 7 strain. We located immediately upstream of the tbpB gene two open reading frames which were 43% homologous to the neisserial ExbBD protein genes. By raising specific antibodies, we showed that ExbB is expressed under i

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Frandoloso, Rafael, Sonia Martínez-Martínez, Charles Calmettes, et al. "Nonbinding Site-Directed Mutants of Transferrin Binding Protein B Exhibit Enhanced Immunogenicity and Protective Capabilities." Infection and Immunity 83, no. 3 (2014): 1030–38. http://dx.doi.org/10.1128/iai.02572-14.

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Host-adapted Gram-negative bacterial pathogens from thePasteurellaceae,Neisseriaceae, andMoraxellaceaefamilies normally reside in the upper respiratory or genitourinary tracts of their hosts and rely on utilizing iron from host transferrin (Tf) for growth and survival. The surface receptor proteins that mediate this critical iron acquisition pathway have been proposed as ideal vaccine targets due to the critical role that they play in survival and disease pathogenesisin vivo. In particular, the surface lipoprotein component of the receptor, Tf binding protein B (TbpB), had received considerabl

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Coppens, Isabelle, Sylvie Alonso, Rudy Antoine, et al. "Production of Neisseria meningitidisTransferrin-Binding Protein B by RecombinantBordetella pertussis." Infection and Immunity 69, no. 9 (2001): 5440–46. http://dx.doi.org/10.1128/iai.69.9.5440-5446.2001.

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ABSTRACT Neisseria meningitidis serogroup B infections are among the major causes of fulminant septicemia and meningitis, especially severe in young children, and no broad vaccine is available yet. Because of poor immunogenicity of the serogroup B capsule, many efforts are now devoted to the identification of protective protein antigens. Among those are PorA and, more recently, transferrin-binding protein B (TbpB). In this study, TbpB of N. meningitidiswas genetically fused to the N-terminal domain of the Bordetella pertussis filamentous hemagglutinin (FHA), and thefha-tbpB hybrid gene was exp

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Pintor, M., J. A. Gomez, L. Ferron, C. M. Ferreiros, and M. T. Criado. "Analysis of TbpA and TbpB functionality in defective mutants of Neisseria meningitidis." Journal of Medical Microbiology 47, no. 9 (1998): 757–60. http://dx.doi.org/10.1099/00222615-47-9-757.

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Ogunnariwo, Julius A., and Anthony B. Schryvers. "Characterization of a Novel Transferrin Receptor in Bovine Strains of Pasteurella multocida." Journal of Bacteriology 183, no. 3 (2001): 890–96. http://dx.doi.org/10.1128/jb.183.3.890-896.2001.

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ABSTRACT Analysis of bovine respiratory isolates of Pasteurella multocida demonstrated that six of nine strains tested were capable of growth dependent upon bovine transferrin and of specifically binding ruminant transferrins. A single 82-kDa protein was affinity isolated from the P. multocida strains with immobilized bovine transferrin. In contrast to what has been observed in other species, binding of this protein to immobilized transferrin was specifically blocked by the N-lobe subfragment of bovine transferrin. A single gene encoding the 82-kDa protein was flanked by a leucyl-tRNA syntheta

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Renauld-Mongénie, Geneviève, Laurence Lins, Tino Krell, et al. "Transferrin-Binding Protein B of Neisseria meningitidis: Sequence-Based Identification of the Transferrin-Binding Site Confirmed by Site-Directed Mutagenesis." Journal of Bacteriology 186, no. 3 (2004): 850–57. http://dx.doi.org/10.1128/jb.186.3.850-857.2004.

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ABSTRACT A sequence-based prediction method was employed to identify three ligand-binding domains in transferrin-binding protein B (TbpB) of Neisseria meningitidis strain B16B6. Site-directed mutagenesis of residues located in these domains has led to the identification of two domains, amino acids 53 to 57 and 240 to 245, which are involved in binding to human transferrin (htf). These two domains are conserved in an alignment of different TbpB sequences from N. meningitidis and Neisseria gonorrhoeae, indicating a general functional role of the domains. Western blot analysis and BIAcore and iso

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Lin, Chun Ping, Yi Ming Chang, Jo Ming Tseng, and Mei Li You. "Comparison of the Isothermal and Non-Isothermal Kinetics for Predicting the Thermal Hazard of Tert-Butyl Peroxybenzoate." Advanced Materials Research 328-330 (September 2011): 124–27. http://dx.doi.org/10.4028/www.scientific.net/amr.328-330.124.

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Tert-butyl peroxybenzoate (TBPB), a liquid organic peroxide, has been widely employed in the petrifaction industry as a polymerization formation agent. This study investigated the thermokinetic parameters of TBPB by isothermal kinetic algorithms and non-isothermal kinetic equations, using thermal activity monitor III (TAM III) and differential scanning calorimetry (DSC), respectively. Simulations of 0.5 L, 25 kg, 55 gallon, and 400 kg reactors in liquid thermal explosion models were performed. It is based on the thermal hazard properties, such as the heat of decomposition (∆Hd), activation ene

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Mayoufi, Nadia, Didier Dalmazzone, Anthony Delahaye, Pascal Clain, Laurence Fournaison, and Walter Fürst. "Experimental Data on Phase Behavior of Simple Tetrabutylphosphonium Bromide (TBPB) and Mixed CO2+ TBPB Semiclathrate Hydrates." Journal of Chemical & Engineering Data 56, no. 6 (2011): 2987–93. http://dx.doi.org/10.1021/je2003918.

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Potter, Andrew A., Anthony B. Schryvers, Julius A. Ogunnariwo, Wendy A. Hutchins, Reggie Y. C. Lo, and Trent Watts. "Protective capacity of the Pasteurella haemolytica transferrin-binding proteins TbpA and TbpB in cattle." Microbial Pathogenesis 27, no. 4 (1999): 197–206. http://dx.doi.org/10.1006/mpat.1999.0297.

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Fukumoto, Ayako, Patrice Paricaud, Didier Dalmazzone, Wassila Bouchafaa, Thi Thu-Suong Ho, and Walter Fürst. "Modeling the Dissociation Conditions of Carbon Dioxide + TBAB, TBAC, TBAF, and TBPB Semiclathrate Hydrates." Journal of Chemical & Engineering Data 59, no. 10 (2014): 3193–204. http://dx.doi.org/10.1021/je500243k.

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Webb, Dianne C., and Allan W. Cripps. "Immunization with Recombinant Transferrin Binding Protein B Enhances Clearance of Nontypeable Haemophilus influenzae from the Rat Lung." Infection and Immunity 67, no. 5 (1999): 2138–44. http://dx.doi.org/10.1128/iai.67.5.2138-2144.1999.

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ABSTRACT Nontypeable Haemophilus influenzae (NTHI) is an opportunistic pathogen, and heterogeneity in the surface-exposed immunodominant domains of NTHI proteins is thought to be associated with the failure of an infection to stimulate an immune response that is cross-protective against heterologous NTHI strains. The aim of this study was to assess the vaccine potential of a surface-exposed component of the NTHI human transferrin receptor, TbpB, and to determine if the antibody response elicited was cross-reactive with heterologous strains of NTHI. The efficacy of immunization with a recombina

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Ostan, N., A. Morgenthau, R. H. Yu, S. D. Gray-Owen, and A. B. Schryvers. "A comparative, cross-species investigation of the properties and roles of transferrin- and lactoferrin-binding protein B from pathogenic bacteria." Biochemistry and Cell Biology 95, no. 1 (2017): 5–11. http://dx.doi.org/10.1139/bcb-2016-0055.

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Pathogenic bacteria from the families Neisseriaeceae and Moraxellaceae acquire iron from their host using surface receptors that have the ability to hijack iron from the iron-sequestering host proteins transferrin (Tf) and lactoferrin (Lf). The process of acquiring iron from Tf has been well-characterized, including the role of the surface lipoprotein transferrin-binding protein B (TbpB). In contrast, the only well-defined role for the homologue, LbpB, is in its protection against cationic antimicrobial peptides, which is mediated by regions present in some LbpBs that are highly enriched in gl

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Cornelissen, Cynthia Nau, James E. Anderson, Ian C. Boulton, and P. Frederick Sparling. "Antigenic and Sequence Diversity in Gonococcal Transferrin-Binding Protein A." Infection and Immunity 68, no. 8 (2000): 4725–35. http://dx.doi.org/10.1128/iai.68.8.4725-4735.2000.

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ABSTRACT Neisseria gonorrhoeae is a gram-negative pathogen that is capable of satisfying its iron requirement with human iron-binding proteins such as transferrin and lactoferrin. Transferrin-iron utilization involves specific binding of human transferrin at the cell surface to what is believed to be a complex of two iron-regulated, transferrin-binding proteins, TbpA and TbpB. The genes encoding these proteins have been cloned and sequenced from a number of pathogenic, gram-negative bacteria. In the current study, we sequenced four additional tbpA genes from other N. gonorrhoeaestrains to begi

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Zhou, Nengneng, Meixia Wu, Man Zhang, Xiaoqiang Zhou, and Wei Zhou. "TBPB-initiated cascade cyclization of 3-arylethynyl-[1,1′-biphenyl]-2-carbonitriles with sulfinic acids: access to sulfone-containing cyclopenta[gh]phenanthridines." Organic & Biomolecular Chemistry 18, no. 9 (2020): 1733–37. http://dx.doi.org/10.1039/d0ob00119h.

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de la Puente-Redondo, Víctor A., Noemí García del Blanco, César B. Gutiérrez-Martín, Jesús Navas Méndez, and Elías F. Rodríguez Ferri. "Detection and subtyping of Actinobacillus pleuropneumoniae strainsby PCR-RFLP analysis of the tbpA and tbpB genes." Research in Microbiology 151, no. 8 (2000): 669–81. http://dx.doi.org/10.1016/s0923-2508(00)00135-2.

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Li, Zheng, Dong-Liang Zhong, Wei-Yan Zheng, Jin Yan, Yi-Yu Lu, and Da-Tong Yi. "Morphology and kinetic investigation of TBAB/TBPB semiclathrate hydrates formed with a CO2 + CH4 gas mixture." Journal of Crystal Growth 511 (April 2019): 79–88. http://dx.doi.org/10.1016/j.jcrysgro.2019.01.042.

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