トランスフェリン結合タンパク質A

WordNet

executed with proper legal authority; "a binding contract"
the protective covering on the front, back, and spine of a book; "the book had a leather binding" (同)book binding, cover, back
strip sewn over or along an edge for reinforcement or decoration
the capacity to attract and hold something
any of a large group of nitrogenous organic compounds that are essential constituents of living cells; consist of polymers of amino acids; essential in the diet of animals for growth and for repair of tissues; can be obtained from meat and eggs and milk and legumes; "a diet high in protein"
the 1st letter of the Roman alphabet (同)a
the blood group whose red cells carry the A antigen (同)type_A, group A
a globulin in blood plasma that carries iron (同)beta_globulin, siderophilin

PrepTutorEJDIC

義務的な,拘束力ある / 〈U〉しばること;〈C〉しばる物 / 〈C〉製本,装丁 / 〈U〉縁(‘ふち')取り材料
蛋白(たんばく)質
answer / ampere

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1. 鉄のバランス調節 regulation of iron balance
2. 鉄欠乏性貧血の原因および診断 causes and diagnosis of anemia due to iron deficiency
3. 慢性疾患の貧血（慢性炎症時の貧血） anemia of chronic disease anemia of chronic inflammation
4. 末期腎不全における栄養状態の評価 assessment of nutritional status in end stage renal disease
5. BおよびTリンパ球の正常な発生 normal b and t lymphocyte development

English Journal

Cross-protective efficacy of recombinant transferrin-binding protein A of Haemophilus parasuis in guinea pigs.

Huang X, Li Y, Fu Y, Ji Y, Lian K, Zheng H, Wei J, Cai X, Zhu Q.Author information State Key Laboratory of Veterinary Etiological Biology, Lanzhou Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Lanzhou, People's Republic of China.AbstractThe causative agent of Glasser's disease in swine is Haemophilus parasuis. Commercial bacterins are widely used for protection of the swine population. However, cross protection is limited because H. parasuis has more than 15 serovars. Transferrin-binding protein A has shown potential as a broad-spectrum vaccine candidate against homologous and heterologous strains. Here we amplified the full-length tbpA gene from an H. parasuis serovar 13 isolate and cloned it into a pET-SUMO expression vector. We then expressed and purified the TbpA protein by Ni affinity chromatography. First, the immunogenicity and protective efficacy of the protein were evaluated in guinea pigs by two subcutaneous immunizations with different doses of Montanide IMS 206 VG adjuvant. The immunized guinea pigs were, respectively, challenged on week 3 after a booster immunization with homologous strain LJ3 (serovar 13) and heterologous strain FX1 (serovar 4), and vaccine-inoculated groups were compared with nonvaccinated controls. All immunized groups showed serum antibody titers higher than those of negative-control groups. Furthermore, the cytokine and chemokine levels were evaluated at the transcriptional level by the real-time PCR analysis of six cytokines and chemokines. Gamma interferon and interleukin-5 in groups immunized with 100 μg were elevated more than 15-fold over those in negative-control groups. The protection rates were 80 and 60% after a challenge with strains LJ3 and FX1, respectively, in the groups vaccinated with 100 μg of recombinant TbpA protein. Subsequently, the data showed that guinea pigs immunized with a single dose (100 μg) were protected at levels of 80, 80, and 60% against LJ3, FX1, and another heterologous strain, SZ (serovar 14), respectively. The results indicate for the first time that TbpA protein cross protects guinea pigs against serovars 13, 4, and 14 of H. parasuis. Taken together, these results suggest that the recombinant TbpA protein is a promising vaccine candidate that needs to be confirmed in a swine population.
Clinical and vaccine immunology : CVI.Clin Vaccine Immunol.2013 Jun;20(6):912-9. doi: 10.1128/CVI.00621-12. Epub 2013 Apr 24.
The causative agent of Glasser's disease in swine is Haemophilus parasuis. Commercial bacterins are widely used for protection of the swine population. However, cross protection is limited because H. parasuis has more than 15 serovars. Transferrin-binding protein A has shown potential as a broad-spe
PMID 23616407

Steric and allosteric factors prevent simultaneous binding of transferrin-binding proteins A and B to transferrin.

Silva LP, Yu RH, Calmettes C, Yang X, Moraes TF, Schriemer DC, Schryvers AB.Author information Department of Biochemistry and Molecular Biology, University of Calgary, Canada.AbstractThe 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 present study we have mapped the effect of TbpA from Actinobacillus pleuropneumoniae on pTf (porcine Tf) using H/DX-MS (hydrogen/deuterium exchange coupled to MS) and compare it with a previously determined binding site for TbpB. The proposed TbpA footprint is adjacent to and potentially overlapping the TbpB-binding site, and induces a structural instability in the TbpB site. This suggests that simultaneous binding to pTf by both receptors would be hindered. We demonstrate that a recombinant TbpB lacking a portion of its anchor peptide is unable to form a stable ternary TbpA-pTf-TbpB complex. This truncated TbpB does not bind to a preformed Tf-TbpA complex, and TbpA removes pTf from a preformed Tf-TbpB complex. Thus the results of the present study support a model whereby TbpB 'hands-off' pTf to TbpA, which completes the iron removal and transport process.
The Biochemical journal.Biochem J.2012 Jun 1;444(2):189-97. doi: 10.1042/BJ20112133.
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 su
PMID 22369045

Evidence of Fe3+ interaction with the plug domain of the outer membrane transferrin receptor protein of Neisseria gonorrhoeae: implications for Fe transport.

Banerjee S, Siburt CJ, Mistry S, Noto JM, DeArmond P, Fitzgerald MC, Lambert LA, Cornelissen CN, Crumbliss AL.Author information Department of Chemistry, Duke University, Durham, NC-27708-0346, USA.AbstractNeisseria gonorrhoeae is an obligate pathogen that hijacks iron from the human iron transport protein, holo-transferrin (Fe(2)-Tf), by expressing TonB-dependent outer membrane receptor proteins, TbpA and TbpB. Homologous to other TonB-dependent outer membrane transporters, TbpA is thought to consist of a β-barrel with an N-terminal plug domain. Previous reports by our laboratories show that the sequence EIEYE in the plug domain is highly conserved among various bacterial species that express TbpA and plays a crucial role in iron utilization for gonococci. We hypothesize that this highly conserved EIEYE sequence in the TbpA plug, rich in hard oxygen donor groups, binds with Fe(3+) through the transport process across the outer membrane through the β-barrel. Sequestration of Fe(3+) by the TbpA-plug supports the paradigm that the ferric iron must always remain chelated and controlled throughout the transport process. In order to test this hypothesis here we describe the ability of both the recombinant wild-type plug, and three small peptides that encompass the sequence EIEYE of the plug, to bind Fe(3+). This is the first report of the expression/isolation of the recombinant wild-type TbpA plug. Although CD and SUPREX spectroscopies suggest that a non-native structure is observed for the recombinant plug, fluorescence quenching titrations indicate that the wild-type recombinant TbpA plug binds Fe (3+) with a conditional log K(d) = 7 at pH 7.5, with no evidence of binding at pH 6.3. A recombinant TbpA plug with mutated sequence (NEIEYEN → NEIAAAN) shows no evidence of Fe(3+) binding under our experimental set up. Interestingly, in silico modeling with the wild-type plug also predicts a flexible loop structure for the EIEYE sequence under native conditions which once again supports the Fe(3+) binding hypothesis. These in vitro observations are consistent with the hypothesis that the EIEYE sequence in the wild-type TbpA plug binds Fe(3+) during the outer membrane transport process in vivo.
Metallomics : integrated biometal science.Metallomics.2012 Apr;4(4):361-72. doi: 10.1039/c2mt20037f. Epub 2012 Mar 8.
Neisseria gonorrhoeae is an obligate pathogen that hijacks iron from the human iron transport protein, holo-transferrin (Fe(2)-Tf), by expressing TonB-dependent outer membrane receptor proteins, TbpA and TbpB. Homologous to other TonB-dependent outer membrane transporters, TbpA is thought to consist
PMID 22399131

Japanese Journal

The expression of transferrin binding protein in the turtle nervous system

PARK Sang Wook,LEE Ha Na,JEON Gye Sun,SIM Ki-Bum,CHO Ik-Hyun,CHO Sa Sun
Archives of histology and cytology 72(1), 65-76, 2009-07-01
NAID 10025868122

The expression of transferrin binding protein in the turtle nervous system

Park Sang Wook,Lee Ha Na,Jeon Gye Sun,Sim Ki-Bum,Cho Ik-Hyun,Cho Sa Sun
Archives of Histology and Cytology 72(1), 65-76, 2009
… Transferrin binding protein (TfBP) is a cytoplasmic glycoprotein that was originally isolated from the chick oviduct. …
NAID 130004462727

Actinobacillus pleuropneumoniaeトランスフェリン結合蛋白Bを気管内投与した子豚におけるキトサンによる粘膜抗体および血中抗体産生促進作用

Kim Tae Jung,Kim Kwang Hyun,Lee Jae Il
The journal of veterinary medical science 69(5), 535-539, 2007-05-25
Actinobacillus pleuropneumoniae組換えトランスフェリン結合蛋白B(rTbp B)を子豚気管内に投与し,キトサンの粘膜抗体および血中抗体産生に対するアジュバント効果を検討した.肺洗浄液および肺乳剤抽出液中の分泌型IgA量を測定したところ,キトサンは粘膜免疫応答を促進することが示された.また,血清中のIgG測定により,全身免疫が促進されることも明らかとなった.
NAID 110006273255