Immunoglobulin Binding

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Chad M. Rienstra - One of the best experts on this subject based on the ideXlab platform.

  • Automated protein resonance assignments of magic angle spinning solid-state NMR spectra of β1 Immunoglobulin Binding domain of protein G (GB1)
    Journal of Biomolecular NMR, 2010
    Co-Authors: Hunter N. B. Moseley, Lindsay J. Sperling, Chad M. Rienstra
    Abstract:

    Magic-angle spinning solid-state NMR (MAS SSNMR) represents a fast developing experimental technique with great potential to provide structural and dynamics information for proteins not amenable to other methods. However, few automated analysis tools are currently available for MAS SSNMR. We present a methodology for automating protein resonance assignments of MAS SSNMR spectral data and its application to experimental peak lists of the β1 Immunoglobulin Binding domain of protein G (GB1) derived from a uniformly ^13C- and ^15N-labeled sample. This application to the 56 amino acid GB1 produced an overall 84.1% assignment of the N, CO, CA, and CB resonances with no errors using peak lists from NCACX 3D, CANcoCA 3D, and CANCOCX 4D experiments. This proof of concept demonstrates the tractability of this problem.

  • magic angle spinning solid state nmr spectroscopy of the β1 Immunoglobulin Binding domain of protein g gb1 15n and 13c chemical shift assignments and conformational analysis
    Journal of the American Chemical Society, 2005
    Co-Authors: Trent W Franks, Chad M. Rienstra, Donghua H Zhou, Benjamin J Wylie, Brian G Money, Daniel T Graesser, Heather L Frericks, Gurmukh Sahota
    Abstract:

    Magic-angle spinning solid-state NMR (SSNMR) studies of the β1 Immunoglobulin Binding domain of protein G (GB1) are presented. Chemical shift correlation spectra at 11.7 T (500 MHz 1H frequency) were employed to identify signals specific to each amino acid residue type and to establish backbone connectivities. High sensitivity and resolution facilitated the detection and assignment of every 15N and 13C site, including the N-terminal (M1) 15NH3, the C-terminal (E56) 13C‘, and side-chain resonances from residues exhibiting fast-limit conformational exchange near room temperature. The assigned spectra lend novel insight into the structure and dynamics of microcrystalline GB1. Secondary isotropic chemical shifts report on conformation, enabling a detailed comparison of the microcrystalline state with the conformation of single crystals and the protein in solution; the consistency of backbone conformation in these three preparations is the best among proteins studied so far. Signal intensities and line widths ...

Tamara F. Solov'eva - One of the best experts on this subject based on the ideXlab platform.

  • Chaperone and Immunoglobulin-Binding Activities of Skp Protein from Yersinia pseudotuberculosis.
    Biochemistry, 2020
    Co-Authors: E. V. Sidorin, V. A. Khomenko, Tamara F. Solov'eva
    Abstract:

    : Here, we determined qualitative and quantitative characteristics of the chaperone and Immunoglobulin-Binding activities of recombinant Skp protein (rSkp) from Yersinia pseudotuberculosis using the methods of dynamic light scattering and surface plasmon resonance. Commercial human polyclonal IgG and Fc and Fab fragments of human IgG were used as substrate proteins. The activity of rSkp strongly depended on the medium pH. The most stable low-molecular-weight complexes with a hydrodynamic radius up to 10 nm were formed by rSkp and protein substrates at acidic pH values. Under these conditions, rSkp exhibited the lowest propensity to self-association and the highest affinity for human IgG and its Fc and Fab fragments, as well as prevented their aggregation most efficiently (i.e., demonstrated the maximal chaperone activity). As the medium pH increased, the affinity of rSkp for IgG and its fragments decreased; rSkp was not able to completely prevent the aggregation of protein substrates, but significantly slowed it down. The obtained information may be of practical interest, since the stability of therapeutic IgG preparations affects their safety and efficacy in medical applications.

  • Chaperone activity of Immunoglobulin-Binding protein from Yersinia pseudotuberculosis
    Biochemistry (moscow) Supplement Series A: Membrane and Cell Biology, 2015
    Co-Authors: E. V. Sidorin, O. V. Sidorova, N. M. Tischenko, V. A. Khomenko, Olga D. Novikova, Tamara F. Solov'eva
    Abstract:

    The chaperone activity of the Yersinia pseudotuberculosis Immunoglobulin-Binding protein Skp has been studied. Its ability to bind the unfolded proteins of the bacterial outer membrane (OMP) was found by means of Western blotting using peroxidase-labeled Skp. Using dynamic light scattering, we have shown that Skp exerts an inhibitory effect on the aggregation of unfolded recombinant OmpF, which occurs after a 10-fold dilution of the porin solution. The results obtained demonstrate that Skp prevents OMP aggregation in aqueous solutions in the absence of detergents.

  • Isolation and characterization of a low-molecular-weight Immunoglobulin-Binding protein from Yersinia pseudotuberculosis.
    Biochemistry, 2006
    Co-Authors: E. V. Sidorin, G. A. Naberezhnykh, Pavel S. Dmitrenok, E. V. Leichenko, Stanislav D. Anastyuk, Tamara F. Solov'eva
    Abstract:

    A low-molecular-weight Immunoglobulin-Binding protein (IBP) bound with the cell envelope has been isolated from Yersinia pseudotuberculosis cells and partially characterized. This IBP is a hydrophilic protein with a high polarity index of 55.3%. The molecular weight of the protein has been determined by MALDI-TOF mass spectrometry as 14.3 kD. CD spectroscopy showed that the IBP has high contents of the β-structure and random coil structure. The IBP contains glycine as the N-terminal amino acid. The protein can be stored for a long time at acidic pH values but aggregates and loses activity at alkaline and neutral pH. The IBP binds rabbit IgG with optimum at pH of 6.0–7.5. The IBP interacts with IgG molecule in the Fc-fragment region. The protein retains activity after heating at 100°C in the presence of SDS.

  • Isolation and characterization of the Immunoglobulin-Binding protein from Yersinia pseudotuberculosis.
    Biochemistry, 2002
    Co-Authors: G. A. Naberezhnykh, E. V. Sidorin, Pavel S. Dmitrenok, Tamara F. Solov'eva
    Abstract:

    A high molecular weight Immunoglobulin-Binding protein localized on the surface of bacterial cells has been isolated from the protein fraction of the outer membrane of Yersinia pseudotuberculosis, and its properties are described. The Immunoglobulin-Binding protein is a trypsin-resistant and temperature-sensitive β-structured protein. As shown by MALDI-TOF mass spectrometry, after heating at 100°C the molecular weight of the protein constituted 37.5 kD. The native protein is capable of interacting with human and rabbit IgG but looses the ability to bind the Immunoglobulins after the temperature denaturation. The Immunoglobulin-Binding protein binds to the Fc-fragments of the Immunoglobulins and Binding depends on the presence of calcium ions.

Masaharu Kamada - One of the best experts on this subject based on the ideXlab platform.

  • Hormonal control of mRNA expression of Immunoglobulin Binding factor in uterine cervix.
    Biochemical and Biophysical Research Communications, 2000
    Co-Authors: Shuji Yoshikawa, Masaharu Kamada, Masahiko Maegawa, Toshihiro Aono, Satoshi Yamamoto, Hiroshi Kido, Minoru Irahara, Shuji Yamano, Samuel S. Koide
    Abstract:

    Uterine cervical mucus contains an Immunoglobulin Binding factor (IgBF). It may play a role in preventing antibody production against sperm in the female reproductive tract. To elucidate the mechanism involved in the production of activated IgBF, we determined the effects of hormones on the expression of mRNAs of IgBF and of protein disulfide isomerase (PDI), activating enzyme, in uterine cervix by quantitative RT-PCR. The uterine cervices of female rats were excised at preovulatory, ovulatory, and postovulatory phases. The human uterine cervical adenocarcinoma cells (TCO-2) were cultured for 24 h in serum-free medium containing 17β-estradiol or progesterone. Expression of IgBF and PDI mRNAs was significantly highest during the ovulatory phase. 17β-estradiol stimulated the expression of both mRNAs in TCO-2; whereas progesterone was ineffective. In conclusion, estrogen regulates the production of IgBF by the endocervix and PDI in vivo, thereby increasing the level of activated IgBF in the female reproductive tract during the ovulatory phase, allowing sperm to enter the uterine cavity.

  • Characterization of Immunoglobulin Binding factor in sputum from patients with chronic airway diseases.
    Respirology, 1999
    Co-Authors: Waka Ichikawa, Masaharu Kamada, Fumitaka Ogushi, Kenji Tani, Koji Maniwa, Yasukazu Ohmoto, Mitsunori Sakatani, Saburo Sone
    Abstract:

    Objective: Immunoglobulin Binding factor (IgBF) is known to bind Immunoglobulin, to interact with anti-Fcγ-III antibodies and to be present in the lower respiratory tract of normal healthy subjects. In this study, in order to clarify the role of IgBF in vespiratory diseases, we investigated whether IgBF exists in the airway of patients with chronic airway diseases. Methodology: IgBF was measured in the sputum of 28 normal subjects and 59 patients with chronic airway diseases including 37 cases of chronic bronchitis, 18 bronchiectasis, and four diffuse panbronchiolitis by enzyme-linked immunosorbent assay. Results: Immunoglobulin Binding factor concentration in the sputum of patients with chronic airway diseases (purulent sputum, 50.2 ± 8.2 μg/mL; mucoid sputum, 88.6 ± 12.8 μg/mL) was higher than that in induced sputum of normal subjects (6.3 ± 5.5 μg/mL; P < 0.001). Immunoglobulin Binding factor level in mucoid sputum was significantly higher than that in purulent sputum (P < 0.05). A significant inverse correlation was shown between the IgBF level and the elastase activity in sputum, and the concentration of IgBF purified from seminal plasma was decreased by treatment with neutrophil elastase, indicating that IgBF might be degraded by elastase. In the gel filtration chromatography of both types of sputum, IgBF was eluted in a region corresponding to a molecular weight of 27 kDa as a single peak. Western blot analysis with a monoclonal antibody to IgBF indicated that IgBF in both types of sputum had a molecular weight of 27 kDa under non-reducing conditions and of 16 kDa under reducing conditions. Conclusion: These results demonstrate that a high level of IgBF is present in the respiratory tract of patients with chronic airway diseases and may be related to the pathogenesis of these diseases.

  • β-Microseminoprotein/prostatic secretory protein is a member of Immunoglobulin Binding factor family
    Biochimica et Biophysica Acta, 1998
    Co-Authors: Masaharu Kamada, Masahiko Maegawa, N. Maeda, Toshihiro Aono, H. Mori, Satoshi Yamamoto, Shiroh Futaki, Kotaro Kunimi, Masaya Takikawa, Samuel S. Koide
    Abstract:

    Abstract Human seminal plasma contains a factor that binds human IgG, designated as Immunoglobulin Binding factor (IgBF). Under reducing condition IgBF interacts with anti-Leu-11b, a murine monoclonal antibody raised against human FcγRIII/CD16. IgBF shows no Binding activity under non-reducing condition. Three components having IgBF activity were separated by HPLC and their amino acid sequences determined. The main IgBF showed structural identity to β-microseminoprotein (β-MSP), prostatic secretory protein of 94 amino acids (PSP94) and β-inhibin. The slight variation in the reported sequences of these proteins has been attributed to analytical error. In the present study the molecular masses of main IgBF and β-MSP/PSP94 were found to be identical by mass spectrometry. In addition, a large component of IgBF and a shorter β-MSP consisting of 93 amino acids were identified. The Binding of β-MSP for human IgG and anti-Leu-11b antibody is demonstrable only under reducing condition, determined by Western blot analysis. The present data clearly show that IgBF is a family composed of at least three isoforms. One of the members is β-MSP/PSP94. This family should be designated as IgBF.

  • Enzymatic Activation of Immunoglobulin Binding Factor in Female Reproductive Tract
    Biochemical and Biophysical Research Communications, 1998
    Co-Authors: H. Mori, Masaharu Kamada, Masahiko Maegawa, Toshihiro Aono, Satoshi Yamamoto, Shiroh Futaki, Mihiro Yano, Hiroshi Kido, Samuel S. Koide
    Abstract:

    Abstract Human seminal plasma and cervical mucus contains an Immunoglobulin Binding factor (IgBF) which interacts with IgG as monomers under reducing condition. It may play a role in preventing antibody production against allogeneic sperms in the female reproductive tract. However, since IgBF is secreted as a homodimer that does not bind IgG,in vivoactivation systems should be investigated. GSH reduces the inactive native dimer to the active monomer. Protein disulfide isomerase (PDI), a molecular chaperone, alters the configuration of dimers to active monomers. 20S proteasomes produced by activated T cells which cleave the dimers in the presence of GSH to active fragments. All these activating systems are widely distributed as cellular enzymesin vivo.Also PDI mRNAs are expressed in uterine cervix, endometrium and fallopian tube. Since these enzymes are produced upon stimulation by the immune system, we hypothesize that immunocompetent cells interact with allogeneic sperms, leading to the local production of these enzymes that will activate IgBF.

  • Colocalization of Immunoglobulin Binding factor and prostate specific antigen in human prostate gland.
    Archives of Andrology, 1996
    Co-Authors: Masahiko Maegawa, Masaharu Kamada, N. Maeda, Toshihiro Aono, Keisuke Izumi, Susumu Kagawa, Shohei Koide
    Abstract:

    Immunoglobulin Binding factor (IgBF) produced in the prostate is a useful marker for the diagnosis of prostatic tumor. IgBF was localized in the majority of epithelial cells of benign prostatic hypertrophy by an immunohistochemical technique. Prostate specific antigen (PSA), a known marker for prostatic cancer, was localized to all epithelial cells. Double immunolabeling of IgBF and PSA using fluorescent methods revealed that all epithelial cells producing IgBF were also immunopositive for PSA and some cells were positive only for PSA. The present findings suggest that the prostatic glands consist of two types of epithelial cells, one producing both IgBF and PSA and the other producing PSA alone.

Shohei Koide - One of the best experts on this subject based on the ideXlab platform.

  • Colocalization of Immunoglobulin Binding factor and prostate specific antigen in human prostate gland.
    Archives of Andrology, 1996
    Co-Authors: Masahiko Maegawa, Masaharu Kamada, N. Maeda, Toshihiro Aono, Keisuke Izumi, Susumu Kagawa, Shohei Koide
    Abstract:

    Immunoglobulin Binding factor (IgBF) produced in the prostate is a useful marker for the diagnosis of prostatic tumor. IgBF was localized in the majority of epithelial cells of benign prostatic hypertrophy by an immunohistochemical technique. Prostate specific antigen (PSA), a known marker for prostatic cancer, was localized to all epithelial cells. Double immunolabeling of IgBF and PSA using fluorescent methods revealed that all epithelial cells producing IgBF were also immunopositive for PSA and some cells were positive only for PSA. The present findings suggest that the prostatic glands consist of two types of epithelial cells, one producing both IgBF and PSA and the other producing PSA alone.

  • Prostatic specific antigen and Immunoglobulin Binding factor in human seminal plasma and prostate.
    Archives of Andrology, 1992
    Co-Authors: Z. G. Liang, S. M. Mitsudo, Shohei Koide
    Abstract:

    Antibodies raised against prostatic specific antigen (PSA) and Immunoglobulin Binding factor (IgBF) of human seminal plasma (SP) were used to localize the antigens in various tissues by Western blot. Both antigens were found only in the prostate, including benign prostatic hypertrophy and prostatic adenocarcinoma. The polyclonal anti-PSA antibodies stained five prostatic protein bands with estimated Mr values of 10, 14, 22, 25, and 33 kD, whereas anti-IgBF antibodies stained a single 16-kD protein. No cross-reaction occurred between the two antibodies. When anti-PSA antibodies were used an additional protein with an estimated Mr of 35 JcD was detected in the extract of benign prostatic hypertrophy, but not with normal prostate or prostatic cancer. When SP and prostatic proteins were analyzed by SDS-PAGE under nonreducing condition and immunoblot with both antibodies, immunoreactive proteins with estimated Mr of 125 and 140 kD, respectively, were stained, suggesting that both factors may be produced as an ...

  • Immunoglobulin Binding factor of seminal plasma: a secretory product of human prostate.
    Archives of Andrology, 1992
    Co-Authors: Z. G. Liang, Masaharu Kamada, S. M. Mitsudo, Shohei Koide
    Abstract:

    To determine the source of the Immunoglobulin Binding factor (IBF) in seminal plasma, extracts of testis and accesory male sex organs were prepared and analyzed by sodium dodecyl sulfate polyacry-lamide gel electrophoresis (SDS-PAGE) and immunoblot. The detection reagents used were human and mouse serum Ig, monoclonal anti-Leu 1 Ib antibodies, and polyclonai rabbit anti-IBF antibodies. Of the tissues examined, only the prostate, including benign hypertrophy and adenocarcinoma, contained IBF. These findings suggest that IBF is a secretory product of the prostate.

  • Structural identity of Immunoglobulin Binding factor and prostatic secretory protein of human seminal plasma
    Biochemical and Biophysical Research Communications, 1991
    Co-Authors: Z. G. Liang, Masaharu Kamada, Shohei Koide
    Abstract:

    The amino acid sequence of the N-terminus of the Immunoglobulin Binding factor of human seminal plasma was determined. The initial 30 amino acids showed complete identity with that of prostatic secretory protein, β-microseminoprotein and β-inhibin. In conclusion, these proteins are probably a single entity.

Roland E Kontermann - One of the best experts on this subject based on the ideXlab platform.

  • a fab selective Immunoglobulin Binding domain from streptococcal protein g with improved half life extension properties
    PLOS ONE, 2015
    Co-Authors: Felix Unverdorben, Meike Hutt, Oliver Seifert, Roland E Kontermann
    Abstract:

    Background Half-life extension strategies have gained increasing interest to improve the pharmacokinetic and pharmacodynamic properties of protein therapeutics. Recently, we established an Immunoglobulin-Binding domain (IgBD) from streptococcal protein G (SpGC3) as module for half-life extension. SpGC3 is capable of Binding to the Fc region as well as the CH1 domain of Fab arms under neutral and acidic conditions. Methodology/Principal Findings Using site-directed mutagenesis, we generated a Fab-selective mutant (SpGC3Fab) to avoid possible interference with the FcRn-mediated recycling process and improved its affinity for mouse and human IgG by site-directed mutagenesis and phage display selections. In mice, this affinity-improved mutant (SpGC3FabRR) conferred prolonged plasma half-lives compared with SpGC3Fab when fused to small recombinant antibody fragments, such as single-chain Fv (scFv) and bispecific single-chain diabody (scDb). Hence, the SpGC3FabRR domain seems to be a suitable fusion partner for the half-life extension of small recombinant therapeutics. Conclusions/Significance The half-life extension properties of SpGC3 can be retained by restricting Binding to the Fab fragment of serum Immunoglobulins and can be improved by increasing Binding activity. The modified SpGC3 module should be suitable to extend the half-life of therapeutic proteins and, thus to improve therapeutic activity.

  • plasma half life extension of small recombinant antibodies by fusion to Immunoglobulin Binding domains
    Journal of Biological Chemistry, 2012
    Co-Authors: Meike Hutt, Aline Farberschwarz, Felix Unverdorben, Fabian Richter, Roland E Kontermann
    Abstract:

    Many therapeutic proteins possessing a small size are rapidly cleared from circulation. Half-life extension strategies have therefore become increasingly important to improve the pharmacokinetic and pharmacodynamic properties of protein therapeutics. Here, we performed a comparative analysis of the half-life extension properties of various bacterial Immunoglobulin-Binding domains (IgBDs) derived from Staphylococcus protein A (SpA), Streptococcus protein G (SpG), and Finegoldia (formerly Peptostreptococcus) protein L (PpL). These domains, composed of 50–60 amino acid residues, were fused to the C terminus of a single-chain Fv and a bispecific single-chain diabody, respectively. All fusion proteins were produced in mammalian cells and retained their antigen-Binding properties. The half-lives of the antibody molecules were prolonged to varying extents for the different IgBDs. The strongest effects in mice were observed for domain C3 of SpG (SpGC3) followed by domains B and D of SpA, suggesting that SpGC3 is particularly useful to extend the plasma half-life of small proteins.