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Start Over Author "Paul, Sudhir" Journal journal of biological chemistry
22 results on '"Paul, Sudhir"'

2. Specific Amyloid β Clearance by a Catalytic Antibody Construct

Author

Planque, Stephanie A., primary, Nishiyama, Yasuhiro, additional, Sonoda, Sari, additional, Lin, Yan, additional, Taguchi, Hiroaki, additional, Hara, Mariko, additional, Kolodziej, Steven, additional, Mitsuda, Yukie, additional, Gonzalez, Veronica, additional, Sait, Hameetha B.R., additional, Fukuchi, Ken-ichiro, additional, Massey, Richard J., additional, Friedland, Robert P., additional, O'Nuallain, Brian, additional, Sigurdsson, Einar M., additional, and Paul, Sudhir, additional

Published
2015
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3. Physiological IgM Class Catalytic Antibodies Selective for Transthyretin Amyloid

Author

Planque, Stephanie A., primary, Nishiyama, Yasuhiro, additional, Hara, Mariko, additional, Sonoda, Sari, additional, Murphy, Sarah K., additional, Watanabe, Kenji, additional, Mitsuda, Yukie, additional, Brown, Eric L., additional, Massey, Richard J., additional, Primmer, Stanley R., additional, O'Nuallain, Brian, additional, and Paul, Sudhir, additional

Published
2014
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6. Toward Effective HIV Vaccination

Author

Nishiyama, Yasuhiro, primary, Planque, Stephanie, additional, Mitsuda, Yukie, additional, Nitti, Giovanni, additional, Taguchi, Hiroaki, additional, Jin, Lei, additional, Symersky, Jindrich, additional, Boivin, Stephane, additional, Sienczyk, Marcin, additional, Salas, Maria, additional, Hanson, Carl V., additional, and Paul, Sudhir, additional

Published
2009
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9. Autoantibody-catalyzed Hydrolysis of Amyloid β Peptide

Author

Taguchi, Hiroaki, primary, Planque, Stephanie, additional, Nishiyama, Yasuhiro, additional, Symersky, Jindrich, additional, Boivin, Stephane, additional, Szabo, Paul, additional, Friedland, Robert P., additional, Ramsland, Paul A., additional, Edmundson, Allen B., additional, Weksler, Marc E., additional, and Paul, Sudhir, additional

Published
2008
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10. Towards Covalent Vaccination

Author

Nishiyama, Yasuhiro, primary, Mitsuda, Yukie, additional, Taguchi, Hiroaki, additional, Planque, Stephanie, additional, Salas, Maria, additional, Hanson, Carl V., additional, and Paul, Sudhir, additional

Published
2007
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11. Naturally Occurring Proteolytic Antibodies

Author

Paul, Sudhir, primary, Karle, Sangeeta, additional, Planque, Stephanie, additional, Taguchi, Hiroaki, additional, Salas, Maria, additional, Nishiyama, Yasuhiro, additional, Handy, Beverly, additional, Hunter, Robert, additional, Edmundson, Allen, additional, and Hanson, Carl, additional

Published
2004
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12. Ontogeny of Proteolytic Immunity

Author

Planque, Stephanie, primary, Bangale, Yogesh, additional, Song, Xiao-Tong, additional, Karle, Sangeeta, additional, Taguchi, Hiroaki, additional, Poindexter, Brian, additional, Bick, Roger, additional, Edmundson, Allen, additional, Nishiyama, Yasuhiro, additional, and Paul, Sudhir, additional

Published
2004
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16. Phosphonate Ester Probes for Proteolytic Antibodies

Author

Paul, Sudhir, primary, Tramontano, Alfonso, additional, Gololobov, Gennady, additional, Zhou, Yong-Xin, additional, Taguchi, Hiroaki, additional, Karle, Sangeeta, additional, Nishiyama, Yasuhiro, additional, Planque, Stephanie, additional, and George, Saji, additional

Published
2001
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19. Natural Catalytic Antibodies: Peptide-hydrolyzing Activities of Bence Jones Proteins and VLFragment (∗)

Author

Paul, Sudhir, Li, Lan, Kalaga, Ravishankar, Wilkins-Stevens, Priscilla, Stevens, Fred J., and Solomon, Alan

Abstract

Monoclonal human light chains, i.e.Bence Jones proteins, and their recombinant variable fragments (VL) were screened for proteolytic activity using peptide-methylcoumarinamide (peptide-MCA) conjugates and vasoactive intestinal polypeptide (VIP) as substrates. Sixteen of 21 Bence Jones proteins and one of three VLfragments were capable of detectable cleavage of one or more substrates. The magnitude and kinetic characteristics of the activity varied with different substrates. Among the peptide-MCA substrates, the presence of tripeptide or tetrapeptide moieties with a basic residue at the scissile bond generally favored expression of the activity. The influence of N-terminal flanking residue recognition was evident from differing values of Kmand kcat(turnover number) observed using different Arg-containing peptide-MCA substrates. Different light chains displayed different kinetic parameters for the same substrate, suggesting unique catalytic sites. Hydrolysis of VIP was characterized by nanomolar Michaelis-Menten constants (Km), suggesting comparatively high affinity recognition of this peptide. The 25-kDa monomer and the 50-kDa dimer forms of one light chain preparation were resolved by gel filtration in 6 M guanidine hydrochloride. Following renaturation, the monomer displayed 51-fold greater peptide-MCA-hydrolyzing activity than the dimer. A renatured VLdomain prepared by gel filtration in 6 M guanidine hydrochloride displayed VIP-hydrolyzing activity in the 12.5-kDa peak fractions. These results provide evidence for the proteolytic activity of certain human light chains and imply that this phenomenon may have a pathophysiological significance.

Published
1995
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20. Covalent Inactivation of Factor VIII Antibodies from Hemophilia A Patients by an Electrophilic FVIII AnaIog.

Author

Plariquet, Stephanie, Escobart, Miguel A., Smith, Ken C., Taguchi, Hiroaki, Nishiyama, Yasuhiro, Donnachie, Elizabeth, Pratt, Kathleen P., and Paul, Sudhir

Subjects
*HEMOPHILIA, *ANTIGENS, *IMMUNOGLOBULINS, *ENZYMES, *SCISSION (Chemistry)
Abstract

The antigen-binding sites of antibodies (Abs) can express enzyme-like nucleophiles that react covalently with electrophilic compounds. We examined the irreversible and specific inactivation of antibodies (Abs) to Factor VIII (FVIII) responsible for failure of FVIII replacement therapy in hemophilia A (HA) patients. Electrophilic analogs of FVIII (E-FVIII) and its C2 domain (E-C2) were prepared by placing the strongly electrophilic phosphonate groups at surface-exposed Lys side chains of diverse antigenic epitopes. IgG Abs to FVIII from HA patients formed stable immune complexes with E-FVIII and E-C2 that were refractory to dissociation by SDS treatment and boiling, procedures that dissociate noncovalent Ab-antigen complexes. The rate-limiting step in the reaction was formation of the initial noncovalent complexes. Conversion of the initial complexes to the irreversible state occurred rapidly. The antigenic epitopes of E-FVIII were largely intact, and most of the Abs were consumed covalently. E-FVIII expressed poor FVIII cofactor activity in clotting factor assays. Nonspecific interference by E-FVIII in clotting factor function was not evident. Treatment with E-FVIII, and to a lesser extent E-C2, irreversibly relieved the FVIII inhibitory effect of HA IgG in clotting factor assays. Small FVIII peptides did not display useful reactivity, highlighting the diverse epitope specificities of the Abs and the conformational character of FVIII epitopes. E-FVIII is a prototype reagent able to attain irreversible and specific inactivation of pathogenic Abs. [ABSTRACT FROM AUTHOR]

Published
2008
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21. Towards Covalent Vaccination: IMPROVED POLYCLONAL HIV NEUTRALIZING ANTIBODY RESPONSE INDUCED BY AN ELECTROPHILIC gp 120 V3 PEPTIDE ANALOG.

Author

Nishiyama, Yasuhiro, Mitsuda, Yukie, Taguchi, Hiroaki, Planque, Stephanie, Salas, Maria, Hanson, Carl V., and Paul, Sudhir

Subjects
*VACCINATION, *HIV, *ANTIGENS, *IMMUNOGLOBULINS, *BACTERIA, *NUCLEOPHILIC reactions
Abstract

Rare monoclonal antibodies (Abs) can form irreversible complexes with antigens by enzyme-like covalent nucleophile-electrophile pairing. To determine the feasibility of applying irreversible antigen inactivation by Abs as the basis of vaccination against microbes, we studied the polyclonal nucleophilic Ab response induced by the electrophilic analog of a synthetic peptide corresponding to the principal neutralizing determinant (PND) of human immunodeficiency virus type-1 (HIV) gp120 located in the V3 domain. Abs from mice immunized with the PND analog containing electrophilic phosphonates (E-PND) neutralized a homologous HIV strain (MN) ∼50-fold more potently than control Abs from mice immunized with PND. The IgG fractions displayed binding to intact HIV particles. HIV complexes formed by anti-E-PND IgG dissociated noticeably more slowly than the complexes formed by anti-PND IgG. The slower dissociation kinetics are predicted to maintain long-lasting blockade of host cell receptor recognition by gp120. Pre-treatment of the anti-PND IgG with a haptenic electrophilic phosphonate compound resulted in more rapid dissociation of the HIV-IgG complexes, consistent with the hypothesis that enhanced Ab nucleophilic reactivity induced by electrophilic immunization imparts irreversible character to the complexes. These results suggest that electrophilic immunization induces a sufficiently robust nucleophilic Ab response to enhance the anti-microbial efficacy of candidate polypeptide vaccines. [ABSTRACT FROM AUTHOR]

Published
2007
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22. Autoantibody-catalyzed hydrolysis of amyloid beta peptide.

Author

Taguchi H, Planque S, Nishiyama Y, Symersky J, Boivin S, Szabo P, Friedland RP, Ramsland PA, Edmundson AB, Weksler ME, and Paul S

Subjects
Adult, Aged, Aged, 80 and over, Alzheimer Disease blood, Alzheimer Disease therapy, Amyloid beta-Peptides immunology, Amyloid beta-Peptides metabolism, Antibodies, Monoclonal blood, Antibodies, Monoclonal immunology, Autoantibodies blood, Autoantibodies immunology, Brain immunology, Brain metabolism, Catalysis, Female, Humans, Hydrolysis, Immunoglobulin M immunology, Immunoglobulin M metabolism, Immunotherapy, Male, Peptide Fragments immunology, Peptide Fragments metabolism, Serine Proteinase Inhibitors chemistry, Waldenstrom Macroglobulinemia blood, Waldenstrom Macroglobulinemia therapy, Alzheimer Disease immunology, Amyloid beta-Peptides chemistry, Antibodies, Monoclonal chemistry, Autoantibodies chemistry, Immunoglobulin M chemistry, Peptide Fragments chemistry, Waldenstrom Macroglobulinemia immunology
Abstract

We describe IgM class human autoantibodies that hydrolyze amyloid beta peptide 1-40 (Abeta40). A monoclonal IgM from a patient with Waldenström's macroglobulinemia hydrolyzed Abeta40 at the Lys-28-Gly-29 bond and Lys-16-Ala-17 bonds. The catalytic activity was inhibited stoichiometrically by an electrophilic serine protease inhibitor. Treatment with the catalytic IgM blocked the aggregation and toxicity of Abeta40 in neuronal cell cultures. IgMs purified from the sera of patients with Alzheimer disease (AD) hydrolyzed Abeta40 at rates superior to IgMs from age-matched humans without dementia. IgMs from non-elderly humans expressed the least catalytic activity. The reaction rate was sufficient to afford appreciable degradation at physiological Abeta and IgM concentrations found in peripheral circulation. Increased Abeta concentrations in the AD brain are thought to induce neurodegenerative effects. Peripheral administration of Abeta binding antibodies has been suggested as a potential treatment of AD. Our results suggest that catalytic IgM autoantibodies can help clear Abeta, and they open the possibility of using catalytic Abs for AD immunotherapy.

Published
2008
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