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Relevant bibliographies by topics / Human monoclonal antibodies (humAbs)

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Academic literature on the topic 'Human monoclonal antibodies (humAbs)'

Author: Grafiati

Published: 14 March 2023

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Journal articles on the topic "Human monoclonal antibodies (humAbs)"

1

Broering, Teresa J., Kerry A. Garrity, Naomi K. Boatright, Susan E. Sloan, Frantisek Sandor, William D. Thomas, Gyongyi Szabo, Robert W. Finberg, Donna M. Ambrosino, and Gregory J. Babcock. "Identification and Characterization of Broadly Neutralizing Human Monoclonal Antibodies Directed against the E2 Envelope Glycoprotein of Hepatitis C Virus." Journal of Virology 83, no. 23 (September 16, 2009): 12473–82. http://dx.doi.org/10.1128/jvi.01138-09.

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ABSTRACT Nearly all livers transplanted into hepatitis C virus (HCV)-positive patients become infected with HCV, and 10 to 25% of reinfected livers develop cirrhosis within 5 years. Neutralizing monoclonal antibody could be an effective therapy for the prevention of infection in a transplant setting. To pursue this treatment modality, we developed human monoclonal antibodies (HuMAbs) directed against the HCV E2 envelope glycoprotein and assessed the capacity of these HuMAbs to neutralize a broad panel of HCV genotypes. HuMAb antibodies were generated by immunizing transgenic mice containing human antibody genes (HuMAb mice; Medarex Inc.) with soluble E2 envelope glycoprotein derived from a genotype 1a virus (H77). Two HuMAbs, HCV1 and 95-2, were selected for further study based on initial cross-reactivity with soluble E2 glycoproteins derived from genotypes 1a and 1b, as well as neutralization of lentivirus pseudotyped with HCV 1a and 1b envelope glycoproteins. Additionally, HuMAbs HCV1 and 95-2 potently neutralized pseudoviruses from all genotypes tested (1a, 1b, 2b, 3a, and 4a). Epitope mapping with mammalian and bacterially expressed proteins, as well as synthetic peptides, revealed that HuMAbs HCV1 and 95-2 recognize a highly conserved linear epitope spanning amino acids 412 to 423 of the E2 glycoprotein. The capacity to recognize and neutralize a broad range of genotypes, the highly conserved E2 epitope, and the fully human nature of the antibodies make HuMAbs HCV1 and 95-2 excellent candidates for treatment of HCV-positive individuals undergoing liver transplantation.

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Mukherjee, Jean, Kerry Chios, Dianne Fishwild, Deborah Hudson, Susan O'Donnell, Stephen M. Rich, Arthur Donohue-Rolfe, and Saul Tzipori. "Human Stx2-Specific Monoclonal Antibodies Prevent Systemic Complications of Escherichia coli O157:H7 Infection." Infection and Immunity 70, no. 2 (February 2002): 612–19. http://dx.doi.org/10.1128/iai.70.2.612-619.2002.

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ABSTRACT Hemolytic-uremic syndrome (HUS) is a serious complication predominantly associated with infection by enterohemorrhagic Escherichia coli (EHEC), such as E. coli O157:H7. EHEC can produce Shiga toxin 1 (Stx1) and/or Shiga toxin 2 (Stx2), both of which are exotoxins comprised of active (A) and binding (B) subunits. In piglets and mice, Stx can induce fatal neurological symptoms. Polyclonal Stx2 antiserum can prevent these effects in piglets infected with the Stx2-producing E. coli O157:H7 strain 86-24. Human monoclonal antibodies (HuMAbs) against Stx2 were developed as potential passive immunotherapeutic reagents for the prevention and/or treatment of HUS. Transgenic mice bearing unrearranged human immunoglobulin (Ig) heavy and κ light chain loci (HuMAb___Mouse) were immunized with formalin-inactivated Stx2. Thirty-seven stable hybridomas secreting Stx2-specific HuMAbs were isolated: 33 IgG1κ A-subunit-specific and 3 IgG1κ and 1 IgG3κ B-subunit-specific antibodies. Six IgG1κ A-subunit-specific (1G3, 2F10, 3E9, 4H9, 5A4, and 5C12) and two IgG1κ B-subunit-specific (5H8 and 6G3) HuMAbs demonstrated neutralization of >95% activity of 1 ng of Stx2 in the presence of 0.04 μg of HuMAb in vitro and significant prolongation of survival of mice given 50 μg of HuMAb intraperitoneally (i.p.) and 25 ng of Stx2 intravenously. When administered i.p. to gnotobiotic piglets 6 or 12 h after infection with E. coli O157:H7 strain 86-24, HuMAbs 2F10, 3E9, 5H8, and 5C12 prolonged survival and prevented development of fatal neurological signs and cerebral lesions. The Stx2-neutralizing ability of these HuMAbs could potentially be used clinically to passively protect against HUS development in individuals infected with Stx-producing bacteria, including E. coli O157:H7.

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Wang, Jianmin, Zhe Chen, Linlin Bao, Weijia Zhang, Ying Xue, XingHuo Pang, Xi Zhang, Chuan Qin, and Qi Jin. "Characterization of Two Human Monoclonal Antibodies Neutralizing Influenza A H7N9 Viruses." Journal of Virology 89, no. 17 (June 10, 2015): 9115–18. http://dx.doi.org/10.1128/jvi.01295-15.

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H7N9 was a cause of significant global health concern due to its severe infection and approximately 35% mortality in humans. By screening a Fab antibody phage library derived from patients who recovered from H7N9 infections, we characterized two human monoclonal antibodies (HuMAbs), HNIgGD5 and HNIgGH8. The epitope of these two antibodies was dependent on two residues in the receptor binding site at positions V186 and L226 of the hemagglutinin glycoprotein. Both antibodies possessed high neutralizing activity.

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Wang, Yang, Rianne Esquivel, Seleeke Flingai, Zachary A. Schiller, Aurélie Kern, Sangya Agarwal, Jacqueline Chu, et al. "Anti-OspA DNA-Encoded Monoclonal Antibody Prevents Transmission of Spirochetes in Tick Challenge Providing Sterilizing Immunity in Mice." Journal of Infectious Diseases 219, no. 7 (November 21, 2018): 1146–50. http://dx.doi.org/10.1093/infdis/jiy627.

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AbstractWe recently developed anti-OspA human immunoglobulin G1 monoclonal antibodies (HuMAbs) that are effective in preventing Borrelia transmission from ticks in a murine model. Here, we investigated a novel approach of DNA-mediated gene transfer of HuMAbs that provide protection against Lyme disease. Plasmid DNA-encoded anti-OspA HuMAbs inoculated in mice achieved a serum antibody concentration of >6 μg/mL. Among mice injected with DNA-encoded monoclonal antibodies, 75%–77% were protected against an acute challenge by Borrelia-infected ticks. Our results represent the first demonstration of employing DNA transfer as a delivery system for antibodies that block transmission of Borrelia in animal models.

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Babcock, Gregory J., Teresa J. Broering, Hector J. Hernandez, Robert B. Mandell, Katherine Donahue, Naomi Boatright, Anne M. Stack, et al. "Human Monoclonal Antibodies Directed against Toxins A and B Prevent Clostridium difficile-Induced Mortality in Hamsters." Infection and Immunity 74, no. 11 (September 11, 2006): 6339–47. http://dx.doi.org/10.1128/iai.00982-06.

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ABSTRACT Clostridium difficile is the leading cause of nosocomial antibiotic-associated diarrhea, and recent outbreaks of strains with increased virulence underscore the importance of identifying novel approaches to treat and prevent relapse of Clostridium difficile-associated diarrhea (CDAD). CDAD pathology is induced by two exotoxins, toxin A and toxin B, which have been shown to be cytotoxic and, in the case of toxin A, enterotoxic. In this report we describe fully human monoclonal antibodies (HuMAbs) that neutralize these toxins and prevent disease in hamsters. Transgenic mice carrying human immunoglobulin genes were used to isolate HuMAbs that neutralize the cytotoxic effects of either toxin A or toxin B in cell-based in vitro neutralization assays. Three anti-toxin A HuMAbs (3H2, CDA1, and 1B11) could all inhibit the enterotoxicity of toxin A in mouse intestinal loops and the in vivo toxicity in a systemic mouse model. Four anti-toxin B HuMAbs (MDX-1388, 103-174, 1G10, and 2A11) could neutralize cytotoxicity in vitro, although systemic toxicity in the mouse could not be neutralized. Anti-toxin A HuMAb CDA1 and anti-toxin B HuMAb MDX-1388 were tested in the well-established hamster model of C. difficile disease. CDA1 alone resulted in a statistically significant reduction of mortality in hamsters; however, the combination treatment offered enhanced protection. Compared to controls, combination therapy reduced mortality from 100% to 45% (P < 0.0001) in the primary disease hamster model and from 78% to 32% (P < 0.0001) in the less stringent relapse model.

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Matsumura, Takuhiro, Sho Amatsu, Ryo Misaki, Masahiro Yutani, Anariwa Du, Tomoko Kohda, Kazuhito Fujiyama, Kazuyoshi Ikuta, and Yukako Fujinaga. "Fully Human Monoclonal Antibodies Effectively Neutralizing Botulinum Neurotoxin Serotype B." Toxins 12, no. 5 (May 7, 2020): 302. http://dx.doi.org/10.3390/toxins12050302.

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Botulinum neurotoxin (BoNT) is the most potent natural toxin known. Of the seven BoNT serotypes (A to G), types A, B, E, and F cause human botulism. Treatment of human botulism requires the development of effective toxin-neutralizing antibodies without side effects such as serum sickness and anaphylaxis. In this study, we generated fully human monoclonal antibodies (HuMAbs) against serotype B BoNT (BoNT/B1) using a murine–human chimera fusion partner cell line named SPYMEG. Of these HuMAbs, M2, which specifically binds to the light chain of BoNT/B1, showed neutralization activity in a mouse bioassay (approximately 10 i.p. LD50/100 µg of antibody), and M4, which binds to the C-terminal of heavy chain, showed partial protection. The combination of two HuMAbs, M2 (1.25 µg) and M4 (1.25 µg), was able to completely neutralize BoNT/B1 (80 i.p. LD50) with a potency greater than 80 i.p. LD50/2.5 µg of antibodies, and was effective both prophylactically and therapeutically in the mouse model of botulism. Moreover, this combination showed broad neutralization activity against three type B subtypes, namely BoNT/B1, BoNT/B2, and BoNT/B6. These data demonstrate that the combination of M2 and M4 is promising in terms of a foundation for new human therapeutics for BoNT/B intoxication.

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Eren, Rachel, Dorit Landstein, Dov Terkieltaub, Ofer Nussbaum, Arie Zauberman, Judith Ben-Porath, Judith Gopher, et al. "Preclinical Evaluation of Two Neutralizing Human Monoclonal Antibodies against Hepatitis C Virus (HCV): a Potential Treatment To Prevent HCV Reinfection in Liver Transplant Patients." Journal of Virology 80, no. 6 (March 15, 2006): 2654–64. http://dx.doi.org/10.1128/jvi.80.6.2654-2664.2006.

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ABSTRACT Passive immunotherapy is potentially effective in preventing reinfection of liver grafts in hepatitis C virus (HCV)-associated liver transplant patients. A combination of monoclonal antibodies directed against different epitopes may be advantageous against a highly mutating virus such as HCV. Two human monoclonal antibodies (HumAbs) against the E2 envelope protein of HCV were developed and tested for the ability to neutralize the virus and prevent human liver infection. These antibodies, designated HCV-AB 68 and HCV-AB 65, recognize different conformational epitopes on E2. They were characterized in vitro biochemically and functionally. Both HumAbs are immunoglobulin G1 and have affinity constants to recombinant E2 constructs in the range of 10−10 M. They are able to immunoprecipitate HCV particles from infected patients' sera from diverse genotypes and to stain HCV-infected human liver tissue. Both antibodies can fix complement and form immune complexes, but they do not activate complement-dependent or antibody-dependent cytotoxicity. Upon complement fixation, the monoclonal antibodies induce phagocytosis of the immune complexes by neutrophils, suggesting that the mechanism of viral clearance includes endocytosis. In vivo, in the HCV-Trimera model, both HumAbs were capable of inhibiting HCV infection of human liver fragments and of reducing the mean viral load in HCV-positive animals. The demonstrated neutralizing activities of HCV-AB 68 and HCV-AB 65 suggest that they have the potential to prevent reinfection in liver transplant patients and to serve as prophylactic treatment in postexposure events.

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Sootichote, Rochanawan, Wilarat Puangmanee, Surachet Benjathummarak, Siriporn Kowaboot, Atsushi Yamanaka, Korbporn Boonnak, Sumate Ampawong, Supawat Chatchen, Pongrama Ramasoota, and Pannamthip Pitaksajjakul. "Potential Protective Effect of Dengue NS1 Human Monoclonal Antibodies against Dengue and Zika Virus Infections." Biomedicines 11, no. 1 (January 16, 2023): 227. http://dx.doi.org/10.3390/biomedicines11010227.

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Due to the lack of an effective therapeutic treatment to flavivirus, dengue virus (DENV) nonstructural protein 1 (NS1) has been considered to develop a vaccine owing to its lack of a role in antibody-dependent enhancement (ADE). However, both NS1 and its antibody have shown cross-reactivity to host molecules and have stimulated anti-DENV NS1 antibody-mediated endothelial damage and platelet dysfunction. To overcome the pathogenic events and reactogenicity, human monoclonal antibodies (HuMAbs) against DENV NS1 were generated from DENV-infected patients. Herein, the four DENV NS1-specific HuMAbs revealed the therapeutic effects in viral neutralization, reduction of viral replication, and enhancement of cell cytolysis of DENV and zika virus (ZIKV) via complement pathway. Furthermore, we demonstrate that DENV and ZIKV NS1 trigger endothelial dysfunction, leading to vascular permeability in vitro. Nevertheless, the pathogenic effects from NS1 were impeded by 2 HuMAbs (D25-4D4C3 and D25-2B11E7) and also protected the massive cytokines stimulation (interleukin [IL-]-1b, IL-1ra, IL-2, IL-4, IL-5, IL-6, IL-8, IL-9, IL-13, IL-17, eotaxin, granulocyte colony-stimulating factor, granulocyte-macrophage colony-stimulating factor, Inducible protein-10, monocyte chemoattractant protein-1, macrophage inflammatory protein [MIP]-1 α, MIP-1β, tumor necrosis factor-α, platelet-derived growth factor, and RANTES). Collectively, our findings suggest that the novel protective NS1 monoclonal antibodies generated from humans has multiple therapeutic benefits against DENV and ZIKV infections.

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Sheppard, Neil C., Sarah L. Davies, Simon A. Jeffs, Sueli M. Vieira, and Quentin J. Sattentau. "Production and Characterization of High-Affinity Human Monoclonal Antibodies to Human Immunodeficiency Virus Type 1 Envelope Glycoproteins in a Mouse Model Expressing Human Immunoglobulins." Clinical and Vaccine Immunology 14, no. 2 (December 13, 2006): 157–67. http://dx.doi.org/10.1128/cvi.00274-06.

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ABSTRACT Human (Hu) monoclonal antibodies (MAbs) against the human immunodeficiency virus type 1 (HIV-1) envelope glycoproteins (Env) are useful tools in the structural and functional analysis of Env, are under development both as potential prophylaxis and as therapy for established HIV-1 infection, and have crucial roles in guiding the design of preventative vaccines. Despite representing more than 50% of infections globally, no MAbs have been generated in any species against C clade HIV-1 Env. To generate HuMAbs to a novel Chinese C clade Env vaccine candidate (primary isolate strain HIV-197CN54), we used BAB5 mice that express a human immunoglobulin (Ig) M antibody repertoire in place of endogenous murine immunoglobulins. When immunized with HIV-197CN54 Env, these mice developed antigen-specific IgM antibodies. Hybridoma fusions using splenocytes from these mice enabled the isolation of two Env-specific IgM HuMAbs: N3C5 and N03B11. N3C5 bound to HIV-1 Env from clades A and C, whereas N03B11 bound two geographically distant clade C isolates but not Env from other clades. These HuMAbs bind conformational epitopes within the immunodominant region of the gp41 ectodomain. N3C5 weakly neutralized the autologous isolate in the absence of complement and weakly enhanced infection in the presence of complement. N03B11 has no effect on infectivity in either the presence or the absence of complement. These novel HuMAbs are useful reagents for the study of HIV-1 Env relevant to the global pandemic, and mice producing human immunoglobulin present a tool for the production of such antibodies.

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Sheoran, Abhineet S., Susan Chapman, Pradeep Singh, Arthur Donohue-Rolfe, and Saul Tzipori. "Stx2-Specific Human Monoclonal Antibodies Protect Mice against Lethal Infection with Escherichia coli Expressing Stx2 Variants." Infection and Immunity 71, no. 6 (June 2003): 3125–30. http://dx.doi.org/10.1128/iai.71.6.3125-3130.2003.

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ABSTRACT Shiga toxin-producing Escherichia coli (STEC) strains are responsible for causing hemolytic-uremic syndrome (HUS), and systemic administration of Shiga toxin (Stx)-specific human monoclonal antibodies (HuMAbs) is considered a promising approach for prevention or treatment of the disease in children. The goal of the present study was to investigate the ability of Stx2-specific HuMAbs to protect against infections with STEC strains that produce Stx2 variants. Dose-response studies on five HuMAbs, using the mouse toxicity model, revealed that only the three directed against the A subunit were protective against Stx2 variants, and 5C12 was the most effective among the three tested. Two HuMAbs directed against the B subunit, while highly effective against Stx2, were ineffective against Stx2 variants. In a streptomycin-treated mouse model, parenteral administration of 5C12 significantly protected mice up to 48 h after oral bacterial challenge. We conclude that 5C12, reactive against the Stx2 A subunit, is an excellent candidate for immunotherapy against HUS and that antibodies directed against the A subunit of Stx2 have broad-spectrum activity that includes Stx2 variants, compared with those directed against the B subunit.

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Dissertations / Theses on the topic "Human monoclonal antibodies (humAbs)"

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Austin, Eric B. "Human monoclonal antibodies." Thesis, University of Nottingham, 1990. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.276187.

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Ohlin, Mats. "Human monoclonal antibody technology a tool to investigate human antibody repertoires /." Lund : Dept. of Immunotechnology, Lund University, 1992. http://catalog.hathitrust.org/api/volumes/oclc/39693827.html.

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Watson, Nigel. "Monoclonal antibodies to human immunoglobulin allotypes." Thesis, University of Strathclyde, 1988. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.304897.

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De, Silva M. G. "Human monoclonal antibodies in the study of diabetes." Thesis, University of Surrey, 1988. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.233146.

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Bell, Graham Thomas. "Studies on the production of human monoclonal antibodies." Thesis, University of Edinburgh, 1988. http://hdl.handle.net/1842/19241.

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Heath, Lindsay Anne. "Heterogeneity in neural crest development detected by monoclonal antibodies." Thesis, University of Southampton, 1990. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.293618.

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Hunter, Nicole Marie. "A system for the production of human monoclonal antibodies." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1999. http://www.collectionscanada.ca/obj/s4/f2/dsk1/tape8/PQDD_0006/MQ46024.pdf.

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Johansson, Daniel X. "Expression and interaction studies of recombinant human monoclonal antibodies /." Stockholm, 2007. http://diss.kib.ki.se/2007/978-91-7357-137-1/.

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Bindon, Carol Ianthe. "Complement-mediated lysis by monoclonal antibodies for human therapy." Thesis, University of Cambridge, 1987. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.253842.

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Soos, M. A. "Studies with monoclonal antibodies to the human insulin receptor." Thesis, University of Cambridge, 1986. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.373704.

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Books on the topic "Human monoclonal antibodies (humAbs)"

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E, Salvaggio John, Shaw Jane E, Fisher Robert S, and Neu Harold C. 1934-, eds. Immunology and monoclonal antibodies. Mount Kisco, N.Y: Futura Pub. Co., 1985.

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J, Burlingham William, ed. A Critical analysis of monoclonal antibody therapy in transplantation. Boca Raton: CRC Press, 1992.

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Steinitz, Michael, ed. Human Monoclonal Antibodies. Totowa, NJ: Humana Press, 2014. http://dx.doi.org/10.1007/978-1-62703-586-6.

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Steinitz, Michael, ed. Human Monoclonal Antibodies. New York, NY: Springer New York, 2019. http://dx.doi.org/10.1007/978-1-4939-8958-4.

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Engleman, Edgar G., Steven K. H. Foung, James W. Larrick, and Andrew A. Raubitschek, eds. Human Hybridomas and Monoclonal Antibodies. Boston, MA: Springer US, 1985. http://dx.doi.org/10.1007/978-1-4684-4949-5.

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G, Engleman Edgar, ed. Human hybridomas and monoclonal antibodies. New York: Plenum Press, 1985.

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Leonard, Vaughan Christopher, ed. Biomechanics of sport. Boca Raton, Fla: CRC Press, 1989.

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IRI International Symposium on Biotechnology, Monoclonal Antibodies in the Treatment of Human Disease (1st 1986 Edinburgh, Scotland). Human monoclonal antibodies: Current techniques and future perspectives : proceedingsof the first IRI International Symposium on Biotechnology, Monoclonal Antibodies in the Treatment of Human Disease, November 10-12, 1986, Edinburgh, UK. Oxford: IRL, 1987.

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Nelson, Paul N. Monoclonal antibodies to human IgG allotypes. Birmingham: University of Birmingham, 1988.

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Michael, Steinitz. Human monoclonal antibodies: Methods and protocols. New York: Humana Press, 2014.

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Book chapters on the topic "Human monoclonal antibodies (humAbs)"

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Olsson, Lennart, and Peter Brams. "Human—Human Hybridoma Technology." In Human Hybridomas and Monoclonal Antibodies, 227–44. Boston, MA: Springer US, 1985. http://dx.doi.org/10.1007/978-1-4684-4949-5_13.

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Denis, Kathleen A., Randolph Wall, and Andrew Saxon. "Human—Human Hybridomas in the Study of Immunodeficiencies." In Human Hybridomas and Monoclonal Antibodies, 293–307. Boston, MA: Springer US, 1985. http://dx.doi.org/10.1007/978-1-4684-4949-5_17.

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Shoenfeld, Yehuda, and Robert S. Schwartz. "The Production of Monoclonal Antibodies by Human—Human Hybridomas." In Human Hybridomas and Monoclonal Antibodies, 247–62. Boston, MA: Springer US, 1985. http://dx.doi.org/10.1007/978-1-4684-4949-5_14.

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Shay, Jerry W. "Human Hybridomas and Monoclonal Antibodies." In Human Hybridomas and Monoclonal Antibodies, 5–20. Boston, MA: Springer US, 1985. http://dx.doi.org/10.1007/978-1-4684-4949-5_1.

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Glassy, Mark C., Harold H. Handley, and Ivor Royston. "Design and Production of Human Monoclonal Antibodies to Human Cancers." In Human Hybridomas and Monoclonal Antibodies, 211–25. Boston, MA: Springer US, 1985. http://dx.doi.org/10.1007/978-1-4684-4949-5_12.

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Foung, Steven K. H., Susan Perkins, Jeffrey Lifson, Nahid Mohagheghpour, Dianne Fishwild, F. Carl Grumet, Edgar G. Engleman, and Ann Arvin. "Production of Human Monoclonal Antibodies Using a Human-Mouse Fusion Partner." In Human Hybridomas and Monoclonal Antibodies, 135–48. Boston, MA: Springer US, 1985. http://dx.doi.org/10.1007/978-1-4684-4949-5_8.

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Ruiter, D. J., G. N. P. van Muijen, H. van Nouhuys, and S. Ferrone. "Immunopathology of Melanoma with Monoclonal Antibodies." In Human Melanoma, 253–77. Berlin, Heidelberg: Springer Berlin Heidelberg, 1990. http://dx.doi.org/10.1007/978-3-642-74496-9_19.

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Larrick, James W., Bradley J. Dyer, George Senyk, Sarah M. Hart, Richard Moss, David Lippman, Mark C. Jahnsen, Janet Wang, Howard Weintraub, and Andrew A. Raubitschek. "In Vitro Expansion of Human B Cells for the Production of Human Monoclonal Antibodies." In Human Hybridomas and Monoclonal Antibodies, 149–65. Boston, MA: Springer US, 1985. http://dx.doi.org/10.1007/978-1-4684-4949-5_9.

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Burnett, Karen G., Julia P. Leung, and Joanne Martinis. "Human Monoclonal Antibodies to Defined Antigens." In Human Hybridomas and Monoclonal Antibodies, 113–33. Boston, MA: Springer US, 1985. http://dx.doi.org/10.1007/978-1-4684-4949-5_7.

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Siadak, Anthony W., and Mark E. Lostrom. "Cell-Driven Viral Transformation." In Human Hybridomas and Monoclonal Antibodies, 167–85. Boston, MA: Springer US, 1985. http://dx.doi.org/10.1007/978-1-4684-4949-5_10.

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Conference papers on the topic "Human monoclonal antibodies (humAbs)"

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Kiefel, V., S. Santoso, and C. Mueller-Eckhardt. "ANALYSIS OF PLATELET REACTIVE ANTIBODIES USING MONOCLONAL ANTIBODIES." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643929.

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The characterization of platelet reactive alloantibodies and autoantibodies is mandatory for the diagnosis of posttransfusion purpura, neonatal alloimmune thrombocytopenia, autoimmune thrombocytopenia and for the selection of platelet donors prior to platelet transfusions in immunized polytransfused patients. The platelet immunofluorescence test is suitable for the detection of platelet reactive antibodies. In many cases, however, mixtures containing different platelet reactive antibodies have to be dissected.In order to analyze these sera, we have developed a novel enzyme immunoassay based upon monoclonal antibody specific immobilization of platelet antigens (MAIPA). In brief, platelets are incubated simultaneously with the (human) serum to be investigated and a monoclonal (mouse) antibody directed against an epitope on the same platelet membrane glycoprotein (GP). Platelets are then washed and solubilized in TRIS buffered saline containing NP40. The lysed platelets are then pipetted into the wells of microtiter plates, coated with goat anti mouse IgG where mouse anti GP-complexes are immobilized. Human platelet reactive antibodies on the same GP are detected using enzyme labelled goat anti human IgG, IgM, or IgA, respectively. Using mab Gi5, mab FMC25, mab w6.32 directed against epitopes on the glycoprotein complex IIb/IIIa, glycoprotein Ib and HLA class I molecule, respectively, and a panel of typed platelet donors, even sera containing different platelet reactive antibodies are readily analyzed. Results of experiments with platelet specific alloantibodies (anti P1A1, anti P1A2 and anti Bak(a)), autoantibodies (against the GP Ilb/IIIa complex and GP Ib) and a drug dependent antibody show that this assay allows to discriminate all these different platelet reactive antibodies.

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2

Hessing, Martin, Joost C. M. Meijers, Jan A. van Mourik, and Bonno N. Bouma. "MONOCLONAL ANTIBODIES TO HUMAN PROTEIN S AND C4b-BINDING PROTEIN." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644291.

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Protein S (PS) circulates in plasma both free and in reversible association with the complement component C4b-binding protein (C4bp). Only free PS is functional as a cofactor for activated protein C (APC). Cleavage of PS by thrombin at a site near the r-carboxyglutamic acid domain is associated with a loss of cofactor activity. This may be a control mechanism for the anticoagulant activity of APC. These observations led us to investigate the role of C4bp and thrombin in the regulation of PS. Complex formation between purified PS and C4bp was studied in plasma and in a system with purified components. 125I-labeled PS was first incubated with either C4bp or citrated plasma and then subjected to polyacrylamide gelelectrophoresis in the absence of SDS. The formation of the C4bp-PS complex in plasma and in the purified system was demonstrated by autoradiography. Crossed immuno-electrophoresis using an antiserum against PS was performed in the presence of 8 mM EDTA. Human citrated plasma showed two precipitin peaks. Free PS migrated rapidly in the first dimension, whereas the C4bp-PS complex was just anodal to the application slot. The addition of C4bp to either plasma or purified PS resulted in the disappearance of the free PS peak and an increase of the slower migrating peak. The effect of purified C4bp on the PS-cofactor function of APC was studied in citrated plasma. The prolongation of the APTT induced by the addition of APC could be inhibited by the addition of increasing amounts of C4bp. Monoclonal antibodies to PS and C4bp were prepared and characterized. The monoclonal antibodies to either PS or C4bp did not block the complex formation between and PS, as was demonstrated by dot blotting of C4bp with 125I-PS and agarose gelelectrophoresis followed by Western blotting. Three out of 7 monoclonal antibodies to PS did not detect PS after thrombin cleavage on an immunoblot after non-reduced SDS polyacrylamide gelelectrophoresis. These 3 antibodies gave a significant shortening of the prolonged APTT induced by the addition of APC to normal plasma, indicating that these monoclonals inhibited the cofactor function of PS. The other 4 monoclonals to PS that did detect PS after thrombin cleavage on an immunoblot, gave only a minor inhibition of the PS cofactor function.

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Marcovina, S., R. Coppola, M. P. Protti, C. Gelfi, and P. M. Mannucci. "EDTA-DEPENDENT MONOCLONAL ANTIBODIES TO HUMAN PROTEIN S." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644294.

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Splenocytes from a Balb/c mouse immunized with purified human protein S (PS) were fused with murine hybridoma cell line SP2/0-Agl4 and cultured in Iscove's medium without addition of fetal bovine serum. Hybrid supernatants were screened for the presence of specific antibodies by solid-phase ELISA and cloned by the limiting dilution technique. Pour clones, named S2, S3, S8, and S10, were selected, recloned several times, and injected intraperitoneally into Balb/c mice for the production of antibody-rich ascitic fluid. The monoclonal antibodies (Mabs), all of IgGl subclass with k light chain, were purified from ascitic fluid by Protein-A chromatography. The specificity of Mabs was controlled by the immunoblotting technique: the Mabs appeared to react only with two plasma proteins, one with a MW of about 70.000 dal tons comigrating with purified PS, and the other with a MW >300.000 da that is likely to be the C4b-binding protein-PS complex. No interaction has been observed with PS-depleted plasma. As tested by a fluid phase radio immunoassay, the binding of Mabs to PS was significantly higher in the presence of EDTA while was totally inhibited in the presence of Ca2+. Scatchard plot analysis of the binding between 125I-PS and Mabs showed that the binding affinity of the antibodies ranged from 108 to 109 1/mol. Each EDTA-dependent Mab was then immobilized on Sepharose 4B-CNBr and used to purify PS from barium precipitation of citrated plasma. The fraction eluted with 2 mmol of CaCl2 from the immunoadsorbent appeared to contain only two proteins when stained with Cocmassie Blue. By immuno blotting, all Mabs reacted with both proteins, one comigrating with purified PS and the other with a MW >300.000. Essentially homogeneous PS, free from the high MW component, was obtained when the barium citrate adsorbate was applied to a DEAE-Sephadex column and the protein peack containing the balk of PS was sussequently applied to the immunoadsorbent and eluted with 2 mmol CaCl2.In summary, we have described an unusual set of EDTA-dependent monoclonal antibodies to PS and their use for the purification of homogeneous protein S from human plasma.

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Frazier, D., Shu Wha Lin, J. Ware, Kenneth Smith, Howard Reisner, M. DeSerres, A. Wallmark, R. Ljung, I. M. Nilsson, and D. W. Stafford. "MAPPING OF 6 MONOCLONAL ANTIBODIES TO HUMAN FACTOR IX." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643565.

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In order to map the regions of human factor IX recognized by monoclonal antibodies we have inserted random fragments of the coding region of the cDNA for human factor IX into the lambda phage expression vector, lambda gtll. The resultant recombinant phage were screened with monoclonal antibodies, the immunoreactive phage were isolated, and the DNA of the inserted fragment was sequenced to determine which amino acids were immunoreactive. This data, coupled with data obtained from the use of specific fragments of human factor IX expressed in E. coli from a T7 phage promoter, has allowed us to map the location of several epitopes on the surface of the factor IX molecule. In those cases where the antibodies are specific for human factor IX, additional narrowing of the epitope is possible by comparing the amino acid sequence of human factor IX to the bovine molecule. Six monoclonal antibodies from 3 different laboratories have been mapped. The immunodominant epitopes appear to be the amino terminus of the activation peptide, the amino terminus of the heavy chain and the epidermal growth factor domains.

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Junjie, Chen, Chen Ping, and Jiang Jinqing. "Production and characterization of monoclonal antibodies against marbofloxacin." In 2011 International Conference on Human Health and Biomedical Engineering (HHBE). IEEE, 2011. http://dx.doi.org/10.1109/hhbe.2011.6029044.

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Furihata, Kenichi, Diane J. Nugent, Amy L. Bissonette, Elizabeth Vokac, and Thomas J. Kunicki. "PRODUCTION OF HUMAN MONOCLONAL ANTIBODIESSPECIFIC FOR PLATELET MEMBRANE GLYCOPROTEIN IIIa." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643705.

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Human monoclonal antibodies specific for platelet membrane glycoproteins (GPs) arepotentially important reagentsfor studies of the immunogenicity of membrane glycoproteins. A human monoclonalautoantibody, 5E5, reactive with plateletGPIIIa has been developed (Nugent, et al.,Blood, 1987, in press). In this report, we describe the production of additional human monoclonal antibodies specific for GPIIIa. Peripheral blood lymphocytes fromone patient with post-transfusion purpur(PTP) and one woman who had delivered an infant with neonatal alloimmune thrombocytopenic purpura (NATP) were used as a source of antigen-specific lymphocytes. A B-lympho-cyte-enriched population was transformed with Epstein Barr virus, strain B95-8, and cultured in microtiter plates. After two weeks, culture supernatants were screened by an antigen-capture ELISA wherein murine monoclonal antibody specificfor the GPIIb-IIIa complex was used to holdcorresponding antigen from a lysate ofnormal platelets. B-lymphoblastoid cell lines producing IgG and/or IgM antibodies were expanded and either cloned by limiting dilution technqiue or hybridized with a HAT-sensitive, ouabain-resistant heterohybrid fusion line, F6, using polyethylene glycol. Hybridomas were selected in medium containing HAT andouabain. After twoweeks, hybridomas producing anti-GPIIb and/or anti-GPIIIa antibody were cloned by limiting dilution. Culture supernatants from cloned B-lymphoblastoid cell lines and cloned hybridomas were rescreened by ELISA wherein affinity-purified GPIIIa or other platelet GP weredirectly conjugatedto microtiter plates. One IgM antibody produced by acloned B-lymphoblastoid cellline (CH16) andtwo IgG antibodies produced bycloned hybridomas(Del5.19 and Del5.23) were shownto react with GPIIIa but not other GP. Further characterization of these human monoclonal antibodies, produced continuouslyin culture now for four months, is in progress.

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Brettler, D., A. A. Forsberg, P. Levine, J. Petillo, K. Lamon, and J. Sullivan. "FACTOR VIII:C PURIFIED FROM PLASMA VIA MONOCLONAL ANTIBODIES: HUMAN STUDIES." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643923.

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Factor VIII:C purified utilizing a mouse monoclonal antibody to FVIII:VWF was used exclusively for 6 months to treat hemorrhages on a demand basis in 7 patients with severe hemophilia A and no inhibitor. The mean age of the patients was 26.1 years with a range of 16-39 years. The dose administered was from 15-18 u/kg at the time of hemorrhage. The patients infused on the average of once every 5 days. One patient required 40-50 u/kg every day for 3 days secondary to an automobile accident. Laboratory assessments included: a fall-off study to determine the factor VIII half-life both when the study commenced and after 6 months on study; inhibitor levels, and ELISA assay to detect antibody to mouse protein. Additionally, immunological data including quantitative T cell subsets and skin testing on each patient was obtained on entrance to the study, at 1 month, 3 months and at conclusion in order to ascertain whether immune function in these patients would improve with the use of purer factor concentrate. The initial mean half-life of the infused concentrate was 15.4 hours ± 2.2 with a range of 12.6 to 18.4 hours. The mean half-life after the patients had been on the concentrate for 6 months was 17.5 ± 5.9 hours (range 11.0 to 29 hours). No inhibitor developed in any patient. Six of seven patients did not develop significant levels of anti-mouse IgG antibody. One patient had a rheumatoid factor which interfered with the ELISA assay for anti-mouse antibody and thus its presence could not be assessed. There were no adverse reactions to the material, and hemostatic efficacy was judged as excellent. There were no significant changes in quantitative T cell subsets. Three out of six patients lost their previous total skin test anergy and two other patients increased the number of antigens to which they reacted. This concentrate proved to be safe and efficacious, to have excellent half-life, and to be associated with apparent improvement in the immune response.

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Berndt, M. C., X. Du, L. Beutler, W. J. Booth, and P. A. Castaldi. "LOCALIZATION OF FUNCTIONAL DOMAINS ON HUMAN PLATELET GP Ib-IX COMPLEX BY EPITOPE ANALYSIS WITH MONOCLONAL ANTIBODIES." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642923.

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There is now considerable evidence that glycoprotein (GP) Ib plays an important functional role in the von Willebrand factor (vWF)-dependent adhesion of platelets to exposed vascular subendothelium and in the a-thrombin activation of platelets, and that GP IX is important for quinine/quinidine drug-dependent antibody platelet recognition. GP Ib (Mr = 170 KD) consists of two disulfide-linked subunits, Iba (Mr = 135 KD) and Ibβ (Mr = 25 KD), and exists as a heterodimer complex with GP IX (Mr = 22 KD). In this study we have used a panel of 10 antiGP Ib-IX complex monoclonal antibodies to define the functional domains on this complex. Immunoprecipitation of trypsin-treated GP Ib-IX complex revealed that the monoclonal antibodies mapped into three distinct groups: FMC 25, AK 1 and SZ 1, epitopes on the membrane-associated fragment (GP IX and an ≃25 KD remnant of the α-chain disulfide linked to the β-chain); AK 3 and WM 23, epitopes on the central macroglycopeptide core (90 KD); AN 51, SZ 2, AK 2, AP 1 and HIP 1, epitopes on peptide tail (45 KD). Crossblocking studies indicated that with the exception of AK 1 and SZ 1, the monoclonal antibodies were directed against distinct epitopes. All five monoclonal antibodies directed against the peptide tail region blocked ristocetin-dependent vWF-platelet interaction whereas the other five monoclonal antibodies were without effect, indicating that the 45 KD peptide tail region at the plasma end of the α-chain of GP Ib contained the vWF binding domain. Similarly, only the three monoclonal antibodies directed against the membrane-associated region interfered with drug-dependent antibody-platelet interaction.By western blot analysis, α-thrombin bound to the 45 KD peptide tail region. However, only AP 1 interfered significantly with the α-thrombin-dependent aggregation of platelets. This panel of epitope-defined monoclonal antibodies should be of value in further defining the structure-function relationships of this important membrane complex.

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Zhao, Huiwu, Jiping Zhang, Ramdev Puligedda, Cezary Swider, Paul Simon, Baron Heimbach, Sharad Adekar, Maureen Murphy, Hossein Borghaei, and Scott Dessain. "Abstract 3625: Tumor-specific human monoclonal antibodies isolated from cancer patients." In Proceedings: AACR Annual Meeting 2014; April 5-9, 2014; San Diego, CA. American Association for Cancer Research, 2014. http://dx.doi.org/10.1158/1538-7445.am2014-3625.

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Rathanaswami, Palaniswami, Oscar Pan, Sarah Ross, Chadwick King, Ian N. Foltz, and Paul Elvin. "Abstract 558: Targeting tumour heparanase activity using fully human monoclonal antibodies." In Proceedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-558.

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Reports on the topic "Human monoclonal antibodies (humAbs)"

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Wright, D. C. The Development of Human Monoclonal Antibodies against Ricin by In vitro Stimulation (SBIR 90.I). Fort Belvoir, VA: Defense Technical Information Center, February 1991. http://dx.doi.org/10.21236/ada237491.

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Spiegel, Yitzhak, Michael McClure, Itzhak Kahane, and B. M. Zuckerman. Characterization of the Phytophagous Nematode Surface Coat to Provide New Strategies for Biocontrol. United States Department of Agriculture, November 1995. http://dx.doi.org/10.32747/1995.7613015.bard.

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Chemical composition and biological role of the surface coat (SC) of the root-knot nematodes, Meloidogyne spp. are described. SC proteins of M. incognita race 3 infective juveniles (J2) were characterized by electrophoresis and western blotting of extracts from radioiodine and biotin-labelled nematodes. J2 labelled with radioiodine and biotin released 125I and biotin-labelled molecules into water after 20 hours incubation, indicating that SC proteins may be loosely attached to the nematode. Antiserum to the principal protein reacted with the surface of live J2 and with surface proteins previously separated by electrophoresis. Human red blood cells (HRBC) adhered to J2 of several tylenchid nematodes over the entire nematode body. HRBC adhered also to nylon fibers coated with SC extracted from M. javanica J2; binding was Ca++/Mg++ dependent, and decreased when the nylon fibers were coated with bovine serum albumin, or pre-incubated with fucose and mannose. These experiments support a working hypothesis that RBC adhesion involves carbohydrate moieties of HRBC and carbohydrate-recognition domain(s) (CRD) distributed on the nematode surface. To our knowledge, this is the first report of a surface CRD i the phylum Nematoda. Gold-conjugated lectins and neoglycoproteins combined with silver enhancement have been used for the detection of carbohydrates and CRD, respectively, on the SC of M. javanica J2. Biotin reagents were used to trace surface proteins, specifically, on live J2. The labile and transitory nature of the SC was demonstrated by the dynamics of HRBC adherence to detergent-treated J2, J2 at different ages or fresh-hatched J2 held at various temperatures. SC recovery was demonstrated also by a SDS-PAGE profile. Monoclonal antibodies developed to a cuticular protein of M. incognita J2 gave a slight, but significant reduction in attachment of Pasteuria penetrans spores. Spore attachment as affected by several enzymes was inconsistent: alcian blue, which specifically blocks sulfyl groups, had no afffect on spore attachment. Treatment with cationized ferritin alone or catonized ferritin following monoclonal antibody caused significant decreases in spore attachment. Those results suggest a role in attachment by negatively charged groups.

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