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Journal articles on the topic 'Half antibody'

Author: Grafiati

Published: 4 June 2021

Last updated: 9 February 2022

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1

Herrington-Symes, Annabelle Patricia, Monika Farys, Hanieh Khalili, and Steve Brocchini. "Antibody fragments: Prolonging circulation half-life special issue-antibody research." Advances in Bioscience and Biotechnology 04, no. 05 (2013): 689–98. http://dx.doi.org/10.4236/abb.2013.45090.

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2

Wu, Shangquan, Hong Liu, Xin M. Liang, Xiaoping Wu, Baomin Wang, and Qingchuan Zhang. "Highly Sensitive Nanomechanical Immunosensor Using Half Antibody Fragments." Analytical Chemistry 86, no. 9 (2014): 4271–77. http://dx.doi.org/10.1021/ac404065m.

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3

Zalevsky, Jonathan, Aaron K. Chamberlain, Holly M. Horton, et al. "Enhanced antibody half-life improves in vivo activity." Nature Biotechnology 28, no. 2 (2010): 157–59. http://dx.doi.org/10.1038/nbt.1601.

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4

Makaraviciute, Asta, Carolyn D. Jackson, Paul A. Millner, and Almira Ramanaviciene. "Considerations in producing preferentially reduced half-antibody fragments." Journal of Immunological Methods 429 (February 2016): 50–56. http://dx.doi.org/10.1016/j.jim.2016.01.001.

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5

Chapman, Andrew P., Pari Antoniw, Mariangela Spitali, Shauna West, Sue Stephens, and David J. King. "Therapeutic antibody fragments with prolonged in vivo half-lives." Nature Biotechnology 17, no. 8 (1999): 780–83. http://dx.doi.org/10.1038/11717.

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6

Sievers, Stuart A., Louise Scharf, Anthony P. West, and Pamela J. Bjorkman. "Antibody engineering for increased potency, breadth and half-life." Current Opinion in HIV and AIDS 10, no. 3 (2015): 151–59. http://dx.doi.org/10.1097/coh.0000000000000148.

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7

Chen, Xiujuan, Ying Wang, and Yifeng Li. "Removing half antibody byproduct by Protein A chromatography during the purification of a bispecific antibody." Protein Expression and Purification 172 (August 2020): 105635. http://dx.doi.org/10.1016/j.pep.2020.105635.

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8

Yoshida, H., S. Maeda, K. Ogura, et al. "Short half-life of serum anti-CagA antibody: Comparison with conventional anti-Helicobacter pylori antibody." Gastroenterology 114 (April 1998): A342. http://dx.doi.org/10.1016/s0016-5085(98)81386-3.

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9

Herbener, Peter, Kurt Schönfeld, Martin König, et al. "Functional relevance of in vivo half antibody exchange of an IgG4 therapeutic antibody-drug conjugate." PLOS ONE 13, no. 4 (2018): e0195823. http://dx.doi.org/10.1371/journal.pone.0195823.

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10

Hinton, Paul R., Joanna M. Xiong, Mary G. Johlfs, Meina Tao Tang, Stephen Keller, and Naoya Tsurushita. "An Engineered Human IgG1 Antibody with Longer Serum Half-Life." Journal of Immunology 176, no. 1 (2005): 346–56. http://dx.doi.org/10.4049/jimmunol.176.1.346.

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11

Sharma, Harsh, and Raj Mutharasan. "Half Antibody Fragments Improve Biosensor Sensitivity without Loss of Selectivity." Analytical Chemistry 85, no. 4 (2013): 2472–77. http://dx.doi.org/10.1021/ac3035426.

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12

Lourenço, Bianca N., Rúben F. Pereira, Cristina C. Barrias, Claudia Fischbach, Carla Oliveira, and Pedro L. Granja. "Engineering Modular Half-Antibody Conjugated Nanoparticles for Targeting CD44v6-Expressing Cancer Cells." Nanomaterials 11, no. 2 (2021): 295. http://dx.doi.org/10.3390/nano11020295.

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Gastric cancer (GC) remains a major cause of death worldwide mainly because of the late detection in advanced stage. Recently, we proposed CD44v6 as a relevant marker for early detection of GC, opening new avenues for GC-targeted theranostics. Here, we designed a modular nanoscale system that selectively targets CD44v6-expressing GC cells by the site-oriented conjugation of a new-engineered CD44v6 half-antibody fragment to maleimide-modified polystyrene nanoparticles (PNPs) via an efficient bioorthogonal thiol-Michael addition click chemistry. PNPs with optimal particle size (200 nm) for crossing a developed biomimetic CD44v6-associated GC stromal model were further modified with a heterobifunctional maleimide crosslinker and click conjugated to the novel CD44v6 half-antibody fragment, obtained by chemical reduction of full antibody, without affecting its bioactivity. Collectively, our results confirmed the specific targeting ability of CD44v6-PNPs to CD44v6-expressing cells (1.65-fold higher than controls), highlighting the potential of CD44v6 half-antibody conjugated nanoparticles as promising and clinically relevant tools for the early diagnosis and therapy of GC. Additionally, the rational design of our nanoscale system may be explored for the development of several other nanotechnology-based disease-targeted approaches.

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13

Klein, Jerry L., Marilyn N. Ling, Peter K. Leichner, Kenneth A. Kopher, Robert A. Rostock, and Stanley E. Order. "A model system that predicts effective half-life for radiolabeled antibody therapy." International Journal of Radiation Oncology*Biology*Physics 11, no. 8 (1985): 1489–94. http://dx.doi.org/10.1016/0360-3016(85)90337-2.

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14

Tang, Jiaqin, Xudong Zhang, Tao Chen, Ying Wang, and Yifeng Li. "Removal of half antibody, hole-hole homodimer and aggregates during bispecific antibody purification using MMC ImpRes mixed-mode chromatography." Protein Expression and Purification 167 (March 2020): 105529. http://dx.doi.org/10.1016/j.pep.2019.105529.

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15

Gomez, Natalia, Agatha Wieczorek, Fang Lu, et al. "Culture temperature modulates half antibody and aggregate formation in a Chinese hamster ovary cell line expressing a bispecific antibody." Biotechnology and Bioengineering 115, no. 12 (2018): 2930–40. http://dx.doi.org/10.1002/bit.26803.

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16

Mifflin, T. E., R. W. Forsman, and D. E. Bruns. "Interaction of immobilized anti-salivary amylase antibody with human macroamylases: implications for use in a pancreatic amylase assay to distinguish macroamylasemia from acute pancreatitis." Clinical Chemistry 35, no. 8 (1989): 1651–54. http://dx.doi.org/10.1093/clinchem/35.8.1651.

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Abstract We examined the ability of an immobilized antibody to salivary amylase (Clin Chem 1985;33:1283-8) to react with amylase in macroamylasemic sera. The antibody removed 50% (SD 23%) of the total amylase activity from 39 macroamylase sera, a percentage indistinguishable (P greater than 0.75) from the percentage removed from concurrently analyzed sera from healthy volunteers (49%, SD 11%). Electrophoretic analysis of 23 macroamylasemic sera revealed that the antibody removed only part of the macroamylase band(s) in 71% of the cases. We conclude that the mean isoenzyme composition of the macroamylase complexes is essentially identical to the mean isoenzyme distribution in normal sera (i.e., about half salivary and half pancreatic amylase). Further, the immobilized antibody can be used to distinguish most patients with macroamylasemia from those with acute pancreatitis, because sera from the latter contain an increased proportion (greater than 80%) of pancreatic amylase.

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17

Finelli, Lyn, Yoonyoung Choi, and Edward Goldstein. "Number needed to immunize to prevent RSV with extended half-life monoclonal antibody." Vaccine 38, no. 34 (2020): 5474–79. http://dx.doi.org/10.1016/j.vaccine.2020.06.034.

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18

Malik, N., S. K. Luthra, P. Price, and F. Brady. "P17. Radiolabelling of a half mustard prodrug for antibody-directed enzyme prodrug therapy." Nuclear Medicine Communications 23, no. 4 (2002): 410. http://dx.doi.org/10.1097/00006231-200204000-00097.

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19

Lee, Tong-Young, Robert M. Tjin Tham Sjin, Shahla Movahedi, et al. "Linking Antibody Fc Domain to Endostatin Significantly Improves Endostatin Half-life and Efficacy." Clinical Cancer Research 14, no. 5 (2008): 1487–93. http://dx.doi.org/10.1158/1078-0432.ccr-07-1530.

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20

Valeo, Tom. "Antibody Reduced Plaque By More Than Half in Animal Model of Alzheimerʼs Disease". Neurology Today 13, № 2 (2013): 20–23. http://dx.doi.org/10.1097/01.nt.0000426344.08137.70.

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21

Yeung, Yik Andy, Xiumin Wu, Arthur E. Reyes, et al. "A Therapeutic Anti–VEGF Antibody with Increased Potency Independent of Pharmacokinetic Half-life." Cancer Research 70, no. 8 (2010): 3269–77. http://dx.doi.org/10.1158/0008-5472.can-09-4580.

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22

McGibbon, Emily, Katherine Bornschlegel, and Sharon Balter. "Half a Diagnosis: Gap in Confirming Infection among Hepatitis C Antibody-positive Patients." American Journal of Medicine 126, no. 8 (2013): 718–22. http://dx.doi.org/10.1016/j.amjmed.2013.01.031.

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23

van Dolleweerd, Craig J., Daniel Chargelegue, and Julian K. C. Ma. "Characterization of the Conformational Epitope of Guy's 13, a Monoclonal Antibody That Prevents Streptococcus mutans Colonization in Humans." Infection and Immunity 71, no. 2 (2003): 754–65. http://dx.doi.org/10.1128/iai.71.2.754-765.2003.

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ABSTRACT Guy's 13 is a mouse monoclonal antibody which recognizes streptococcal antigen I/II (SA I/II), a major cell surface glycoprotein of Streptococcus mutans. In a number of clinical trials, this antibody has been shown to prevent colonization in the human oral cavity. The aim of this study was to identify the SA I/II epitope recognized by Guy's 13. The data suggest that the epitope is conformational, delimited by two noncontiguous regions of the antigen: residues 45 to 457, within the N-terminal half of SA I/II, and residues 816 to 983, within the C-terminal half. In fluid-phase immunoassays a strict requirement for the simultaneous presence of both regions was demonstrated for antibody binding. Furthermore, these two regions of SA I/II were shown to have the ability to interact with each other in the absence of Guy's 13 antibody, suggesting that the normal conformation of SA I/II might be determined by the interaction of these two regions.

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24

Keith, James C., Thomas J. Ferranti, Bibhu Misra, et al. "Evaluation of Recombinant Human Factor IX: Pharmacokinetic Studies in the Rat and the Dog." Thrombosis and Haemostasis 73, no. 01 (1995): 101–5. http://dx.doi.org/10.1055/s-0038-1653732.

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SummaryThe pharmacokinetics of intravenously administered recombinant human factor IX (rhFIX) were studied in Sprague-Dawley rats and Beagle dogs. Rats received rhFIX (50 IU/kg once daily) for 28 days, and the plasma half-life was 5 h. Anti-Human Factor IX serum antibody levels were found in only 1 of 12 rats. The pharmacokinetic profiles of rhFIX or Mononine™, a purified human plasma-derived factor IX, after single 100 IU/kg IV doses in dogs, were similar. Peak plasma concentrations of rhFIX and Mononine™ were 4–5 μg/ml. The mean plasma half-lives were 13.2 ± 1.6 h for rhFIX and 13.3 ± 1.6 h for Mononine™. Dogs also received rhFIX (40 IU/kg IV, daily) for 28 days or Mononine™ (40 IU/kg IV daily) for 14 days. Anti-human Factor IX serum antibody levels were determined for each compound. Pharmacokinetic half-lives decreased in these treated dogs which developed antihuman Factor IX antibodies. The antibody responses in 28 day rhFIX (40 IU/kg) dogs were similar to 14 day Mononine™ (40 IU/kg) dogs.

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25

Burke, John M., Anna Katharina Wilkins, Andrew Matteson, Lore Gruenbaum, and Josh F. Apgar. "Computational exploration of mechanistic determinants of antibody drug-conjugate pharmacokinetics using quantitative systems pharmacology modeling strategies." Journal of Clinical Oncology 35, no. 15_suppl (2017): e14000-e14000. http://dx.doi.org/10.1200/jco.2017.35.15_suppl.e14000.

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e14000 Background: The pharmacokinetics of antibody drug conjugate (ADC) therapeutics typically show a discrepancy between the PK of total antibody (conjugated and unconjugated antibody) and that of conjugated antibody, carrying one or more payload molecules This discrepancy is often attributed to deconjugation (Kamath, 2014), however recent evidence suggests that the underlying mechanisms may be more complex. Methods: This work employs a computational quantitative systems pharmacology (QSP) approach to understand the impact of drug antibody ratio (DAR) and the resulting changes in molecular properties on overall PK and relative payload disposition as observed in preclinical and clinical studies. Results: Using QSP approaches, the model (1) describes the kinetics of individual DAR species and agrees well with typical ADC PK, individual DAR PK, and average DAR measurements in vivo; (2), quantitatively describes the trade-off between higher DAR and lower exposure; consequently, we predict that ADC2 is half as potent as ADC4 and ADC8, which are equipotent; (3) longer mAb half-life reduces payload delivery after multiple doses; and (4) ADC half-life affects the percent of payload delivered through different mechanisms. Conclusions: A QSP model describing mechanism is a useful tool to translate and understand PK from preclinical species to human, by acting as a central repository of data, knowledge, and hypotheses. It provided a rational basis to generate testable hypotheses and provide early insights into complex ADC PK data and established the benefit of using computational models to design novel ADCs and to optimize the discovery and development of existing ADCs.

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26

Shapiro, Renée I., Tatiana Plavina, Brian R. Schlain, et al. "Development and validation of immunoassays to quantify the half-antibody exchange of an IgG4 antibody, natalizumab (Tysabri®) with endogenous IgG4." Journal of Pharmaceutical and Biomedical Analysis 55, no. 1 (2011): 168–75. http://dx.doi.org/10.1016/j.jpba.2011.01.006.

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27

Li, Qiyu, Wenjing Li, Keyuan Xu, et al. "PEG Linker Improves Antitumor Efficacy and Safety of Affibody-Based Drug Conjugates." International Journal of Molecular Sciences 22, no. 4 (2021): 1540. http://dx.doi.org/10.3390/ijms22041540.

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Antibody drug conjugates (ADCs) have become an important modality of clinical cancer treatment. However, traditional ADCs have some limitations, such as reduced permeability in solid tumors due to the high molecular weight of monoclonal antibodies, difficulty in preparation and heterogeneity of products due to the high drug/antibody ratio (4–8 small molecules per antibody). Miniaturized ADCs may be a potential solution, although their short circulation half-life may lead to new problems. In this study, we propose a novel design strategy for miniaturized ADCs in which drug molecules and small ligand proteins are site-specifically coupled via a bifunctional poly(ethylene glycol) (PEG) chain. The results showed that the inserted PEG chains significantly prolonged the circulation half-life but also obviously reduced the cytotoxicity of the conjugates. Compared with the conjugate ZHER2-SMCC-MMAE (HM), which has no PEG insertion, ZHER2-PEG4K-MMAE (HP4KM) and ZHER2-PEG10K-MMAE (HP10KM) with 4 or 10 kDa PEG insertions have 2.5- and 11.2-fold half-life extensions and 4.5- and 22-fold in vitro cytotoxicity reductions, respectively. The combined effect leads to HP10KM having the most ideal tumor therapeutic ability at the same dosages in the animal model, and its off-target toxicity was also reduced by more than 4 times compared with that of HM. These results may indicate that prolonging the half-life is very helpful in improving the therapeutic capacity of miniaturized ADCs. In the future, the design of better strategies that can prolong half-life without affecting cytotoxicity may be useful for further improving the therapeutic potential of these molecules.

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28

Fredman, P., L. Mattsson, K. Andersson, et al. "Characterization of the binding epitope of a monoclonal antibody to sulphatide." Biochemical Journal 251, no. 1 (1988): 17–22. http://dx.doi.org/10.1042/bj2510017.

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An IgG1 monoclonal antibody, Sulph I, reacting with sulphatide (3′-sulphogalactosylceramide), was produced by immunizing Balb/c mice with that glycolipid coated on Salmonella minnesota bacterial membrane. Radioimmunodetection of the binding of the monoclonal antibody to structurally related glycolipids adsorbed to microtitre plates or chromatographed on thin-layer plates was used to determine its binding epitope. The antibody showed similar binding avidity to three sulphated glycolipids: sulphatide, sulpholactosylceramide and seminolipid. Lysosulphatide did bind the antibody, but, compared with sulphatide, 30 times more antigen was needed for half-maximal binding. Bis(sulphogangliotriosyl)ceramide and bis-sulphogangliotetraosylceramide did not bind the antibody. These results suggest that terminal galactose-3-O-sulphate and part of the hydrophobic region of the glycolipid are recognized by the Sulph I antibody.

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29

Davé, Emma, Ralph Adams, Oliver Zaccheo, et al. "Fab-dsFv: A bispecific antibody format with extended serum half-life through albumin binding." mAbs 8, no. 7 (2016): 1319–35. http://dx.doi.org/10.1080/19420862.2016.1210747.

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30

Mackness, Brian C., Julie A. Jaworski, Ekaterina Boudanova, et al. "Antibody Fc engineering for enhanced neonatal Fc receptor binding and prolonged circulation half-life." mAbs 11, no. 7 (2019): 1276–88. http://dx.doi.org/10.1080/19420862.2019.1633883.

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31

Vallée, E., C. Heuer, JM Collins-Emerson, J. Benschop, and PR Wilson. "Serological patterns, antibody half-life and shedding in urine ofLeptospiraspp. in naturally exposed sheep." New Zealand Veterinary Journal 63, no. 6 (2015): 301–12. http://dx.doi.org/10.1080/00480169.2015.1049668.

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32

Hong, Hao, Jiangtao Sun, and Weibo Cai. "Radionuclide-Based Cancer Imaging Targeting the Carcinoembryonic Antigen." Biomarker Insights 3 (January 2008): BMI.S1124. http://dx.doi.org/10.4137/bmi.s1124.

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Carcinoembryonic antigen (CEA), highly expressed in many cancer types, is an important target for cancer diagnosis and therapy. Radionuclide-based imaging techniques (gamma camera, single photon emission computed tomography [SPECT] and positron emission tomography [PET]) have been extensively explored for CEA-targeted cancer imaging both preclinically and clinically. Briefly, these studies can be divided into three major categories: antibody-based, antibody fragment-based and pretargeted imaging. Radiolabeled anti-CEA antibodies, reported the earliest among the three categories, typically gave suboptimal tumor contrast due to the prolonged circulation life time of intact antibodies. Subsequently, a number of engineered anti-CEA antibody fragments (e.g. Fab’, scFv, minibody, diabody and scFv-Fc) have been labeled with a variety of radioisotopes for CEA imaging, many of which have entered clinical investigation. CEA-Scan (a 99mTc-labeled anti-CEA Fab’ fragment) has already been approved by the United States Food and Drug Administration for cancer imaging. Meanwhile, pre-targeting strategies have also been developed for CEA imaging which can give much better tumor contrast than the other two methods, if the system is designed properly. In this review article, we will summarize the current state-of-the-art of radionuclide-based cancer imaging targeting CEA. Generally, isotopes with short half-lives (e.g. 18F and 99mTc) are more suitable for labeling small engineered antibody fragments while the isotopes with longer half-lives (e.g. 123I and 111In) are needed for antibody labeling to match its relatively long circulation half-life. With further improvement in tumor targeting efficacy and radiolabeling strategies, novel CEA-targeted agents may play an important role in cancer patient management, paving the way to “personalized medicine”.

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33

Dalby, Tine, Jesper Westphal Petersen, Zitta B. Harboe, and Karen Angeliki Krogfelt. "Antibody responses to pertussis toxin display different kinetics after clinical Bordetella pertussis infection than after vaccination with an acellular pertussis vaccine." Journal of Medical Microbiology 59, no. 9 (2010): 1029–36. http://dx.doi.org/10.1099/jmm.0.020826-0.

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The measurement of IgG anti-pertussis toxin (IgG anti-PT) antibodies by ELISA is a frequently used method for studying the antibody responses after pertussis vaccination and after Bordetella pertussis infection. Such responses vary according to the different vaccines used as well as to the immunization and infection history of the participants. In the present study, the decay kinetics of the IgG anti-PT antibody response was determined for 71 Danish children and adults with bacteriologically confirmed B. pertussis infection and for 20 Danish adults booster-vaccinated with an acellular pertussis vaccine. For both groups, biphasic decay was seen, but the individual antibody responses varied greatly. No differences related to age were seen. Within each group, individual decay profiles showed parallel log-linear decay for the late part of the response. Antibody half-life was calculated for the late, slower part of the biphasic response curves for both groups (>5 months after diagnosis for individuals with confirmed infection; >3 months for vaccinated individuals). The median half-life for post-infection antibodies was 221 days [interquartile range (IQR) 159–314 days, 36 individuals], and the median half-life for post-vaccination antibodies was 508 days (IQR 428–616 days, 14 individuals). This difference was statistically significant (P<0.0001). Thus, in this setting, we found that the IgG anti-PT antibody decay after an infection with B. pertussis is more than twice as fast as the decay after booster vaccination with an acellular pertussis vaccine. Such knowledge of the IgG anti-PT decay kinetics is crucial for interpretation of serological data that will be used either for diagnosis or for epidemiological studies and surveillance of B. pertussis infections.

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34

Kalfa, Theodosia A. "Warm antibody autoimmune hemolytic anemia." Hematology 2016, no. 1 (2016): 690–97. http://dx.doi.org/10.1182/asheducation-2016.1.690.

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Abstract Autoimmune hemolytic anemia (AIHA) is a rare and heterogeneous disease that affects 1 to 3/100 000 patients per year. AIHA caused by warm autoantibodies (w-AIHA), ie, antibodies that react with their antigens on the red blood cell optimally at 37°C, is the most common type, comprising ∼70% to 80% of all adult cases and ∼50% of pediatric cases. About half of the w-AIHA cases are called primary because no specific etiology can be found, whereas the rest are secondary to other recognizable underlying disorders. This review will focus on the postulated immunopathogenetic mechanisms in idiopathic and secondary w-AIHA and report on the rare cases of direct antiglobulin test–negative AIHA, which are even more likely to be fatal because of inherent characteristics of the causative antibodies, as well as because of delays in diagnosis and initiation of appropriate treatment. Then, the characteristics of w-AIHA associated with genetically defined immune dysregulation disorders and special considerations on its management will be discussed. Finally, the standard treatment options and newer therapeutic approaches for this chronic autoimmune blood disorder will be reviewed.

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35

McLaughlin, P., A. J. Grillo-López, B. K. Link, et al. "Rituximab chimeric anti-CD20 monoclonal antibody therapy for relapsed indolent lymphoma: half of patients respond to a four-dose treatment program." Journal of Clinical Oncology 16, no. 8 (1998): 2825–33. http://dx.doi.org/10.1200/jco.1998.16.8.2825.

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PURPOSE The CD20 antigen is expressed on more than 90% of B-cell lymphomas. It is appealing for targeted therapy, because it does not shed or modulate. A chimeric monoclonal antibody more effectively mediates host effector functions and is itself less immunogenic than are murine antibodies. PATIENTS AND METHODS This was a multiinstitutional trial of the chimeric anti-CD20 antibody, IDEC-C2B8. Patients with relapsed low grade or follicular lymphoma received an outpatient treatment course of IDEC-C2B8 375 mg/m2 intravenously weekly for four doses. RESULTS From 31 centers, 166 patients were entered. Of this intent-to-treat group, 48% responded. With a median follow-up duration of 11.8 months, the projected median time to progression for responders is 13.0 months. Serum antibody levels were sustained longer after the fourth infusion than after the first, and were higher in responders and in patients with lower tumor burden. The majority of adverse events occurred during the first infusion and were grade 1 or 2; fever and chills were the most common events. Only 12% of patients had grade 3 and 3% grade 4 toxicities. A human antichimeric antibody was detected in only one patient. CONCLUSION The response rate of 48% with IDEC-C2B8 is comparable to results with single-agent cytotoxic chemotherapy. Toxicity was mild. Attention needs to be paid to the rate of antibody infusion, with titration according to toxicity. Further investigation of this agent is warranted, including its use in conjunction with standard chemotherapy.

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36

Ayoub, Houssein H., Hiam Chemaitelly, Monia Makhoul, et al. "Epidemiological impact of prioritising SARS-CoV-2 vaccination by antibody status: mathematical modelling analyses." BMJ Innovations 7, no. 2 (2021): 327–36. http://dx.doi.org/10.1136/bmjinnov-2021-000677.

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BackgroundVaccines against SARS-CoV-2 have been developed, but their availability falls far short of global needs. This study aimed to investigate the impact of prioritising available doses on the basis of recipient antibody status, that is by exposure status, using Qatar as an example.MethodsVaccination impact (defined as the reduction in infection incidence and the number of vaccinations needed to avert one infection or one adverse disease outcome) was assessed under different scale-up scenarios using a deterministic meta-population mathematical model describing SARS-CoV-2 transmission and disease progression in the presence of vaccination.ResultsFor a vaccine that protects against infection with an efficacy of 95%, half as many vaccinations were needed to avert one infection, disease outcome or death by prioritising antibody-negative individuals for vaccination. Prioritisation by antibody status reduced incidence at a faster rate and led to faster elimination of infection and return to normalcy. Further prioritisation by age group amplified the gains of prioritisation by antibody status. Gains from prioritisation by antibody status were largest in settings where the proportion of the population already infected at the commencement of vaccination was 30%–60%. For a vaccine that only protects against disease and not infection, vaccine impact was reduced by half, whether this impact was measured in terms of averted infections or disease outcomes, but the relative gains from using antibody status to prioritise vaccination recipients were similar.ConclusionsMajor health and economic gains can be achieved more quickly by prioritizing those who are antibody-negative while doses of the vaccine remain in short supply.

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37

Schoch, Angela, Hubert Kettenberger, Olaf Mundigl, et al. "Charge-mediated influence of the antibody variable domain on FcRn-dependent pharmacokinetics." Proceedings of the National Academy of Sciences 112, no. 19 (2015): 5997–6002. http://dx.doi.org/10.1073/pnas.1408766112.

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Here, we investigated the influence of the variable fragment (Fv) of IgG antibodies on the binding to the neonatal Fc receptor (FcRn) as well as on FcRn-dependent pharmacokinetics (PK). FcRn plays a key role in IgG homeostasis, and specific manipulation in the crystallizable fragment (Fc) is known to affect FcRn-dependent PK. Although the influence of the antigen-binding fragment (Fab) on FcRn interactions has been reported, the underlying mechanism is hitherto only poorly understood. Therefore, we analyzed the two IgG1 antibodies, briakinumab and ustekinumab, that have similar Fc parts but different terminal half-lives in human and systematically engineered variants of them with cross-over exchanges and varied charge distribution. Using FcRn affinity chromatography, molecular dynamics simulation, and in vivo PK studies in human FcRn transgenic mice, we provide evidence that the charge distribution on the Fv domain is involved in excessive FcRn binding. This excessive binding prevents efficient FcRn–IgG dissociation at physiological pH, thereby reducing FcRn-dependent terminal half-lives. Furthermore, we observed a linear correlation between FcRn column retention times of the antibody variants and the terminal half-lives in vivo. Taken together, our study contributes to a better understanding of the FcRn–IgG interaction, and it could also provide profound potential in FcRn-dependent antibody engineering of the variable Fab region.

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38

Bender, BS, TC Quinn, and JL Spivak. "Homosexual men with thrombocytopenia have impaired reticuloendothelial system Fc receptor-specific clearance." Blood 70, no. 2 (1987): 392–95. http://dx.doi.org/10.1182/blood.v70.2.392.392.

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Abstract Classic immune thrombocytopenia purpura (ITP) occurs predominantly in women and is associated with either normal or impaired Fc receptor- mediated clearance of antibody-coated cells. Recently, an increasing incidence of thrombocytopenia has been observed in homosexual men, but whether Fc receptor-mediated clearance of antibody-coated cells is normal or impaired in these men is unknown. To study this question, we measured the in vivo clearance of anti-Rho(D) IgG antibody-sensitized 51Cr-labeled autologous red cells in five homosexual men with thrombocytopenia without an evident cause. All five had antibodies to human immunodeficiency virus, and four had circulating immune complexes as determined by a Clq-binding assay. Two of the men tested also had an increase in platelet-associated IgG. In the four homosexual men with platelet counts of 20,000/microL or less, the clearance half-time of IgG-sensitized red cells was prolonged (mean, 106 minutes; range, 72 to 140 minutes) as compared with the clearance of such cells in five hematologically normal men (mean, 39 minutes; range 30 to 50 minutes; P less than .005). One homosexual man with a platelet count of 81,000/microL had a normal clearance half-time (30 minutes). Three patients whose platelet counts increased after corticosteroid therapy were restudied. In all three, the clearance of antibody-coated cells was shortened and returned to normal in the one patient who had achieved a complete remission. No correlation was observed between the presence of platelet-associated IgG or circulating immune complexes and the clearance half-time. These data indicate that severe thrombocytopenia occurring in homosexual men as in some patients with classic ITP is associated with defective in vivo Fc receptor-mediated clearance of antibody-coated cells.

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Bender, BS, TC Quinn, and JL Spivak. "Homosexual men with thrombocytopenia have impaired reticuloendothelial system Fc receptor-specific clearance." Blood 70, no. 2 (1987): 392–95. http://dx.doi.org/10.1182/blood.v70.2.392.bloodjournal702392.

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Classic immune thrombocytopenia purpura (ITP) occurs predominantly in women and is associated with either normal or impaired Fc receptor- mediated clearance of antibody-coated cells. Recently, an increasing incidence of thrombocytopenia has been observed in homosexual men, but whether Fc receptor-mediated clearance of antibody-coated cells is normal or impaired in these men is unknown. To study this question, we measured the in vivo clearance of anti-Rho(D) IgG antibody-sensitized 51Cr-labeled autologous red cells in five homosexual men with thrombocytopenia without an evident cause. All five had antibodies to human immunodeficiency virus, and four had circulating immune complexes as determined by a Clq-binding assay. Two of the men tested also had an increase in platelet-associated IgG. In the four homosexual men with platelet counts of 20,000/microL or less, the clearance half-time of IgG-sensitized red cells was prolonged (mean, 106 minutes; range, 72 to 140 minutes) as compared with the clearance of such cells in five hematologically normal men (mean, 39 minutes; range 30 to 50 minutes; P less than .005). One homosexual man with a platelet count of 81,000/microL had a normal clearance half-time (30 minutes). Three patients whose platelet counts increased after corticosteroid therapy were restudied. In all three, the clearance of antibody-coated cells was shortened and returned to normal in the one patient who had achieved a complete remission. No correlation was observed between the presence of platelet-associated IgG or circulating immune complexes and the clearance half-time. These data indicate that severe thrombocytopenia occurring in homosexual men as in some patients with classic ITP is associated with defective in vivo Fc receptor-mediated clearance of antibody-coated cells.

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Reilly, Thomas M., Robert M. Knabb, Andrew T. Chiu, David L. Bradfute, and Pieter B. M. W. M. Timmermans. "Monoclonal Antibodies to Tissue-Type Plasminogen Activator which Prolong its Clearance In Vivo." Thrombosis and Haemostasis 61, no. 02 (1989): 259–61. http://dx.doi.org/10.1055/s-0038-1646571.

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SummaryThree murine monoclonal antibodies to tissue-type plasminogen activator (t-PA) were evaluated for their effects on the binding of iodinated t-PA to cultured human hepatoma cells (Hep G2), and on extending the half-life of t-PA injected into rabbits. Two of the antibodies, AE5 and EG2, significantly inhibited t-PA binding in vitro, and extended the in vivo half-life of t-PA four to five-fold. A third antibody, BA10, which had a much smaller inhibitory effect on t-PA binding, had no influence in extending t-PA’s half-life. MOPC-21, a control antibody not directed to t-PA, had no effect on either test. Our results are the first to correlate different compounds’ effects on t-PA binding with their ability to retard t-PA clearance in vivo, and provide additional evidence for the importance of a liver cell receptor in the t-PA clearance process.

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Senior, Bernard W., James I. Dunlop, Margaret R. Batten, Mogens Kilian, and Jenny M. Woof. "Cleavage of a Recombinant Human Immunoglobulin A2 (IgA2)-IgA1 Hybrid Antibody by Certain Bacterial IgA1 Proteases." Infection and Immunity 68, no. 2 (2000): 463–69. http://dx.doi.org/10.1128/iai.68.2.463-469.2000.

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ABSTRACT To understand more about the factors influencing the cleavage of immunoglobulin A1 (IgA1) by microbial IgA1 proteases, a recombinant human IgA2/IgA1 hybrid molecule was generated. In the hybrid, termed IgA2/A1 half hinge, a seven-amino-acid sequence corresponding to one half of the duplicated sequence making up the IgA1 hinge was incorporated into the equivalent site in IgA2. Insertion of the IgA1 half hinge into IgA2 did not affect antigen binding capacity or the functional activity of the hybrid molecule, as judged by its ability to bind to IgA Fcα receptors and trigger respiratory bursts in neutrophils. Although the IgA2/A1 hybrid contained only half of the IgA1 hinge, it was found to be cleaved by a variety of different bacterial IgA1 proteases, including representatives of those that cleave IgA1 in the different duplicated halves of the hinge, namely, those of Prevotella melaninogenica, Streptococcus pneumoniae, S. sanguis, Neisseria meningitidis types 1 and 2, N. gonorrhoeae types 1 and 2, and Haemophilus influenzae type 2. Thus, for these enzymes the recognition site for IgA1 cleavage is contained within half of the IgA1 hinge region; additional distal elements, if required, are provided by either an IgA1 or an IgA2 framework. In contrast, the IgA2/A1 hybrid appeared to be resistant to cleavage with S. oralis and some H. influenzae type 1 IgA1 proteases, suggesting these enzymes require additional determinants for efficient substrate recognition.

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Robbie, Gabriel J., Ryan Criste, William F. Dall'Acqua, et al. "A Novel Investigational Fc-Modified Humanized Monoclonal Antibody, Motavizumab-YTE, Has an Extended Half-Life in Healthy Adults." Antimicrobial Agents and Chemotherapy 57, no. 12 (2013): 6147–53. http://dx.doi.org/10.1128/aac.01285-13.

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ABSTRACTThe study objective was to evaluate the pharmacokinetics (PK), antidrug antibody (ADA), and safety of motavizumab-YTE (motavizumab with amino acid substitutions M252Y/S254T/T256E [YTE]), an Fc-modified anti-respiratory syncytial virus (RSV) monoclonal antibody. Healthy adults (n= 31) were randomized to receive a single intravenous (i.v.) dose of motavizumab-YTE or motavizumab (0.3, 3, 15, or 30 mg/kg) and followed for 240 days. Clearance of motavizumab-YTE was significantly lower (71% to 86%) and the half-life (t1/2) was 2- to 4-fold longer than with motavizumab. However, similar peak concentrations and volume-of-distribution values, indicative of similar distribution properties, were seen at all dose levels. The sustained serum concentrations of motavizumab-YTE were fully functional, as shown by RSV neutralizing activity that persisted for 240 days with motavizumab-YTE versus 90 days postdose for motavizumab. Safety and incidence of ADA were comparable between groups. In this first study of an Fc-modified monoclonal antibody in humans, motavizumab-YTE was well tolerated and exhibited an extended half-life of up to 100 days. (This study has been registered at ClinicalTrials.gov under registration no. NCT00578682.)

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Yim, Changyong, Hyeonjeong Lee, Sanghee Lee, and Sangmin Jeon. "One-step immobilization of antibodies on ZIF-8/Fe3O4 hybrid nanoparticles for the immunoassay of Staphylococcus aureus." RSC Advances 7, no. 3 (2017): 1418–22. http://dx.doi.org/10.1039/c6ra25527b.

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ZIF-8/Fe<sub>3</sub>O<sub>4</sub> hybrid nanoparticles were functionalized with half-fragmented antibodies via Zn–S bonding, which enabled one-step antibody immobilization with favorable orientations.

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Liu, Tao, Yong Zhang, Yan Liu, et al. "Functional human antibody CDR fusions as long-acting therapeutic endocrine agonists." Proceedings of the National Academy of Sciences 112, no. 5 (2015): 1356–61. http://dx.doi.org/10.1073/pnas.1423668112.

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On the basis of the 3D structure of a bovine antibody with a well-folded, ultralong complementarity-determining region (CDR), we have developed a versatile approach for generating human or humanized antibody agonists with excellent pharmacological properties. Using human growth hormone (hGH) and human leptin (hLeptin) as model proteins, we have demonstrated that functional human antibody CDR fusions can be efficiently engineered by grafting the native hormones into different CDRs of the humanized antibody Herceptin. The resulting Herceptin CDR fusion proteins were expressed in good yields in mammalian cells and retain comparable in vitro biological activity to the native hormones. Pharmacological studies in rodents indicated a 20- to 100-fold increase in plasma circulating half-life for these antibody agonists and significantly extended in vivo activities in the GH-deficient rat model and leptin-deficient obese mouse model for the hGH and hLeptin antibody fusions, respectively. These results illustrate the utility of antibody CDR fusions as a general and versatile strategy for generating long-acting protein therapeutics.

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Liu, Zhihong, Vincent S. Stoll, Peter J. DeVries, et al. "A potent erythropoietin-mimicking human antibody interacts through a novel binding site." Blood 110, no. 7 (2007): 2408–13. http://dx.doi.org/10.1182/blood-2007-04-083998.

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Recombinant human erythropoietin (rHu-EPO) is used to treat anemia by activating the erythropoietin receptor (EPOR) in erythroid progenitor cells, leading to proliferation and differentiation into mature red blood cells. To allow less frequent dosing, a hyperglycosylated version of EPO has been developed with a longer half-life. In principle, an agonistic antibody targeting EPOR would offer an even longer half-life, support robust monthly dosing, and, unlike EPO products, reduce the risk of pure red cell aplasia. The efficiency of signaling and corresponding potency of previously reported antibody mimics are generally suboptimal compared with EPO and not suitable for clinical use. Here we describe a potent, fully human, agonistic antibody (ABT007) targeting EPOR that supports potent, more sustained, and less pulsatile elevation of hematocrit in a human EPOR–expressing transgenic mouse model compared with standard doses of rHu-EPO while requiring less frequent dosing. Resolution of the crystal structure of the EPOR extracellular domain (ECD) complexed to the ABT007 Fab fragment, determined at 0.32 nm, identifies a binding site that is consistent with a novel mechanism of receptor activation based on a unique antibody-imposed conformational change. These results demonstrate that a symmetric molecule can serve as a potent activator of the EPOR.

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Walsh, Scott, Anjali Shah, and James Mond. "Improved Pharmacokinetics and Reduced Antibody Reactivity of Lysostaphin Conjugated to Polyethylene Glycol." Antimicrobial Agents and Chemotherapy 47, no. 2 (2003): 554–58. http://dx.doi.org/10.1128/aac.47.2.554-558.2003.

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ABSTRACT Lysostaphin is a 27-kDa endopeptidase that enzymatically disrupts the cell wall of Staphylococcus aureus and is a promising candidate for treating S. aureus blood-borne infections. It would be extremely useful to define conditions that would both increase lysostaphin's in vivo half-life to allow for more effective tissue distribution and reduce its immunogenicity. Conjugation of polyethylene glycol (PEG) to lysostaphin (PEGylation) was investigated as a means to accomplish these goals. Rather than using linear forms of PEG, branched PEGs were chosen as the initial candidates because their large spatial volumes prevent entry of the polymer into the enzyme's active sites, which could potentially reduce enzymatic function. Enzymatic activity for most PEGylated lysostaphins was reduced, but these compounds were still considerably active compared to unconjugated lysostaphin, with conjugates that had lower degrees of PEG modification having greater activity than those with higher degrees. PEGylated lysostaphin injected intravenously had a serum drug half-life of up to 24 h and resulted in much higher plasma drug concentrations than an equal dose of unconjugated lysostaphin, which had a half-life of less than 1 h. Finally, reduced binding affinity was shown for PEGylated lysostaphin in an antilysostaphin capture enzyme-linked immunosorbent assay, with some PEG-lysostaphin conjugates having binding affinities that were reduced more than 10-fold compared to unconjugated lysostaphin. These findings demonstrate that PEGylation of lysostaphin, while diminishing its S. aureus killing activity, results in prolonged serum drug persistence and reduced antibody binding. These features should significantly enhance lysostaphin's therapeutic value as an intravenous “antibiotic” against S. aureus.

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Schneider, Eric L., Brian R. Hearn, Samuel J. Pfaff, et al. "Approach for Half-Life Extension of Small Antibody Fragments That Does Not Affect Tissue Uptake." Bioconjugate Chemistry 27, no. 10 (2016): 2534–39. http://dx.doi.org/10.1021/acs.bioconjchem.6b00469.

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Ying, Tianlei, Yanping Wang, Yang Feng, et al. "Engineered antibody domains with significantly increased transcytosis and half-life in macaques mediated by FcRn." mAbs 7, no. 5 (2015): 922–30. http://dx.doi.org/10.1080/19420862.2015.1067353.

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Watson, D. L. "Biological half-life of ovine antibody in neonatal lambs and adult sheep following passive immunization." Veterinary Immunology and Immunopathology 30, no. 2-3 (1992): 221–32. http://dx.doi.org/10.1016/0165-2427(92)90140-l.

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Juge-Aubry, CE, Hong Liang, Jochen Lang, John W. Barlow, and Albert G. Burger. "Synthesis and characterization of anti-idiotypic anti-T4 antibodies." European Journal of Endocrinology 130, no. 1 (1994): 107–12. http://dx.doi.org/10.1530/eje.0.1300107.

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Juge-Aubry CE, Liang H, Lang J, Barlow JW, Burger AG. Synthesis and characterization of anti-idiotypic anti-thyroxine antibodies. Eur J Endocrinol 1994;130:107–12. ISSN 0804–4643 We injected rabbits with purified monoclonal murine immunoglobulin (IgG1) or polyclonal anti-thyroxine antibodies (anti-T4) and polyclonal anti-triiodothyroacetic acid (anti-Triac) antibodies to stimulate the production of anti-idiotypic antibodies. Purified immunoglobulins from all five rabbits immunized with monoclonal primary antibodies were able to inhibit the interaction between [125I]T4 and the primary antibody. The preimmune sera were inactive. This effect was not due to endogenous T4 contamination or contamination with the injected primary antibody. Half-maximal inhibition of binding of primary antibody with anti-idiotype was between 1.6 and 30 μg of total immunoglobulins. Addition of normal mouse IgG1 did not alter the inhibitory effect of the anti-idiotypic antibody. suggesting that this effect is specific. These anti-idiotypic antibodies reacted differently with different polyclonal antibodies, reflecting the heterogeneous nature of polyclonal antibody populations. Polyclonal antibodies were less effective in stimulating anti-idiotypic antibody production. One polyclonal anti-T4 and one anti-Triac antibody produced weak anti-idiotypic antibody that had to be used at a concentration of > 600 μg of total immunoglobulins to be inhibitory. Both inhibited the binding of T4 to the monoclonal anti-T4 antibody. However, they were ineffective in inhibiting the function of their own antigen, the polyclonal anti-T4 or anti-Triac antibody. We tested the most potent anti-idiotypic antibodies for their ability to compete with T4 for other T4-binding proteins. Specific inhibition of T4 binding to thyroid-binding globulin was observed with half-maximal effect at approximately 450 μg of total IgG. The antibody was negative when tested against Transthyretin, rat liver deiodinase type I, triiodothyronine cell uptake and liver cytoplasmic triiodothyronine binding. In conclusion, the technique described herein allows production of anti-idiotypic anti-T4, which can be useful in the characterization of the range of iodothyronine-binding sites involved in thyroid hormone action. AG Burger, Unité de la Thyroïde, Hôpital Cantonal Universitaire, 1211 Genève 4, Switzerland

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