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Статті в журналах з теми "Antibody affinity"

Щоб переглянути інші типи публікацій з цієї теми, перейдіть за посиланням: Antibody affinity.

Автор: Grafiati

Опубліковано: 4 червня 2021

Оновлено: 14 лютого 2022

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1

Azimzadeh, A., and M. H. V. Van Regenmortel. "Antibody affinity measurements." Journal of Molecular Recognition 3, no. 3 (June 1990): 108–16. http://dx.doi.org/10.1002/jmr.300030304.

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2

van Regenmortel, Marc H. V., and Agnëgs Azimzadeh. "Determination of Antibody Affinity." Journal of Immunoassay 21, no. 2-3 (May 2000): 211–34. http://dx.doi.org/10.1080/01971520009349534.

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3

Wabl, Matthias, Marilia Cascalho, and Charles Steinberg. "Hypermutation in antibody affinity maturation." Current Opinion in Immunology 11, no. 2 (April 1999): 186–89. http://dx.doi.org/10.1016/s0952-7915(99)80031-4.

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4

Webster, D. M., S. Roberts, J. C. Cheetham, R. Griest, and A. R. Rees. "Engineering antibody affinity and specificity." International Journal of Cancer 41, S3 (1988): 13–16. http://dx.doi.org/10.1002/ijc.2910410804.

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5

Nervig, Christine S., and Shawn C. Owen. "Affinity-bound antibody–drug conjugates." Nature Biomedical Engineering 3, no. 11 (November 2019): 850–51. http://dx.doi.org/10.1038/s41551-019-0478-0.

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6

Griswold, William R. "A Quantitative Relationship Between Antibody Affinity and Antibody Avidity." Immunological Investigations 16, no. 2 (January 1987): 97–106. http://dx.doi.org/10.3109/08820138709030567.

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7

Yu, Guimei, Kunpeng Li, and Wen Jiang. "Antibody-based affinity cryo-EM grid." Methods 100 (May 2016): 16–24. http://dx.doi.org/10.1016/j.ymeth.2016.01.010.

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8

Steward, Michael W., Carolynne Stanley, and Maria D. Furlong. "Antibody affinity maturation in selectively bred high and low-affinity mice." European Journal of Immunology 16, no. 1 (1986): 59–63. http://dx.doi.org/10.1002/eji.1830160112.

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9

Makabe, Koki. "Molecular basis of flexible peptide recognition by an antibody." Journal of Biochemistry 167, no. 4 (February 6, 2020): 343–45. http://dx.doi.org/10.1093/jb/mvaa017.

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Анотація:

Abstract Antibodies can recognize various types of antigens with high specificity and affinity and peptide is one of their major targets. Understanding an antibody’s molecular recognition mechanism for peptide is important for developing clones with a higher specificity and affinity. Here, the author reviews recent progresses in flexible peptide recognition by an antibody using several biophysical techniques, including X-ray crystallography, molecular dynamics simulations and calorimetric measurements. A set of two reports highlight the importance of intramolecular hydrogen bonds that form in an unbound flexible state. Such intramolecular hydrogen bonds restrict the fluctuation of the peptide and reduce the conformational entropy, resulting in the destabilization of the unbound state and increasing the binding affinity by increasing the free energy change. These detailed analyses will aid in the antibody design in the future.

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10

Fukunishi, Hiroaki, Jiro Shimada, and Kenji Shiraishi. "Antigen–Antibody Interactions and Structural Flexibility of a Femtomolar-Affinity Antibody." Biochemistry 51, no. 12 (March 13, 2012): 2597–605. http://dx.doi.org/10.1021/bi3000319.

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11

Sawutz, David G., Richard Koury, and Charles J. Homcy. "Enhanced antigen-antibody binding affinity mediated by an anti-idiotypic antibody." Biochemistry 26, no. 17 (August 25, 1987): 5275–82. http://dx.doi.org/10.1021/bi00391a010.

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12

Griswold, William R., and Dennis P. Nelson. "Calculation of monoclonal antibody affinity constants directly from antibody dilution curves." Immunology Letters 9, no. 1 (January 1985): 15–18. http://dx.doi.org/10.1016/0165-2478(85)90087-2.

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13

Ohno, K., Y. Inoue, and M. Sakurai. "Quantum Chemical Study of Antibody Affinity Maturation." Seibutsu Butsuri 43, supplement (2003): S50. http://dx.doi.org/10.2142/biophys.43.s50_4.

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14

Salmi, Aimo A. "Antibody affinity and protection in virus infections." Current Opinion in Immunology 3, no. 4 (August 1991): 503–6. http://dx.doi.org/10.1016/0952-7915(91)90011-o.

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15

Daugherty, P. S., G. Chen, M. J. Olsen, B. L. Iverson, and G. Georgiou. "Antibody affinity maturation using bacterial surface display." Protein Engineering Design and Selection 11, no. 9 (September 1, 1998): 825–32. http://dx.doi.org/10.1093/protein/11.9.825.

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16

Bobrovnik, S. A. "Determination of antibody affinity by ELISA. Theory." Journal of Biochemical and Biophysical Methods 57, no. 3 (September 2003): 213–36. http://dx.doi.org/10.1016/s0165-022x(03)00145-3.

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17

Tas, J. M. J., L. Mesin, G. Pasqual, S. Targ, J. T. Jacobsen, Y. M. Mano, C. S. Chen, et al. "Visualizing antibody affinity maturation in germinal centers." Science 351, no. 6277 (February 18, 2016): 1048–54. http://dx.doi.org/10.1126/science.aad3439.

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18

Vanderlaan, Martin, Bruce Watkins, Cynthia Thomas, Frank Dolbeare, and Larry Stanker. "Improved high-affinity monoclonal antibody to lododeoxyuridine." Cytometry 7, no. 6 (November 1986): 499–507. http://dx.doi.org/10.1002/cyto.990070602.

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19

Bereli, Nilay, Sinan Akgöl, Handan Yavuz, and Adil Denizli. "Antibody purification by concanavalin A affinity chromatography." Journal of Applied Polymer Science 97, no. 3 (2005): 1202–8. http://dx.doi.org/10.1002/app.21862.

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20

Lee, Bao-Shiang, Shalini Gupta, Sangeeth Krisnanchettier, and Syed S. Lateef. "Catching protein antigens by antibody affinity electrophoresis." ELECTROPHORESIS 25, no. 20 (October 2004): 3331–35. http://dx.doi.org/10.1002/elps.200406058.

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21

Dunn-Walters, D. K., M. Banerjee, and R. Mehr. "Effects of age on antibody affinity maturation." Biochemical Society Transactions 31, no. 2 (April 1, 2003): 447–48. http://dx.doi.org/10.1042/bst0310447.

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Анотація:

The elderly are more susceptible to infectious diseases. Mortality and morbidity from infections increase sharply over the age of 65 years. At the same time, the efficacy of vaccinations in the elderly is decreased. The elderly also have an increased incidence of cancer and inflammatory diseases. All the above indicate an age-related dysregulation of the immune system. Evidence suggests that the change in the humoral immune response with age is a qualitative rather than a quantitative one, i.e. it is the affinity and specificity of the antibody that changes, rather than the quantity of antibody produced. There are a number of possible causes of this failure, one of which is a defect in the mechanism of hypermutation of immunoglobulin genes. We have studied individual clonal responses within germinal centres of spleen and Peyer's patches in young and old patient groups. Our results indicate that there is no difference in the actual mechanism of hypermutation with age. There are, however, differences that are due either to a change in selection processes or to a change in the founder cells available for activation.

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22

Gao, Jun, Zhijun Li, Thomas Russell, and Zhiyu Li. "Antibody affinity purification using metallic nickel particles." Journal of Chromatography B 895-896 (May 2012): 89–93. http://dx.doi.org/10.1016/j.jchromb.2012.03.019.

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23

Geisow, Michael J. "Antibody engineering — successful affinity maturation in vitro." Trends in Biotechnology 10 (1992): 299–301. http://dx.doi.org/10.1016/0167-7799(92)90252-q.

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24

Hall, Tony J., and Corinne Heckel. "Thiocyanate elution estimation of relative antibody affinity." Journal of Immunological Methods 115, no. 1 (November 1988): 153–54. http://dx.doi.org/10.1016/0022-1759(88)90324-9.

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25

Fibriansah, Guntur, Elisa X. Y. Lim, Jan K. Marzinek, Thiam-Seng Ng, Joanne L. Tan, Roland G. Huber, Xin-Ni Lim, et al. "Antibody affinity versus dengue morphology influences neutralization." PLOS Pathogens 17, no. 2 (February 23, 2021): e1009331. http://dx.doi.org/10.1371/journal.ppat.1009331.

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Анотація:

Different strains within a dengue serotype (DENV1-4) can have smooth, or “bumpy” surface morphologies with different antigenic characteristics at average body temperature (37°C). We determined the neutralizing properties of a serotype cross-reactive human monoclonal antibody (HMAb) 1C19 for strains with differing morphologies within the DENV1 and DENV2 serotypes. We mapped the 1C19 epitope to E protein domain II by hydrogen deuterium exchange mass spectrometry, cryoEM and molecular dynamics simulations, revealing that this epitope is likely partially hidden on the virus surface. We showed the antibody has high affinity for binding to recombinant DENV1 E proteins compared to those of DENV2, consistent with its strong neutralizing activities for all DENV1 strains tested regardless of their morphologies. This finding suggests that the antibody could out-compete E-to-E interaction for binding to its epitope. In contrast, for DENV2, HMAb 1C19 can only neutralize when the epitope becomes exposed on the bumpy-surfaced particle. Although HMAb 1C19 is not a suitable therapeutic candidate, this study with HMAb 1C19 shows the importance of choosing a high-affinity antibody that could neutralize diverse dengue virus morphologies for therapeutic purposes.

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26

Ebrahimi, Zahra, Saeme Asgari, Reza Ahangari Cohan, Reza Hosseinzadeh, Ghader Hosseinzadeh, and Roghaye Arezumand. "Rational affinity enhancement of fragmented antibody by ligand-based affinity improvement approach." Biochemical and Biophysical Research Communications 506, no. 3 (November 2018): 653–59. http://dx.doi.org/10.1016/j.bbrc.2018.10.127.

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27

Rath, S., C. M. Stanley, and M. W. Steward. "An inhibition enzyme immunoassay for estimating relative antibody affinity and affinity heterogeneity." Journal of Immunological Methods 106, no. 2 (February 1988): 245–49. http://dx.doi.org/10.1016/0022-1759(88)90204-9.

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28

Luo Yamei, 骆亚梅, 蹇林 Jian Lin, 罗浩奇 Luo Haoqi, 黄科赢 Huang Keying, 张沃伦 Zhang Wolun, 王柱楼 Wang Zhulou, 张会芝 Zhang Huizhi, 肖茜 Xiao Qian та 黄韶辉 Huang Shaohui. "荧光自相关光谱技术检测抗原抗体亲和力". Acta Optica Sinica 41, № 17 (2021): 1730004. http://dx.doi.org/10.3788/aos202141.1730004.

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29

Kostolanský, F., E. Varečková, T. Betáková, V. Mucha, G. Russ, and S. A. Wharton. "The strong positive correlation between effective affinity and infectivity neutralization of highly cross-reactive monoclonal antibody IIB4, which recognizes antigenic site B on influenza A virus haemagglutinin." Microbiology 81, no. 7 (July 1, 2000): 1727–35. http://dx.doi.org/10.1099/0022-1317-81-7-1727.

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Анотація:

Monoclonal antibody (MAb) IIB4 displays a rare combination of virus neutralization (VN) activity and broad cross-reactivity with influenza A virus strains of the H3 subtype isolated in a period from 1973 to 1988. The epitope of this antibody has been identified as around HA1 residues 198, 199 and 201. Here we report that residues 155, 159, 188, 189 and 193 also influence the binding of this antibody. We have used this antibody to study the relationship between antibody affinity and VN activity. Using one MAb and a single epitope on the haemagglutinin (HA) of different influenza viruses we found a strong positive correlation between effective affinity and VN activity of MAb IIB4. A 10-fold increase in effective affinity corresponded to the 2000-fold increase in VN titre. It follows from the law of mass action that for an effective affinity K=9×108 l/mol, 50% VN was achieved at approx. 10% occupation of HA spikes with antibody. In contrast, for an effective affinity K=6×107 l/mol, to achieve 50% VN, occupation of up to 98% of HA spikes was required. An effective affinity about K=6×107 l/mol thus represents the limiting value for VN because a further decrease in the affinity cannot be compensated by a higher concentration of antibody.

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30

Steward, Michael W., and Andrew M. Lew. "The importance of antibody affinity in the performance of immunoassays for antibody." Journal of Immunological Methods 78, no. 2 (April 1985): 173–90. http://dx.doi.org/10.1016/0022-1759(85)90074-2.

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31

CAMPO, P. "HDI-specific IgE antibody results are influenced by relative antibody affinity*1." Journal of Allergy and Clinical Immunology 113, no. 2 (February 2004): S60. http://dx.doi.org/10.1016/j.jaci.2003.12.185.

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32

VanAntwerp, Jennifer J., and K. Dane Wittrup. "Thermodynamic characterization of affinity maturation: the D1.3 antibody and a higher-affinity mutant." Journal of Molecular Recognition 11, no. 1-6 (December 1998): 10–13. http://dx.doi.org/10.1002/(sici)1099-1352(199812)11:1/6<10::aid-jmr381>3.0.co;2-h.

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33

Paik, Chang H., William C. Eckelman, and Richard C. Reba. "Transchelation of 99mTc from low affinity sites to high affinity sites of antibody." International Journal of Radiation Applications and Instrumentation. Part B. Nuclear Medicine and Biology 13, no. 4 (January 1986): 359–62. http://dx.doi.org/10.1016/0883-2897(86)90010-3.

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34

Skamaki, Kalliopi, Stephane Emond, Matthieu Chodorge, John Andrews, D. Gareth Rees, Daniel Cannon, Bojana Popovic, Andrew Buchanan, Ralph R. Minter, and Florian Hollfelder. "In vitro evolution of antibody affinity via insertional scanning mutagenesis of an entire antibody variable region." Proceedings of the National Academy of Sciences 117, no. 44 (October 16, 2020): 27307–18. http://dx.doi.org/10.1073/pnas.2002954117.

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Анотація:

We report a systematic combinatorial exploration of affinity enhancement of antibodies by insertions and deletions (InDels). Transposon-based introduction of InDels via the method TRIAD (transposition-based random insertion and deletion mutagenesis) was used to generate large libraries with random in-frame InDels across the entire single-chain variable fragment gene that were further recombined and screened by ribosome display. Knowledge of potential insertion points from TRIAD libraries formed the basis of exploration of length and sequence diversity of novel insertions by insertional-scanning mutagenesis (InScaM). An overall 256-fold affinity improvement of an anti–IL-13 antibody BAK1 as a result of InDel mutagenesis and combination with known point mutations validates this approach, and suggests that the results of this InDel mutagenesis and conventional exploration of point mutations can synergize to generate antibodies with higher affinity.

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35

Magor, Brad. "Antibody Affinity Maturation in Fishes—Our Current Understanding." Biology 4, no. 3 (July 31, 2015): 512–24. http://dx.doi.org/10.3390/biology4030512.

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36

Rathore, Abhishek S., Animesh Sarker, and Rinkoo D. Gupta. "Recent Developments Toward Antibody Engineering and Affinity Maturation." Protein & Peptide Letters 25, no. 10 (November 30, 2018): 886–96. http://dx.doi.org/10.2174/0929866525666180925142757.

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37

Temirov, Jamshid P., Andrew R. M. Bradbury, and James H. Werner. "Measuring an Antibody Affinity Distribution Molecule by Molecule." Analytical Chemistry 80, no. 22 (November 15, 2008): 8642–48. http://dx.doi.org/10.1021/ac8015592.

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38

Kamali, Ali N., Patricia Marín-García, Isabel G. Azcárate, Antonio Puyet, Amalia Diez, and José M. Bautista. "Experimental Immunization Based onPlasmodiumAntigens Isolated by Antibody Affinity." Journal of Immunology Research 2015 (2015): 1–11. http://dx.doi.org/10.1155/2015/723946.

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Анотація:

Vaccines blocking malaria parasites in the blood-stage diminish mortality and morbidity caused by the disease. Here, we isolated antigens from total parasite proteins by antibody affinity chromatography to test an immunization against lethal malaria infection in a murine model. We used the sera of malaria self-resistant ICR mice to lethalPlasmodium yoelii yoelii17XL for purification of their IgGs which were subsequently employed to isolate blood-stage parasite antigens that were inoculated to immunize BALB/c mice. The presence of specific antibodies in vaccinated mice serum was studied by immunoblot analysis at different days after vaccination and showed an intensive immune response to a wide range of antigens with molecular weight ranging between 22 and 250 kDa. The humoral response allowed delay of the infection after the inoculation to high lethal doses ofP. yoelii yoelii17XL resulting in a partial protection against malaria disease, although final survival was managed in a low proportion of challenged mice. This approach shows the potential to prevent malaria disease with a set of antigens isolated from blood-stage parasites.

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39

Shaw, Christine A., Gillis Otten, Andreas Wack, Gene A. Palmer, Christian W. Mandl, M. Lamine Mbow, Nicholas Valiante, and Philip R. Dormitzer. "Antibody affinity maturation and respiratory syncytial virus disease." Nature Medicine 15, no. 7 (July 2009): 725. http://dx.doi.org/10.1038/nm0709-725a.

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40

Ayyar, B. Vijayalakshmi, Sushrut Arora, Caroline Murphy, and Richard O’Kennedy. "Affinity chromatography as a tool for antibody purification." Methods 56, no. 2 (February 2012): 116–29. http://dx.doi.org/10.1016/j.ymeth.2011.10.007.

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41

Arora, Sushrut, Vikas Saxena, and B. Vijayalakshmi Ayyar. "Affinity chromatography: A versatile technique for antibody purification." Methods 116 (March 2017): 84–94. http://dx.doi.org/10.1016/j.ymeth.2016.12.010.

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42

Allen, Deborah, Ana Cumano, Thomas Simon, Fred Sablitzky, and Klaus Rajewsky. "Modulation of antibody binding affinity by somatic mutation." International Journal of Cancer 41, S3 (1988): 1–8. http://dx.doi.org/10.1002/ijc.2910410802.

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43

Vega, Rafael A., Daniel Maspoch, Clifton K. F. Shen, Joseph J. Kakkassery, Benjamin J. Chen, Robert A. Lamb, and Chad A. Mirkin. "Functional Antibody Arrays through Metal Ion-Affinity Templates." ChemBioChem 7, no. 11 (August 8, 2006): 1653–57. http://dx.doi.org/10.1002/cbic.200600271.

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44

Akkaya, Munir, Billur Akkaya, Ann S. Kim, Pietro Miozzo, Haewon Sohn, Mirna Pena, Alexander S. Roesler, et al. "Toll-like receptor 9 antagonizes antibody affinity maturation." Nature Immunology 19, no. 3 (February 23, 2018): 255–66. http://dx.doi.org/10.1038/s41590-018-0052-z.

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45

Rudnick, Stephen I., and Gregory P. Adams. "Affinity and Avidity in Antibody-Based Tumor Targeting." Cancer Biotherapy and Radiopharmaceuticals 24, no. 2 (April 2009): 155–61. http://dx.doi.org/10.1089/cbr.2009.0627.

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46

Wark, Kim L., and Peter J. Hudson. "Latest technologies for the enhancement of antibody affinity." Advanced Drug Delivery Reviews 58, no. 5-6 (August 2006): 657–70. http://dx.doi.org/10.1016/j.addr.2006.01.025.

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47

OHLIN, M., and C. BORREBAECK. "Low affinity, antibody binding of an -derived component." FEMS Immunology and Medical Microbiology 13, no. 2 (February 1996): 161–68. http://dx.doi.org/10.1016/0928-8244(95)00122-0.

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48

Doria-Rose, Nicole A., and M. Gordon Joyce. "Strategies to guide the antibody affinity maturation process." Current Opinion in Virology 11 (April 2015): 137–47. http://dx.doi.org/10.1016/j.coviro.2015.04.002.

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49

Nelson, Dennis P., and William R. Griswold. "A computer program for calculating antibody affinity constants." Computer Methods and Programs in Biomedicine 27, no. 1 (July 1988): 65–68. http://dx.doi.org/10.1016/0169-2607(88)90104-6.

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50

Joshi, Rajani R. "Statistical mechanics of antibody-antigen binding: affinity analysis." Physica A: Statistical Mechanics and its Applications 218, no. 1-2 (August 1995): 214–28. http://dx.doi.org/10.1016/0378-4371(95)00088-o.

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