The Use of Phage Antibodies for Microbial Cells Detection (Review)

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Abstract

Phage antibody display technology has revolutionized the field of bacterial immunodetection. This technology allows the expression of an antibody fused to the coat protein of a filamentous bacteriophage. The use of phage display makes it possible to obtain high-affinity antibodies by passing the stage of animal immunization, reducing the time for obtaining stable antibody-producing clones from several months to several weeks, significantly reducing the cost of the process. These advantages make phage antibodies an important tool for bacterial detection. The paper presents a brief description of the technological methods for obtaining phage antibodies to microbial cells. The possibilities and prospects for using phage antibodies as a selective agent in analytical systems, including biosensors, are discussed.

About the authors

O. I. Guliy

Institute of Biochemistry and Physiology of Plants and Microorganisms – Subdivision of the Federal State Budgetary Research Institution Saratov Federal Scientific Centre of the Russian Academy of Sciences (IBPPM RAS)

Author for correspondence.
Email: guliy_olga@mail.ru
Russia, 410049, Saratov

S. S. Evstigneeva

Institute of Biochemistry and Physiology of Plants and Microorganisms – Subdivision of the Federal State Budgetary Research Institution Saratov Federal Scientific Centre of the Russian Academy of Sciences (IBPPM RAS)

Email: guliy_olga@mail.ru
Russia, 410049, Saratov

L. A. Dykman

Institute of Biochemistry and Physiology of Plants and Microorganisms – Subdivision of the Federal State Budgetary Research Institution Saratov Federal Scientific Centre of the Russian Academy of Sciences (IBPPM RAS)

Email: guliy_olga@mail.ru
Russia, 410049, Saratov

References

  1. Gascoyne P., Pethig R., Satayavivad J., Becker F.F., Ruchirawat M. // Biochim. Biophys. Acta. 1997. V. 1323. P. 240–252.
  2. Uithoven K.A., Schmidt J.C., Ballman M.E. // Biosens. Bioelectron. 2000. V. 14. № 10–11. P. 761–770.
  3. Vaughan P.S., Leszyk J.D., Vaughan K.T. // J. Biol. Chem. 2001. V. 276. № 28. P. 26171–26179.
  4. Lesniewski A., Los M., Jonsson–Niedziółka M., Krajewska A., Szot K., Los J.M., Niedziolka–Jonsson J. // Bioconjug. Chem. 2014. V. 25. № 4. P. 644–648.
  5. Spadiut O., Capone S., Krainer F., Glieder A., Herwig C. // Trends Biotechnol. 2014. V. 32. № 1. P. 54–60.
  6. Ратнер Г.М. Поликлональные антитела как реагенты для иммуноанализа: получение, характеристика, применение. Aвтореф. дис. д-ра мед. наук. Томск, 1996. 47 с.
  7. Альтшулер E.П., Серебряная Д.В., Катруха А.Г. // Успехи биологической химии. 2010. Т. 50. С. 203–258.
  8. Flajnik M.F., Singh N.J., Holland S.M. Paul’s Fundamental Immunology / 8 Ed. Amsterdam: Wolters Kluwer Health, 2022. 1312 p.
  9. Глик Б., Пастернак Дж. Молекулярная биотехнология. Принципы и применение. Перевод с англ. М.: Мир, 2002. 589 с.
  10. Петрова Е.Э., Комалева Р.Л., Лахтина О.Е., Самохвалова Л.В., Калинина Н.А., Шошина Н.С. et al. // Биоорганическая химия. 2009. Т. 35. № 3. С. 357–368.
  11. Казачинская Е.И., Иванова А.В., Сорокин А.В., Качко А.В., Субботина Е.Л., Разумов И.А., Локтев В.Б. // Медицинская иммунология. 2010. Т. 12. № 3. С. 177–190.
  12. Bradbury A.R., Marks J.D. // J. Immunol. Methods. 2004. V. 290. № 1–2. P. 29–49.
  13. Bradbury A.R.M., Sidhu S., Dübel S., McCafferty J. // Nat. Biotechnol. 2011. V. 29. № 3. P. 245–254.
  14. Деев С.М., Лебеденко Е.Н., Петровская Л.Е., Долгих Д.А., Габибов А.Г., Кирпичников М.П. // Успехи химии. 2015. Т. 84. № 1. С. 1–26.
  15. Miller L.E., Stevens C.D. Clinical Immunology and Serology: A Laboratory Perspective. 5 Ed. Philadelphia: F.A. Davis, 2020. 624 p.
  16. Abbas A.K., Lichtman A.H., Pillai S. Cellular and Molecular Immunology. 10 Ed. Amsterdam: Elsevier, 2021. 600 p.
  17. Hendrickson O.D., Zherdev A.V., Kaplun A.P., Dzantiev B.B. //Mol. Immunol. 2002. V. 39. № 7–8. P. 413–422.
  18. Schroeder H.W. Jr, Cavacini L. // J. Allergy Clin. Immunol. 2010. V. 125. № 2. Suppl 2. P. S41–52.
  19. Duquesnoy R.J. // Hum. Immunol. 2006. V. 67. № 11. P. 847–862.
  20. Chi S.W., Maeng C.Y., Kim S.J., Oh M.S., Ryu C.J., Kim S.J. et al. // Proc. Natl. Acad. Sci. USA. 2007. V. 104. № 22. P. 9230–9235.
  21. Sundberg E.J. // Methods Mol. Biol. 2009. V. 524. P. 23–36.
  22. McCafferty J., Griffiths A.D., Winter G., Chiswell D.J. // Nature. 1990. V. 348. № 6301. P. 552–554.
  23. Sidhu S.S., Geyer C.R. Phage Display in Biotechnology and Drug Discovery / 2nd Edition. Boca Raton: CRC Press, 2015. 584 p.
  24. Kehoe J.W., Kay B.K. // Chem. Rev. 2005. V. 105. № 11. P. 4056–4072.
  25. Hammers C.M., Stanley J.R. // J. Invest. Dermatol. 2014. V. 134. № 2. P. 1–5.
  26. Hoffman J.A., Giraudo E., Singh M., Zhang L., Inoue M., Porkka K., Hanahan D., Ruoslahti E. // Cancer Cell. 2003. V. 4. № 5. P. 383–391.
  27. Joyce J.A., Laakkonen P., Bernasconi M., Bergers G., Ruoslahti E., Hanahan D. // Cancer Cell. 2003. V. 4. № 5. 393–403.
  28. Zurita A.J., Arap W., Pasqualini R. // J. Control. Release. 2003. V. 91. № 1–2. P. 183–186.
  29. Valadon P., Garnett J.D., Testa J.E., Bauerle M., Oh P., Schnitzer J.E. // Proc. Natl. Acad. Sci. USA. 2006. V. 103. № 2. P. 407–412.
  30. Frank R., Hargreaves R. // Nat. Rev. Drug Discov. 2003. V. 2. № 7. P. 566–580.
  31. Rudin M., Weissleder R. // Nat. Rev. Drug Discov. 2003. V. 2. № 2. P. 123–131.
  32. Ladner R.C., Sato A.K., Gorzelany J., de Souza M. // Drug Discov. Today. 2004. V. 9. № 12. P. 525–529.
  33. Perez J.M., Josephson L., O’Loughlin T., Högemann D., Weissleder R. // Nat. Biotechnol. 2002. V. 20. № 8. P. 816–820.
  34. Akerman M.E., Chan W.C., Laakkonen P., Bhatia S.N., Ruoslahti E. // Proc. Natl. Acad. Sci. USA. 2002. V. 99. № 20. P. 12617–12621.
  35. Mikawa M., Wang H., Guo L., Liu R., Marik J., Takada Y., Lam K., Lau D. // Mol. Cancer Ther. 2004. V. 3. № 10. P. 1329–1334.
  36. Kelly K.A., Allport J.R., Tsourkas A., Shinde–Patil V.R., Josephson L., Weissleder R. // Circ. Res. 2005. V. 96. № 3. P. 327–336.
  37. Zitzmann S., Mier W., Schad A., Kinscherf R., Askoxylakis V., Krämer S. et al. // Clin. Cancer Res. 2005. V. 11. № 1. P. 139–146.
  38. Гулий О.И., Зайцев Б.Д., Бородина И.А., Фомин А.С., Староверов С.А., Дыкман Л.А., Шихабудинов А.М. // Биофизика. 2017. Т. 62. № 3. С. 472–484.
  39. Guliy O.I., Zaitsev B.D., Borodina I.A., Shikhabudinov A.M., Teplykh A.A., Staroverov S.A., Fomin A.S. // Talanta. 2018. V. 178. P. 569–576.
  40. Deantonio C., Cotella D., Macor P., Santoro C., Sblattero D. // Human Monoclonal Antibodies: Methods and Protocols. 2014. P. 277–295.
  41. Lo B.K.C. Antibody Engineering. Methods and Protocols. V. 248. Totowa, N.J.: Humana Press, 2004. 562 p.
  42. McConnell S.J., Dinh T., Le M.H., Spinella D.G. // Biotechniques. 1999. V. 26. P. 208–210.
  43. Сумарока М.В., Дыкман Л.А., Богатырев В.А., Зайцева И.С., Соколов О.И., Щеголев С.Ю., Харрис У. // Аллергология и иммунология. 2000. Т. 1. № 2. С. 134–135.
  44. Krebber A., Bornhauser S., Burmester J., Honegger A., Willuda J., Bosshard H.R., Plückthun A. // J. Immunol. Methods. 1997. V. 201. № 1. P. 35–55.
  45. Hoogenboom H.R., Chames P. // Immunol. Today. 2000. V. 21. № 8. P. 371–378.
  46. Staroverov S.A., Volkov A.A., Fomin A.S., Laskavuy V.N., Mezhennyy P.V., Kozlov S.V. et al. // J. Immunoassay Immunochem. 2015. V. 36. № 1. P. 100–110.
  47. Тикунова Н.В., Морозова В.В. // Acta Naturae. 2009. Т. 1. № 3. С. 22–31.
  48. Ahmad Z.A., Yeap S.K., Ali A.M., Ho W.Y., Alitheen N.B.M., Hamid M. // Clin. Dev. Immunol. 2012. V. 2012. Article 980250.https://doi.org/10.1155/2012/980250
  49. Dormeshkin D.O., Brichko E.A., Gilep A.A., Usanov S.A. // Proceedings of the National Academy of Sciences of Belarus, Chemical Series. 2017. № 2. P. 93–110.
  50. Anderson G.P., Liu J.L., Hale M.L., Bernstein R.D., Moore M., Swain M.D., Goldman E.R. // Anal. Chem. 2008. V. 80. № 24. P. 9604–9611.
  51. Шаталова А.В., Якубова А.С., Палимпсестов В.В., Есмагамбетов И.Б. // Разработка и регистрация лекарственных средств. 2019. Т. 8. № 1. С. 14–22.
  52. Goldman E.R., Liu J.L., Bernstein R.D., Swain M.D., Mitchell S.Q., Anderson G.P. // Sensors. 2009. V. 9. № 1. P. 542–555.
  53. Тиллиб С.В. // Мол. биология. 2011. Т. 45. № 1. С. 77–85.
  54. Charlton K.A., Moyle S., Porter A.J., Harris W.J. // J. Immunol. 2000. V. 164. № 12. P. 6221–6229.
  55. Bashir S., Paeshuyse J. // Antibodies. 2020. V. 9. № 2. Article 21.https://doi.org/10.3390/antib9020021
  56. Щелкунов С.Н. Генетическая инженерия: Учебно-справочное пособие. 2 Изд. Новосибирск: Сиб. унив. изд-во, 2004. 496 с.
  57. Gavilondo J.V., Larrick J.W. // Biotechniques. 2000. V. 29. № 1. P. 128–132.
  58. Roth K.D.R., Wenzel E.V., Ruschig M., Steinke S., Langreder N., Heine P.A. et al. // Front. Cell. Infect. Microbiol. 2021. V. 11. Article 697876.https://doi.org/10.3389/fcimb.2021.697876
  59. de Kruif J., Boel E., Logtenberg T. // J. Mol. Biol. 1995. V. 248. № 1. P. 97–105.
  60. Аникаев А.Ю., Ломоносов А.М. // Лабораторная служба. 2014. Т. 3. № 1. С. 32–36.
  61. Collins F.S., Hamburg M.A. // N. Engl. J. Med. 2013. V. 369. № 25. P. 2369–2371.
  62. Fantini M., Pandolfini L., Lisi S., Chirichella M., Arisi I., Terrigno M., Goracci M., Cremisi F., Cattaneo A. // PLoS One. 2017. V. 12. № 5. Article e0177574. https://doi.org/10.1371/journal.pone.0177574
  63. Braun R., Schönberger N., Vinke S., Lederer F., Kalinowski J., Pollmann K. // Viruses. 2020. V. 12. № 12. Article 1360. https://doi.org/10.3390/v12121360
  64. Peltomaa R., Benito–Peña E., Barderas R., Moreno–Bondi M.C. // ACS Omega. 2019. V. 4. № 7. P. 11569–11580.
  65. Smith G.P. // Science. 1985. V. 228. № 4705. P. 1315–1317.
  66. Smith G.P., Petrenko V.A. // Chem. Rev. 1997. V. 97. № 2. P. 391–410.
  67. Chassagne S., Laffly E., Drouet E., Hérodin F., Lefranc M.P., Thullier P. // Mol. Immunol. 2004. V. 41. № 5. P. 539–546.
  68. Jacobsson K., Rosander A., Bjerketorp J., Frykberg L. // Biol. Proced. Online. 2003. V. 5. P. 123–135.
  69. Stich N., Gandhum A., Matyushin V., Raats J., Mayer C., Alguel Y., Schalkhammer T. // J. Nanosci. Nanotechnol. 2002. V. 2. № 3–4. P. 375–381.
  70. Rudenko N., Fursova K., Banada P.P., Bhunia A.K. Antibodies and Immunoassays for Detection of Bacterial Pathogens. / Eds. M. Zourob, S. Elwary, A. Turner. N.Y.: Springer Science + Business Media, 2008. P. 567–602.
  71. Byrne B., Stack E., Gilmartin N., O’Kennedy R. // Sensors. 2009. V. 9. № 6. P. 4407–4445.
  72. Walper S.A., Lasarte Aragonés G., Sapsford K.E., Brown III C.W., Rowland C.E., Breger J.C., Medintz I.L. // ACS Sens. 2018. V. 3. № 10. P. 1894–2024.
  73. Rudenko N., Fursova K., Shepelyakovskaya A., Karatovskaya A., Brovko F. // Sensors. 2021. V. 21. № 22. Article 7614. https://doi.org/10.3390/s21227614
  74. Dykman L.A., Staroverov S.A., Guliy O.I., Ignatov O.V., Fomin A.S., Vidyasheva I.V. et al. // J. Immunoassay Immunochem. 2012. V. 33. № 2. P. 115–127.
  75. Гулий О.И., Зайцев Б.Д., Кузнецова И.Е., Шиxабудинов А.М., Каpаваева О.А., Дыкман Л.А., Cтаpовеpов C.А., Игнатов О.В. // Биофизика. 2012. Т. 57. № 3. С. 460–467.
  76. Huang S., Yang H., Lakshmanan R.S., Johnson M.L., Wan J., Chen I.-H. et al. // Biosens. Bioelectron. 2009. V. 24. № 6. P. 1730–1736.
  77. Guliy O.I., Velichko N.S., Fedonenko Yu.P., Bunin V.D. // Talanta. 2019. V. 202. P. 362–368.
  78. Гулий О.И., Величко Н.С., Федоненко Ю.П., Бунин В.Д. // Прикл. биохимия и микробиология. 2020. Т. 56. № 1. С. 96–104.
  79. Kuhn P., Thiem S., Steinert M., Purvis D., Lugmayr V., Treutlein U. et al. // Hum. Antibodies. 2017. V. 26. № 1. P. 29–38.
  80. Nanduri V., Bhunia A.K., Tu S.I., Paoli G.C., Brewster J.D. // Biosens. Bioelectron. 2007. V. 23. № 2. P. 248–252.
  81. Liu P., Han L., Wang F., Petrenko V.A., Liu A. // Biosens. Bioelectron. 2016. V. 82. P. 195–203.
  82. Wang X.-Y., Yang J.-Y., Wang Y.-T., Zhang H.-C., Chen M.-L., Yang T., Wang J.-H. // Talanta. 2021. V. 221. https://doi.org/10.1016/j.talanta.2020.121668
  83. De Plano L.M., Fazio E., Rizzo M.G., Franco D., Carnazza S., Trusso S., Neri F., Guglielmino S.P.P. // J. Immunol. Methods. 2019. V. 465. P. 45–52.
  84. Paoli G.C., Brewster J.D. // J. Rapid Methods Autom. Microbiol. 2007. V. 15. P. 77–91.
  85. McIvor M.J., Karoonuthaisiri N., Charlermroj R., Stewart L.D., Elliott C.T., Grant I.R. // PLoS One. 2013. V. 8. № 9. Article e74312.https://doi.org/10.1371/journal.pone.0074312
  86. Holst O., Ulmer, A.J., Brade H., Flad H.-D., Rietschel E.T. // FEMS Immunol. Med. Microbiol. 1996. V. 16. № 2. P. 83–104.
  87. Saunders N.J., Peden J.F., Hood D.W., Moxon E.R. // Mol. Microbiol. 1998. V. 27. № 6. P. 1091–1098.
  88. Kannenberg E.L., Carlson R.W. // Mol. Microbiol. 2001. V. 39. № 2. P. 379–391.
  89. Mora L., Newton W.E. Isolation, Identification and localization of Diazotrophic Bacteria from C4-plant Miscanthus. / Ed. B. Eckert. Dordrecht: Kluwer academic publishers, 2008. 705 p.
  90. Егоров А.М., Осипов А.П., Дзантиев Б.Б., Гаврилова Е.М. Теория и практика иммуноферментного анализа. М.: Изд-во “Высшая школа”, 1991. С. 3–42.
  91. Meyer T., Schirrmann T., Frenzel A., Miethe S., Stratmann–Selke J., Gerlach G.F. et al. // BMC Biotechnol. 2012. V. 12. Article 29. https://doi.org/10.1186/1472-6750-12-29
  92. Payandeh Z., Rasooli I., Mousavi Gargari S.L., Rajabi Bazl M., Ebrahimizadeh W. // Trans. R. Soc. Trop. Med. Hyg. 2014. V. 108. № 2. P. 92–98.
  93. Ahn B.E., Bae H.W., Lee H.R., Woo S.J., Park O.K., Jeon J.H., Park J., Rhie G.E. // Biochem. Biophys. Res. Commun. 2019. V. 509. № 2. P. 611–616.
  94. Hussein A.H., Davis E.M., Halperin S.A., Lee S.F. // Infect. Immun. 2007. V. 75. № 11. P. 5476–5482.
  95. Hayhurst A., Happe S., Mabry R., Koch Z., Iverson B.L., Georgiou G. // J. Immunol. Methods. 2003. V. 276. № 1–2. P. 185–196.
  96. Zou N., Newsome T., Li B., Tsai S., Lo S.-C. // Exp. Biol. Med. 2007. V. 232. № 4. P. 550–556.
  97. Gerstenbruch S., Brooks C.L., Kosma P., Brade L., Mackenzie C.R., Evans S.V., Brade H., Müller–Loennies S. // Glycobiology. 2010. V. 20. № 4. P. 461–472.
  98. Lindquist E.A., Marks J.D., Kleba B.J., Stephens R.S. // Microbiology. 2002. V. 148. № 2. P. 443–451.
  99. Shirvan A.N., Aitken R. // Braz. J. Microbiol. 2016. V. 47. № 2. P. 394–402.
  100. Alibeiki M., Golchin M., Tabatabaei M. // BMC Vet. Res. 2020. V. 16. № 1. Article 361. https://doi.org/10.1186/s12917-020-02572-4
  101. Salhi I., Bessalah S., Snoun D., Khorchani T., Hammadi M. // Iran. J. Biotechnol. 2020. V. 18. № 1. Article e2247. https://doi.org/10.30498/IJB.2020.127753.2247
  102. Mechaly A., Elia U., Alcalay R., Cohen H., Epstein E., Cohen O., Mazor O. // Sci. Rep. 2019. V. 9. № 1. Article 11418.https://doi.org/10.1038/s41598-019-47931-w
  103. Wang Q., Chang C.S., Pennini M., Pelletier M., Rajan S., Zha J. et al. // J. Infect. Dis. 2016. V. 213. № 11. P. 1800–1808.
  104. Reason D.C., Wagner T.C., Lucas A.H. // Infect. Immun. 1997. V. 65. № 1. P. 261–266.
  105. Fouladi M., Sarhadi S., Tohidkia M., Fahimi F., Samadi N., Sadeghi J., Barar J., Omidi Y. // Appl. Microbiol. Biotechnol. 2019. V. 103. № 8. P. 3407–3420.
  106. Fahimi F., Sarhaddi S., Fouladi M., Samadi N., Sadeghi J., Golchin A. et al. // Appl. Microbiol. Biotechnol. 2018. V. 102. № 16. P. 6899–6913.
  107. Close D.W., Ferrara F., Dichosa A.E., Kumar S., Daughton A.R., Daligault H.E. et al. // BMC Microbiol. 2013. V. 13. Article 270. https://doi.org/10.1186/1471-2180-13-270
  108. Mohd Ali M.R., Sum J.S., Aminuddin Baki N.N., Choong Y.S., Nor Amdan N.A., Amran F., Lim T.S. // Int. J. Biol. Macromol. 2021. V. 168. P. 289–300.
  109. Moreira G.M.S.G., Köllner S.M.S, Helmsing S., Jänsch L., Meier A., Gronow S. et al. // Sci. Rep. 2020. V. 10. № 1. Article 15267. https://doi.org/10.1038/s41598-020-72159-4
  110. Moreira G.M.S.G., Gronow S., Dübel S., Mendonça M., Moreira Â.N., Conceição F.R., Hust M. // Front. Public Health. 2022. V. 10. Article 712657. https://doi.org/10.3389/fpubh.2022.712657
  111. Tu Z., Chen Q., Li Y., Xiong Y., Xu Y., Hu N., Tao Y. // Anal. Biochem. 2016. V. 493. P. 1–7.
  112. Boel E., Bootsma H., de Kruif J., Jansze M., Klingman K.L., van Dijk H., Logtenberg T. // Infect. Immun. 1998. V. 66. № 1. P. 83–88.
  113. Fuchs M., Kämpfer S., Helmsing S., Spallek R., Oehlmann W., Prilop W. et al. // BMC Biotechnol. 2014. V. 14. Article 68. https://doi.org/10.1186/1472-6750-14-68
  114. Kawasaki M., Echiverri C., Raymond L., Cadena E., Reside E., Gler M.T. et al. // PLoS Med. 2019. V. 16. № 4. Article e1002780. https://doi.org/10.1371/journal.pmed.1002780
  115. Yan Z.-H., Zhao B., Pang Y., Wang X.-J., Yi L., Wang H.-L., Yang B., Wie P.-J., Jia H.-Y., Li S.-P., Zhao Y.-L., Zhang H.-T. // J. Microbiol. Immunol. Infect. 2021. V. 54. № 3. P. 437–446.
  116. Liu C.-Y., Weng C.-C., Lin C.-H., Yang C.-Y., Mong K.-K.T., Li Y.-K. // Biotechnol. Lett. 2017. V. 39. № 3. P. 407–413.
  117. Kulkarni A., Mochnáčová E., Majerova P., Čurlík J., Bhide K., Mertinková P., Bhide M. // Front. Mol. Biosci. 2020. V. 7. Article 573281. https://doi.org/10.3389/fmolb.2020.573281
  118. Skottrup P.D., Leonard P., Kaczmarek J.Z., Veillard F., Enghild J.J., O’Kennedy R. et al. // Anal. Biochem. 2011. V. 415. № 2. P. 158–167.
  119. Tout N.L., Lam J.S. // Clin. Diagn. Lab. Immunol. 1997. V. 4. № 2. P. 147–155.
  120. Postel S., Deredge D., Bonsor D.A., Yu X., Diederichs K., Helmsing S. et al. // Elife. 2016. V. 5. Article e18857. https://doi.org/10.7554/eLife.18857.001
  121. Zhang Y., Sun X., Qian Y., Yi H., Song K., Zhu H. et al. // J. Mol. Biol. 2019. V. 431. № 24. P. 4882–4896.
  122. Griep R.A., van Twisk C., van Beckhoven J.R., van der Wolf J.M., Schots A. // Phytopathology. 1998. V. 88. № 8. P. 795–803.
  123. Nian S., Wu T., Ye Y., Wang X., Xu W., Yuan Q. // BMC Immunol. 2016. V. 17. № 1. Article 8. https://doi.org/10.1186/s12865-016-0146-z
  124. Zanganeh S., Rouhani Nejad H., Mehrabadi J.F., Hosseini R., Shahi B., Tavassoli Z., Aramvash A. // Appl. Biochem. Biotechnol. 2019. V. 187. № 2. P. 493–505.
  125. de Greeff A., van Alphen L., Smith H.E. // Infect. Immun. 2000. V. 68. № 7. P. 3949–3955.
  126. Ebrahimizadeh W., Mousavi Gargari S., Rajabibazl M., Safaee Ardekani L., Zare H., Bakherad H. // Appl. Microbiol. Biotechnol. 2013. V. 97. № 10. P. 4457–4466.
  127. Yu J., Sun Z., Sun X., Sun X., Wei H., Jia W. et al. // Microb. Pathog. 2020. V. 143. Article 104136. https://doi.org/10.1016/j.micpath.2020.104136
  128. Lillo A.M., Ayriss J.E., Shou Y., Graves S.W., Bradbury A.R., Pavlik P. // PLoS One. 2011. V. 6. № 12. Article e27756. https://doi.org/10.1371/journal.pone.0027756
  129. Hust M., Meyer T., Voedisch B., Rülker T., Thie H., El-Ghezal A. et al. // J. Biotechnol. 2011. V. 152. № 4. P. 159–170.
  130. Ch’ng A.C.W., Choong Y.S., Lim T.S. Phage Display-Derived Antibodies: Application of Recombinant Antibodies for Diagnostics. / Ed. S.K. Saxena. London: IntechOpen Limited, 2016. P. 107–135.
  131. Beadle C., Long G.W., Weiss W.R., McElroy P.D., Maret S.M., Oloo A.J., Hoffman S.L. // Lancet. 1994. V. 343. № 8897. P. 564–568.
  132. Grilo A.L., Mantalaris A. // Trends Biotechnol. 2019. V. 37. P. 9–16.

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