Dependence of the Group Specificity of Immunoenzyme Determination of Penicillins in Milk on the Temperature and Duration of Antibiotic Cross Reactions with Polyclonal Antibodies

Cover Page

Cite item

Full Text

Open Access Open Access
Restricted Access Access granted
Restricted Access Subscription Access

Abstract

The influence of thermodynamic and kinetic conditions on the interaction of polyclonal antibodies to penicillins with the antibiotics of a penicillin group was studied in the system of a direct enzyme-linked immunosorbent assay (ELISA). Minimum differences in the cross reactions of the polyclonal antibodies with different penicillins were observed when the ELISA was carried out at 4°C for 1 hour. An increase in temperature and duration of the assay led to an increase in antibodies reactivity only to amoxicillin, and significantly enhanced differences among the sensitivities of individual penicillins determination. Under the chosen assay conditions, the following antibodies cross-reactivity values were obtained: to penicillin G — 90%, to ampicillin — 100%, to amoxicillin — 110%. The analytical sensitivity was 0.03 ng/mL for ampicillin, and the limit of ampicillin quantification in milk was 0.4 μg/L. The developed group-specific ELISA was used for the determination in milk of seven penicillins that are regulatory controlled in foods and raw materials of animal origin — penicillin G, ampicillin, amoxicillin, cloxacillin, oxacillin, dicloxacillin and nafcillin.

Full Text

Restricted Access

About the authors

O. S. Kuprienko

Institute of Bioorganic Chemistry, National Academy of Sciences of Belarus

Author for correspondence.
Email: kuprienko@iboch.by
Belarus, Minsk, 220084

I. I. Vashkevich

Institute of Bioorganic Chemistry, National Academy of Sciences of Belarus

Email: kuprienko@iboch.by
Belarus, Minsk, 220084

A. I. Zilberman

Institute of Bioorganic Chemistry, National Academy of Sciences of Belarus

Email: kuprienko@iboch.by
Belarus, Minsk, 220084

O. V. Sviridov

Institute of Bioorganic Chemistry, National Academy of Sciences of Belarus

Email: kuprienko@iboch.by
Belarus, Minsk, 220084

References

  1. Miller E. L. // J. Midwifery Women’s Health. 2002. V. 47. № 6. P. 426–434. https://doi.org/10.1016/s1526-9523(02)00330-6
  2. Nathwani D., Wood M. J. // Drugs. 1993. V. 45. № 6. P. 866–894. https://doi.org/10.2165/00003495-199345060-00002
  3. Шульга Н. Н., Шульга И. С., Плавшак Л. П. // Тенденции развития науки и образования. 2019. Т. 46. № 5. С. 32–35. https://doi.org/10.18411/lj-01-2019-98
  4. Sazykin I. S., Khmelevtsova L. E., Seliverstova E. Y., Sazykina M. A. // Appl. Biochem. Microbiol. 2021. V. 57. № 1. P. 20–30. https://doi.org/10.1134/S0003683821010166
  5. Berendonk T. U., Manaia C. M., Merlin C., Fatta-Kassinos D., Cytryn E., Walsh F., et al. // Nat. Rev. Microbiol. 2015. V. 13. P. 310–317. https://doi.org/10.1038/nrmicro3439
  6. Шевелева С. А., Хотимченко С. А., Минаева Л. П., Смотрина Ю. В. // Вопросы питания. 2021. Т. 90. № 3. С. 50–57. https://doi.org/10.33029/0042-8833-2021-90-3-50-57
  7. Van Hoek A. H.A.M., Mevius D., Guerra B., Mullany P., Roberts A. P., Aarts H. J.M. // Front. Microbiol. 2011. V. 2. Article 203. https://doi.org/10.3389/fmicb.2011.00203
  8. Mikhaleva T. V., Ilyasov P. V., Zakharova O. I. // Appl. Biochem. Microbiol. 2019. V. 55. № 2. P. 99–106. https://doi.org//10.1134/S000368381902011X
  9. Решение Коллегии Евразийской экономической комиссии от 13 февраля 2018 г. № 28. docs.eaeunion.org/docs/ru-ru/01217013/clc-d_15022018_28
  10. European Comission. Council Regulation (EU) No. 37/2010 of 22 December 2009 on Pharmacologically Active Substances and their Classification Regarding Maximum Residue Limits in Foodstuffs of Animal Origin. // Official Journal of the European Union. 2010. L 15/10.
  11. Barros S. C., Silva A. S., Torres D. // Antibiotics 2023. V. 12. № 2. P. 202. https://doi.org/10.3390/antibiotics12020202
  12. Moga A., Vergara-Barberán M., Lerma-García M.J., Carrasco-Correa E.J., Herrero-Martínez J.M., Simó-Alfonso E.F. // Compr. Rev. Food Sci. Food Saf. 2021. V. 20. № 2. P. 1681–1716. https://doi.org/10.1111/1541-4337.12702
  13. Marazuela M. D., Bogialli S. // Anal. Chim. Acta. 2009. Vol. 645. № 1–2. P. 5–17. https://doi.org/10.1016/j.aca.2009.04.031
  14. Holstege D. M., Puschner B., Whitehead G., Galey F. D. // J. Agric. Food. Chem. 2002. V. 50. № 2. P. 406–411. https://doi.org/10.1021/jf010994s
  15. Pugajeva I., Ikkere L. E., Judjallo E., Bartkevics V. // J. Pharm. Biomed. Anal. 2019. V. 166. P. 252–263. https://doi.org/10.1016/j.jpba.2019.01.024
  16. Bessaire T., Mujahid C., Beck A., Tarres A., Savoy M. C., Woo P. M. et al. // Food Addit. Contam. Part A. 2018. V. 35. № 4. P. 661–673. https://doi.org/10.1080/19440049.2018.1426891
  17. Dzantiev B. B., Byzova N. A., Urusov A. E., Zherdev A. V. // Trends Anal. Chem. 2014. V. 55. P. 81–93. https://doi.org/10.1016/j.trac.2013.11.007.
  18. Reig M., Toldrá F. // Meat Sci. 2008. V. 78. № 1–2. P. 60–67. https://doi.org/10.1016/j.meatsci.2007.07.029
  19. Duffy G. F., Moore E. J. // Anal. Lett. 2017. V. 50. № 1. P. 1–32. https://doi.org/10.1080/00032719.2016.1167900
  20. Xu F., Ren K., Yang Y. Z., Guo J. P., Ma G. P., Liu Y. M. et al. // J. Integ. Agric. 2015. V. 14. № 11. P. 2282–2295. https://doi.org/10.1016/S2095-3119(15)61121-2.
  21. Serchenya T. S., Semizhon P. A., Schaslionak A. P., Harbachova I. V., Vashkevich I. I., Sviridov O. V. // Appl. Biochem. Microbiol. 2023. V. 59. № 1. P. 79–92. https://doi.org/10.1134/S0003683823010106
  22. Samsonova Z. V., Shchelokova O. S., Ivanova N. L., Rubtsova M. Y., Egorov A. M. // Appl. Biochem. Microbiol. 2005. V. 41. № 6. P. 589–595. https://doi.org/10.1007/s10438-005-0107-4
  23. Bacigalupo M. A., Meroni G., Secundo F., Lelli R. // Talanta. 2008. V. 77. № 1. P. 126–130. https://doi.org/10.1016/j.talanta.2008.05.057
  24. Jiao S. N., Wang P., Zhao G. X., Zhang H. C., Liu J., Wang J. P. // J. Environ. Sci. Health B. 2013. V. 48. № 6. P. 486–494. https://doi.org/10.1080/03601234.2013.761908
  25. Zeng K., Zhang J., Wang Y., Wang Z. H., Zhang S. X., Wu C. M. et al. // Biomed. Environ. Sci. 2013. V. 26. № 2. P. 100–109. https://doi.org/10.3967/0895-3988.2013.02.004
  26. Peng, J., Cheng, G., Huang, L., Wang Y., Hao H., Peng D. et al. // Anal. Bioanal. Chem. 2013. V. 405. P. 8925–8933. https://doi.org/10.1007/s00216-013-7311-5
  27. Serchenya T. S., Harbachova I. V., Sviridov O. V. // Russ. J. Bioorg. Chem. 2022. V. 48. № 1. P. 85–95. https://doi.org/10.1134/S1068162022010125
  28. Shanin I. A., Eremin S. A., Zvereva E. A., Zherdev A. V., Dzantiev B. B., Sviridov O. V. // Appl. Biochem. Microbiol. 2019. V. 55. № 5. P. 563–569. https://doi.org/10.1134/S0003683819050132
  29. Kuprienko O. S., Serchenya T. S., Vashkevich I. I., Harbachova I. V., Zilberman A. I., Sviridov O. V. // Russ. J. Bioorg. Chem. 2022. V. 48. № 1. P. 105–114. https://doi.org/10.1134/S106816202201006X
  30. Sotnikov D. V., Zherdev A. V., Zvereva E. A., Eremin S. A., Dzantiev B. B. // Appl. Sci. 2021. V. 11. № 14. Article 6581. https://doi.org/10.3390/app11146581
  31. Boutten B., Ezan E., Mamas S., Dray F. // Clin. Chem. 1991. V. 37. № 3. P. 394–397. https://doi.org/10.1093/clinchem/37.3.394
  32. Sulea T., Rohani N., Baardsnes J., Corbeil C. R., Deprez C., Cepero-Donates Y. et al. // MAbs. 2020. Vol. 12. № 1. Article 1682866. https://doi.org/10.1080/19420862.2019.1682866
  33. Miller J. J., Valdes R. // Clin. Chem. 1991. V. 37. № 2. P. 144–153. https://doi.org/10.1093/clinchem/37.2.144
  34. Sheehan C., He J., Smith M. The Immunoassay Handbook. 4 Ed. /Ed. D. Wild. Amsterdam: Elsevier, 2013. P. 395–402. https://doi.org/10.1016/B978-0-08-097037-0.00026-9
  35. Komova N. S., Berlina A. N., Zherdev A. V., Dzantiev B. B. // Orient. J. Chem. 2020. V. 36. № 1. P. 21–25. https://doi.org/10.13005/ojc/360103

Supplementary files

Supplementary Files
Action
1. JATS XML
Download
2. Fig.1

Download (13KB)
Indexing metadata
3. Fig.2

Download (14KB)
Indexing metadata
4. Fig.3

Download (15KB)
Indexing metadata
5. Fig.4

Download (16KB)
Indexing metadata
6. Fig.5

Download (15KB)
Indexing metadata
7. Fig.6

Download (17KB)
Indexing metadata
8. Fig.7

Download (16KB)
Indexing metadata
9. Fig. 1. Inhibition curves of binding of the Amp-HRP conjugate to PAb in the presence of penicillin G (1), ampicillin (2) or amoxicillin (3) during incubation for 1 h at temperatures of 4 (a), 25 (b) or 37°C (c).

Download (187KB)
Indexing metadata
10. Fig. 2. Inhibition curves of binding of the Amp-HRP conjugate to PAb in the presence of penicillin G (1), ampicillin (2) or amoxicillin (3) during incubation for 2 h (a) or 18 h (b) at 4 °C.

Download (148KB)
Indexing metadata
11. Fig. 3. IC50 values ​​for penicillin G (1) and amoxicillin (2) using different penicillin-HRP conjugates (incubation for 1 h at 4°C). I — Amp-HRP; II — Amox-HRP; III — Amp-Ad-HRP; IV — Amox-pFT-HRP.

Download (54KB)
Indexing metadata
12. Fig. 4. Completeness of detection of penicillin group antibiotics (%) added to milk samples. The values ​​obtained by ELISA (1) and recalculated taking into account the PR of specific PAbs (2) are presented. I — penicillin G; II — ampicillin; III — amoxicillin; IV — oxacillin; V — cloxacillin; VI — dicloxacillin; VII — nafcillin.

Download (74KB)
Indexing metadata

Copyright (c) 2024 Russian Academy of Sciences