DOI QR코드

DOI QR Code

Virus Inactivation during the Manufacture of a Collagen Type I from Bovine Hides

소 가죽 유래 Type I Collagen 생산 공정에서 바이러스 불활화

  • Bae, Jung Eun (Department of Biological Sciences and Biotechnology, Center for Biopharmaceuticals Safety Validation, Hannam University) ;
  • Kim, Chan Kyung (Department of Biological Sciences and Biotechnology, Center for Biopharmaceuticals Safety Validation, Hannam University) ;
  • Kim, Sungpo (R&D Center, Bioland Co. Ltd.) ;
  • Yang, Eun Kyung (R&D Center, Bioland Co. Ltd.) ;
  • Kim, In Seop (Department of Biological Sciences and Biotechnology, Center for Biopharmaceuticals Safety Validation, Hannam University)
  • 배정은 (한남대학교 생명.나노과학대학 생명시스템과학과 & 바이오의약품안전성검증센터) ;
  • 김찬경 (한남대학교 생명.나노과학대학 생명시스템과학과 & 바이오의약품안전성검증센터) ;
  • 김성포 ((주)바이오랜드 조직공학연구소) ;
  • 양은경 ((주)바이오랜드 조직공학연구소) ;
  • 김인섭 (한남대학교 생명.나노과학대학 생명시스템과학과 & 바이오의약품안전성검증센터)
  • Received : 2012.10.29
  • Accepted : 2012.12.12
  • Published : 2012.12.31

Abstract

Most types of collagen used for biomedical applications, such as cell therapy and tissue engineering, are derived from animal tissues. Therefore, special precautions must be taken during the production of these proteins in order to assure against the possibility of the products transmitting infectious diseases to the recipients. The ability to remove and/or inactivate known and potential viral contaminants during the manufacturing process is an ever-increasingly important parameter in assessing the safety of biomedical products. The purpose of this study was to evaluate the efficacies of the 70% ethanol treatment and pepsin treatment at pH 2.0 for the inactivation of bovine viruses during the manufacture of collagen type I from bovine hides. A variety of experimental model viruses for bovine viruses including bovine herpes virus (BHV), bovine viral diarrhea virus (BVDV), bovine parainfluenza 3 virus (BPIV-3), and bovine parvovirus (BPV), were chosen for the evaluation of viral inactivation efficacy. BHV, BVDV, BPIV-3, and BPV were effectively inactivated to undetectable levels within 1 h of 70% ethanol treatment for 24 h, with log reduction factors of ${\geq}5.58$, ${\geq}5.32$, ${\geq}5.11$, and ${\geq}3.42$, respectively. BHV, BVDV, BPIV-3, and BPV were also effectively inactivated to undetectable levels within 5 days of pepsin treatment for 14 days, with the log reduction factors of ${\geq}7.08$, ${\geq}6.60$, ${\geq}5.60$, and ${\geq}3.59$, respectively. The cumulative virus reduction factors of BHV, BVDV, BPIV-3, and BPV were ${\geq}12.66$, ${\geq}11.92$, ${\geq}10.71$, and ${\geq}7.01$. These results indicate that the production process for collagen type I from bovine hides has a sufficient virus-reducing capacity to achieve a high margin of virus safety.

Keywords

bovine collagen;ethanol treatment;pepsin treatment;virus safety

References

  1. Bae, J.E., Kim, J., Ahn, J., Choi, D.M., Jeong, H.S., Lee, D.H., and Kim, I.S. 2010a. Virus inactivation process for manufacturing of human acellular dermal matrix. Kor. J. Microbiol. Biotechnol. 38, 168-176.
  2. Bae, J.E., Kim, C.K., and Kim, I.S. 2009. Inactivation of infectious microorganisms by disinfection and sterilization processes for human amniotic membrane grafts. Kor. J. Microbiol. 45, 346-353.
  3. Bae, J.E., Kim, C.K., Kim, S., Yang, E.K., and Kim, I.S. 2010b. Process development of a virally-safe acellular bovine amniotic membrane for biological dressing. Kor. J. Microbiol. Biotechnol. 38, 420-427.
  4. Di Lullo, G.A., Sweeney, S.M., Korkko, J., Ala-Kokko, L., and San Antonio, J.D. 2002. Mapping the ligand-binding sites and disease-associated mutations on the most abundant protein in the human, type I collagen. J. Biol. Chem. 277, 4223-4231. https://doi.org/10.1074/jbc.M110709200
  5. Engelenburg, F.A.C., Terpstra, F.G., Schuitemaker, H., and Moorer, W.R. 2002. The virucidal spectrum of a high concentration alcohol mixture. J. Hospital Infect. 51, 121-125. https://doi.org/10.1053/jhin.2002.1211
  6. Eterpi, M., McDonnell, G., and Thomas, V. 2009. Disinfection efficacy against parvoviruses compared with reference viruses. J. Hospital Infect. 73, 64-70. https://doi.org/10.1016/j.jhin.2009.05.016
  7. Forest, P., Morfin, F., Bergeron, E., Dore, J., Bensa, S., Wittmann, C., Picot, S., Renaud, F.N., Freney, J., and Gagnieu, C. 2007. Validation of a viral and bacterial inactivation step during the extraction and purification process of porcine collagen. Biomed. Mater. Eng. 17, 199 -208.
  8. Franchi, M., Trire, A., Quaranta, M., Orsini, E., and Ottani, V. 2007. Collagen structure of tendon relates to function. Sci. World J. 7, 404- 420. https://doi.org/10.1100/tsw.2007.92
  9. Harkness, R.D. 1961. Biological functions of collagen. Biol. Rev. 36, 399-463. https://doi.org/10.1111/j.1469-185X.1961.tb01596.x
  10. Hodde, J. and Hiles, M. 2002. Virus safety of a porcine-derived medical device: evaluation of a viral inactivation method. Biotechnol. Bioeng. 79, 211-216. https://doi.org/10.1002/bit.10281
  11. International Conference on Harmonisation. 1998. Guidance on viral safety evaluation of biotechnology products derived from cell lines of human or animal origin. Federal Resister 63, 51074-51084.
  12. International Organization for Sandardization. 1998. Sterilization of medical devices-Microbiological methods. Part 2: Test of sterility performed in the validation of a sterilization process. Geneva, Switzerland.
  13. International Organization for Standardization. 2002. Sterilization of health care products - Radiation sterilization-Substantiation of 25 kGy as a sterilization dose for small or infrequent production batches. Geneva, Switzerland.
  14. Karber, J. 1931. Beitrag zur kollectiven Behandlung pharmakologische Reihenversuche. Arch. Exp. Path. Pharmak. 162, 480-483. https://doi.org/10.1007/BF01863914
  15. Kim, I.S., Choi, Y.W., Lee, S.R., Cho, H.B., Eo, H.G., Woo, H.S., Chang, C.E., and Lee, S. 2001. Improvement of virus safety of a human intravenous immunoglobulin by low pH incubation. J. Microbiol. Biotechnol. 11, 619-627.
  16. Kim, I.S., Eo, H.G., Chang, C.E., and Lee, S. 2000. Partitioning and inactivation of viruses by cold ethanol fractionation and pasteurization during manufacture of albumin from human plasma. J. Microbiol. Biotechnol. 10, 858-864.
  17. Lee, C.H., Singla, A., and Lee, Y. 2001. Biomedical applications of collagen. Int. J. Pharm. 221, 1-22. https://doi.org/10.1016/S0378-5173(01)00691-3
  18. Ma, J., Holden, K., Zhu, J., Pan, H., and Li, Y. 2011. The application of three-dimensional collagen-scaffolds seeded with myoblasts to repair skeletal muscle defects. J. Biomed. Biotechnol. Article ID 812135.
  19. Malafaya, P.B., Silva, G.A., Baran, E.T., and Reis, R.L. 2002. Drug delivery therapies I : General trends and its importance on bone tissue engineering applications. Curr. Opin. Solid Sate Mat. Science 6, 283- 295. https://doi.org/10.1016/S1359-0286(02)00075-X
  20. Malafaya, P.B., Silva, G.A., and Reis, R.L. 2007. Natural-origin polymers as carriers and scaffolds for biomolecules and cell delivery in tissue engineering applications. Adv. Drug Deliv. Rev. 59, 207-233. https://doi.org/10.1016/j.addr.2007.03.012
  21. McDonnell, G.E. 2007a. Antisepsis, disinfection, and sterilization, pp. 79-83. ASM Press, Washington, D.C., USA.
  22. McDonnell, G.E. 2007b. Antisepsis, disinfection, and sterilization, pp. 90-92. ASM Press, Washington, D.C., USA.
  23. Pruss, A., Kao, M., Garrel, T., Frommelt, L., Gurtler, L., Benedix, F., and Pauli, G. 2003. Virus inactivation in bone tissue transplants (femoral heads) by moist heat with the 'Marburg bone bank system'. Biologicals 31, 75-82. https://doi.org/10.1016/S1045-1056(02)00095-7
  24. Shoulders, M.D. and Raines, R.T. 2009. Collagen structure and stability. Annu. Rev. Biochem. 78, 929-958. https://doi.org/10.1146/annurev.biochem.77.032207.120833
  25. Willerth, S.M. and Sakiyama-Elbert, S.E. 2007. Approaches to neural tissue engineering using scaffolds for drug delivery. Adv. Drug Deliv. Rev. 59, 325-338. https://doi.org/10.1016/j.addr.2007.03.014

Cited by

  1. Process development of a virally-safe dental xenograft material from porcine bones vol.52, pp.2, 2016, https://doi.org/10.7845/kjm.2016.6019