Optimization of the Production Process and Characterization of the Yeast-Expressed SARS-CoV Recombinant Receptor-Binding Domain (RBD219-N1), a SARS Vaccine Candidate

Journal of Pharmaceutical Sciences

Volumn 106, Issue 8, 2017, Pages 1961-1970

  Chen, Wen Hsiang ^a   Chag, Shivali M ^a   Poongavanam, Mohan V ^a   Biter, Amadeo B ^a   Ewere, Ebe A ^a   Rezende, Wanderson ^a   Seid, Christopher A ^a   Hudspeth, Elissa M ^a   Pollet, Jeroen ^a,b   McAtee, C Patrick ^a   Strych, Ulrich ^a,b   Bottazzi, Maria Elena ^a,b,c   Hotez, Peter J ^a,b,c,d  

^a TEXAS CHILDREN S HOSPITAL   (United States)

^b BAYLOR COLLEGE OF MEDICINE   (United States)

^c BAYLOR UNIVERSITY   (United States)

^d RICE UNIVERSITY   (United States)

Author keywords

circular dichroism; hydrophobic interaction chromatography; Pichia pastoris; protein characterization; protein purification

Indexed keywords

ALUMINUM HYDROXIDE; NEUTRALIZING ANTIBODY; RECEPTOR BINDING DOMAIN 219 N1; RECOMBINANT PROTEIN; RECOMBINANT RECEPTOR; SEVERE ACUTE RESPIRATORY SYNDROME VACCINE; UNCLASSIFIED DRUG; CORONAVIRUS SPIKE GLYCOPROTEIN; RECOMBINANT VACCINE; S PROTEIN, SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS; VIRUS VACCINE;

ANTIBODY TITER; ARTICLE; CONTROLLED STUDY; FERMENTATION; KOMAGATAELLA PASTORIS; NONHUMAN; PROCESS OPTIMIZATION; PROTEIN EXPRESSION; PROTEIN PURIFICATION; RECEPTOR BINDING; SARS CORONAVIRUS; SUPERNATANT; CHEMISTRY; GENETICS; HUMAN; ISOLATION AND PURIFICATION; MICROBIOLOGY; MOLECULAR CLONING; PICHIA; PROCEDURES; PROTEIN DOMAIN; SEVERE ACUTE RESPIRATORY SYNDROME; VIROLOGY;

CLONING, MOLECULAR; FERMENTATION; HUMANS; INDUSTRIAL MICROBIOLOGY; PICHIA; PROTEIN DOMAINS; RECOMBINANT PROTEINS; SARS VIRUS; SEVERE ACUTE RESPIRATORY SYNDROME; SPIKE GLYCOPROTEIN, CORONAVIRUS; VACCINES, SYNTHETIC; VIRAL VACCINES;

EID: 85020022873     PISSN: 00223549     EISSN: 15206017     Source Type: Journal    
DOI: 10.1016/j.xphs.2017.04.037     Document Type: Article

References (32)

1. Du, L., He, Y., Zhou, Y., Liu, S., Zheng, B.-J., Jiang, S., The spike protein of SARS-CoV—a target for vaccine and therapeutic development. Nat Reviews Microbiol 7:3 (2009), 226–236.
2. Perlman, S., Dandekar, A.A., Immunopathogenesis of coronavirus infections: implications for SARS. Nat Rev Immunol 5:12 (2005), 917–927.
3. Bolles, M., Deming, D., Long, K., et al. A double-inactivated severe acute respiratory syndrome coronavirus vaccine provides incomplete protection in mice and induces increased eosinophilic proinflammatory pulmonary response upon challenge. J Virol 85:23 (2011), 12201–12215.
4. Jaume, M., Yip, M.S., Kam, Y.W., et al. SARS CoV subunit vaccine: antibody-mediated neutralisation and enhancement. Hong Kong Med J 18 Suppl 2 (2012), 31–36.
5. Wong, S.K., Li, W., Moore, M.J., Choe, H., Farzan, M., A 193-amino acid fragment of the SARS coronavirus S protein efficiently binds angiotensin-converting enzyme 2. J Biol Chem 279:5 (2004), 3197–3201.
6. Jiang, S., Bottazzi, M.E., Du, L., et al. Roadmap to developing a recombinant coronavirus S protein receptor-binding domain vaccine for severe acute respiratory syndrome. Expert Rev Vaccin 11:12 (2012), 1405–1413.
7. Du, L., Zhao, G., Li, L., et al. Antigenicity and immunogenicity of SARS-CoV S protein receptor-binding domain stably expressed in CHO cells. Biochem Biophys Res Commun 384:4 (2009), 486–490.
8. Du, L., Zhao, G., Chan, C.C., et al. Recombinant receptor-binding domain of SARS-CoV spike protein expressed in mammalian, insect and E. coli cells elicits potent neutralizing antibody and protective immunity. Virology 393:1 (2009), 144–150.
9. He, Y., Lu, H., Siddiqui, P., Zhou, Y., Jiang, S., Receptor-binding domain of severe acute respiratory syndrome coronavirus spike protein contains multiple conformation-dependent epitopes that induce highly potent neutralizing antibodies. J Immunol 174:8 (2005), 4908–4915.
10. He, Y., Li, J., Li, W., Lustigman, S., Farzan, M., Jiang, S., Cross-neutralization of human and palm civet severe acute respiratory syndrome coronaviruses by antibodies targeting the receptor-binding domain of spike protein. J Immunol 176:10 (2006), 6085–6092.
11. Du, L., Zhao, G., He, Y., et al. Receptor-binding domain of SARS-CoV spike protein induces long-term protective immunity in an animal model. Vaccine 25:15 (2007), 2832–2838.
12. Du, L., Zhao, G., Chan, C.C., et al. A 219-mer CHO-expressing receptor-binding domain of SARS-CoV S protein induces potent immune responses and protective immunity. Viral Immunol 23:2 (2010), 211–219.
13. Chen, W.-H., Du, L., Chag, S.M., et al. Yeast-expressed recombinant protein of the receptor-binding domain in SARS-CoV spike protein with deglycosylated forms as a SARS vaccine candidate. Hum Vaccin Immunother 10:3 (2014), 648–658.
14. Goud, G.N., Zhan, B., Ghosh, K., et al. Cloning, yeast expression, isolation, and vaccine testing of recombinant Ancylostoma-secreted protein (ASP)-1 and ASP-2 from Ancylostoma ceylanicum. J Infect Dis 189:5 (2004), 919–929.
15. Lin, H., Kim, T., Xiong, F., Yang, X., Enhancing the production of Fc fusion protein in fed-batch fermentation of Pichia pastoris by design of experiments. Biotechnol Prog 23:3 (2007), 621–625.
16. Zhu, D., Saul, A.J., Miles, A.P., A quantitative slot blot assay for host cell protein impurities in recombinant proteins expressed in E. coli. J Immunol Methods 306:1-2 (2005), 40–50.
17. Plieskatt, J., Rezende, W., Olsen, C., et al. Advances in vaccines against neglected tropical diseases. Hum Vaccin Immunother 8:6 (2012), 765–776.
18. Curti, E., Seid, C.A., Hudspeth, E., et al. Optimization and revision of the production process of the Necator americanus glutathione S-transferase 1 (Na-GST-1), the lead hookworm vaccine recombinant protein candidate. Hum Vaccin Immunother 10:7 (2014), 1914–1925.
19. Sackett, D.L., Wolff, J., Nile red as a polarity-sensitive fluorescent probe of hydrophobic protein surfaces. Anal Biochem 167:2 (1987), 228–234.
20. Haskard, C.A., Li-Chan, E.C.Y., Hydrophobicity of bovine serum albumin and ovalbumin determined using uncharged (PRODAN) and anionic (ANS-) fluorescent probes. J Agric Food Chem 46:7 (1998), 2671–2677.
21. Kato, A., Nakai, S., Hydrophobicity determined by a fluorescence probe method and its correlation with surface properties of proteins. Biochim Biophys Acta 624:1 (1980), 13–20.
22. Saluja, A., Fesinmeyer, R.M., Hogan, S., Brems, D.N., Gokarn, Y.R., Diffusion and sedimentation interaction parameters for measuring the second virial coefficient and their utility as predictors of protein aggregation. Biophys J 99:8 (2010), 2657–2665.
23. Tal, M., Silberstein, A., Nusser, E., Why does Coomassie Brilliant Blue R interact differently with different proteins? A partial answer. J Biol Chem 260:18 (1985), 9976–9980.
24. Cao, Z., Liu, L., Du, L., et al. Potent and persistent antibody responses against the receptor-binding domain of SARS-CoV spike protein in recovered patients. Virol J 7:1 (2010), 1–6.
25. Vedvick, T., Buckholz, R.G., Engel, M., et al. High-level secretion of biologically active aprotinin from the yeast Pichia pastoris. J Ind Microbiol 7:3 (1991), 197–201.
26. Werten, M.W., van den Bosch, T.J., Wind, R.D., Mooibroek, H., de Wolf, F.A., High-yield secretion of recombinant gelatins by Pichia pastoris. Yeast 15:11 (1999), 1087–1096.
27. Punt, P.J., van Biezen, N., Conesa, A., Albers, A., Mangnus, J., van den Hondel, C., Filamentous fungi as cell factories for heterologous protein production. Trends Biotechnol 20:5 (2002), 200–206.
28. Cereghino, G.P.L., Cereghino, J.L., Ilgen, C., Cregg, J.M., Production of recombinant proteins in fermenter cultures of the yeast Pichia pastoris. Curr Opin Biotechnol 13:4 (2002), 329–332.
29. Athmaram, T.N., Singh, A.K., Saraswat, S., et al. A simple Pichia pastoris fermentation and downstream processing strategy for making recombinant pandemic Swine Origin Influenza A virus Hemagglutinin protein. J Ind Microbiol Biotechnol 40:2 (2013), 245–255.
30. Goud, G.N., Deumic, V., Gupta, R., et al. Expression, purification, and molecular analysis of the Necator americanus glutathione S-transferase 1 (Na-GST-1): a production process developed for a lead candidate recombinant hookworm vaccine antigen. Protein Expr Purif 83:2 (2012), 145–151.
31. Curti, E., Kwityn, C., Zhan, B., et al. Expression at a 20L scale and purification of the extracellular domain of the Schistosoma mansoni TSP-2 recombinant protein: a vaccine candidate for human intestinal schistosomiasis. Hum Vaccin Immunother 9:11 (2012), 2342–2350.
32. Switzer, R.C. 3rd, Merril, C.R., Shifrin, S., A highly sensitive silver stain for detecting proteins and peptides in polyacrylamide gels. Anal Biochem 98:1 (1979), 231–237.