A recombinant mutant abrin A chain expressed in Escherichia coli can be used as an effective vaccine candidate

Human Vaccines

Volumn 7, Issue 8, 2011, Pages 838-844

  Han, Yan Hui ^a,b   Gao, Shan ^a   Xin, Wen Wen ^a   Kang, Lin ^a   Wang, Jing Lin ^a  

^a BEIJING INSTITUTE OF MICROBIOLOGY AND EPIDEMIOLOGY   (China)

^b WUHAN GENERAL HOSPITAL OF GUANGZHOU COMMAND   (China)

Author keywords

Abrin A chain; Immunogen; Mutant abrin A chain; Vaccine candidate

Indexed keywords

IMMUNOLOGICAL ADJUVANT; RECOMBINANT MUTANT ABRIN A CHAIN VACCINE; UNCLASSIFIED DRUG; VACCINE; ABRIN; ANTIBODY; RECOMBINANT PROTEIN; RECOMBINANT VACCINE;

ABRIN TOXICITY; AFFINITY CHROMATOGRAPHY; AMINO ACID SUBSTITUTION; ANIMAL EXPERIMENT; ANIMAL MODEL; ANTIBODY TITER; ARTICLE; CONTROLLED STUDY; CYTOTOXICITY; DRUG EFFICACY; ESCHERICHIA COLI; HUMAN; HUMAN CELL; IC 50; IMMUNE RESPONSE; IMMUNOGENICITY; IMMUNOREACTIVITY; LD 50; MALE; MOUSE; NONHUMAN; NUCLEOTIDE SEQUENCE; PHYTOTOXICITY; PROTEIN EXPRESSION; PROTEIN PURIFICATION; SITE DIRECTED MUTAGENESIS; TOXICITY TESTING; ABRUS; ANIMAL; BAGG ALBINO MOUSE; BIOSYNTHESIS; BLOOD; DNA SEQUENCE; FEMALE; GENETICS; IMMUNOLOGY; MOLECULAR GENETICS; MUTATION; VACCINATION;

ABRIN; ABRUS; ANIMALS; ANTIBODIES; BASE SEQUENCE; ESCHERICHIA COLI; FEMALE; MICE; MICE, INBRED BALB C; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; MUTATION; RECOMBINANT PROTEINS; SEQUENCE ANALYSIS, DNA; VACCINATION; VACCINES, SYNTHETIC;

EID: 85046979973     PISSN: 15548600     EISSN: 15548619     Source Type: Journal    
DOI: 10.4161/hv.7.8.16258     Document Type: Article

References (25)

1. Olsnes S., Sandvig K., Eiklid K., Pihl A. Properties and action mechanism of the toxic lectin modeccin: interaction with cell lines resistant to modeccin, abrin and ricin. J Supramol Struct 1978; 9:15-25; PMID:732310; DOI:10.1002/jss.400090103.
2. Benson S., Olsnes S., Pihl A., Skorve J., Abraham AK. On the mechanism of protein-synthesis inhibition by abrin and ricin. Inhibition of the GTP-hydrolysis site on the 60-S ribosomal subunit. Eur J Biochem 1975; 59:573-80; PMID:128455; DOI:10.1111/j.1432-033.1975.tb02484.x.
3. Olsnes S., Fernandez-Puentes C., Carrasco L., Vazquez D. Ribosome inactivation by the toxic lectins abrin and ricin. Kinetics of the enzymic activity of the toxin A-chains. Eur J Biochem 1975; 60:281-8; PMID:1204642; DOI:10.1111/j.1432-033.1975.tb21001.x.
4. Olsnes S., Pihl A. Isolation and properties of abrin: a toxic protein inhibiting protein synthesis. Evidence for different biological functions of its two constituentpeptide chains. Eur J Biochem 1973; 35:179-85; PMID:4123356; DOI:10.1111/j.1432-033.1973.tb02823.x.
5. Sperti S., Montanaro L., Mattioli A., Stirpe F. Inhibition by ricin of protein synthesis in vitro: 60-S ribosomal subunit as the target of the toxin. Biochem J 1973; 136:813-815; PMID:4360718.
6. Evensen G., Mathiesen A., Sundan A. Direct molecular cloning and expression of two distinct abrin A-chains. J Biol Chem 1991; 266:6848-6852; PMID:2016300.
7. Wood K.A.L.J., Wawrzynczak E.J., Piatak M. Preproabrin: genomic cloning, characterization and the expression of the A-chain in Escherichia coli. Eur J Biochem 1991; 198:723-32; PMID:2050149; DOI:10.1111/j.1432-033.1991.tb16072.x.
8. Montfort W., Villafranca J.E., Monzingo A.F., Ernst S.R., Katzin B., Rutenber E., et al. The three-dimensional structure of ricin at 2.8 A. J Biol Chem 1987; 262:5398-5403; PMID:3558397.
9. Katzin B.J., Collins E.J., Robertus JD. Structure of ricin A-chain at 2.5 A. Proteins 1991; 10:251-9; PMID:1881881; DOI:10.1002/prot.340100309.
10. Chen J.K., Hung C.H., Liaw Y.C., Lin JY. Identification of amino acid residues of abrin-a A chain is essential for catalysis and reassociation with abrin-a B chain by site-directed mutagenesis. Protein Eng 1997; 10:827-33; PMID:9342148; DOI:10.1093/protein/10.7.827.
11. Hung C.H., Lee M.C., Chen J.K., Lin JY. Cloning and expression of three abrin A-chains and their mutants derived by site-specific mutagenesis in Escherichia coli. Eur J Biochem 1994; 219:83-7; PMID:8307038; DOI:10.1111/j.1432-033.1994.tb19917.x.
12. Griffiths G.D., Lindsay C.D., Allenby A.C., Bailey S.C., Scawin J.W., Rice P., et al. Protection against inhalation toxicity of ricin and abrin by immunisation. Hum Exp Toxicol 1995; 14:155-64; PMID:7779439; DOI:10.1177/096032719501400201.
13. Gao Y.L., Gao S., Kang L., Nie C., Wang JL. Expression of Hc fragment from Clostridium botulinum neurotoxin serotype B in Escherichia coli and its use as a good immunogen. Hum Vaccin 2010; 6:462-6; PMID:20519939; DOI:10.4161/hv.6.6.11709.
14. The Biological and Toxin Weapons Convention (BTWC) Procedural Report and Rolling Text 2001.
15. Stirpe F., Barbieri L., Battelli M.G., Soria M., Lappi DA. Ribosome-inactivating proteins from plants: present status and future prospects. Biotechnology (NY) 1992; 10:405-12; PMID:1368484; DOI:10.1038/nbt0492-405.
16. Smallshaw J.E., Firan A., Fulmer J.R., Ruback S.L., Ghetie V., Vitetta ES. A novel recombinant vaccine which protects mice against ricin intoxication. Vaccine 2002; 20:3422-7; PMID:12213413; DOI:10.1016/S0264-410X(02)00312-2.
17. Smallshaw J.E., Richardson J.A., Vitetta ES. RiVax, a recombinant ricin subunit vaccine, protects mice against ricin delivered by gavage or aerosol. Vaccine 2007; 25:7459-69; PMID:17875350; DOI:10.1016/j.vaccine.2007.08.018.
18. Vitetta E.S., Smallshaw J.E., Coleman E., Jafri H., Foster C., Munford R., et al. A pilot clinical trial of a recombinant ricin vaccine in normal humans. Proc Natl Acad Sci USA 2006; 103:2268-73; PMID:16461456; DOI:10.1073/pnas.0510893103.
19. Smallshaw J.E., Richardson J.A., Pincus S., Schindler J., Vitetta ES. Preclinical toxicity and efficacy testing of RiVax, a recombinant protein vaccine against ricin. Vaccine 2005; 23:4775-84; PMID:15961194; DOI:10.1016/j.vaccine.2005.04.037.
20. Surendranath K., Karande AA. A neutralizing antibody to the a chain of abrin inhibits abrin toxicity both in vitro and in vivo. Clin Vaccine Immunol 2008; 15:737-43; PMID:18353919; DOI:10.1128/CVI.00254-07.
21. Tahirov T.H., Lu T.H., Liaw Y.C., Chen Y.L., Lin JY. Crystal structure of abrin-a at 2.14 A. J Mol Biol 1995; 250:354-67; PMID:7608980; DOI:10.1006/jmbi.1995.0382.
22. Wang L.C., Kang L., Hu T.M., Wang JL. Abrin-a A chain expressed as soluble form in Escherichia coli from a PCR-synthesized gene is catalytically and functionally active. Biochimie 2004; 86:327-33; PMID:15194237; DOI:10.1016/j.biochi.2004.03.006.
23. Braman J., Papworth C., Greener A. Site-directed mutagenesis using double-stranded plasmid DNA templates. Methods Mol Biol 1996; 57:31-44; PMID:8849992.
24. In: Sambrook J FE, Maniatis T, Ed. Molecular cloning: a laboratory manual: Cold Spring Harbor Laboratory 1989.
25. Mosmann T. Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays. J Immunol Methods 1983; 65:55-63; PMID:6606682; DOI:10.1016/0022-1759(83)90303-4.