Expression of full length and deletion homologues of Carcinoscorpius rotundicauda Factor C in Saccharomyces cerevisiae: Immunoreactivity and endotoxin binding

Innate Immunity

Volumn 4, Issue 1, 1997, Pages 33-43

  Ding, J L ^a   Chai, C ^a   Pui, A W M ^a   Ho, B ^a  

^a NATIONAL UNIVERSITY OF SINGAPORE   (Singapore)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 79958095464     PISSN: 17534259     EISSN: 17534267     Source Type: Journal    
DOI: 10.1177/096805199700400105     Document Type: Article

References (26)

1. Levin J., Bang F.B. The role of endotoxin in the extracellular coagulation of Limulus blood. Bull Johns Hopkins Hosp 1964; 115:265-274.
2. Nakamura T., Morita T., Iwanaga S. Intracellular proclotting enzyme in Limulus (Tachypleus tridentatus) hemocytes: its purification and properties. J Biochem (Tokyo) 1985; 97: 1561-1574.
3. Ho B., Kim J.C., Ding J.L. Electrophoretic analysis of endotoxin-activated gelation reaction of Carcinoscorpius rotundicauda amoebocyte lysate. Biochem Mol Biol Int 1993; 29: 687-694.
4. Iwanaga S., Morita T., Miyata T., Nakamura T. Hemolymph coagulation system in Limulus. In: Lieve L.et al.(eds) Microbiology. Washington: American Society of Microbiology, 1985;21-24.
5. Nakamura T., Horiuchi T., Morita T., Iwanaga S. Purification and properties of intracellular clotting factor, Factor B from horseshoe crab (Tachypleus tridentatus) hemocytes. J Biochem (Tokyo) 1986a; 99: 847-857.
6. Tokunaga F., Miyata T., Nakamura T.et al.Lipopolysaccharide-sensitive serine protease zymogen (Factor C) in horseshoe crab hemocytes: identification and alignment of proteolytic fragments produced during the activation show that it is a novel type of serine protease. Eur J Biochem 1987; 167: 405-416.
7. Z Ding J.L., Navas III M.A.A., Ho B. Two forms of Factor C from the amoebocytes of Carcinoscorpius rotundicauda: purification and characterisation. Biochim Biophys Acta 1993; 1202: 149-156.
8. Nakamura T., Morita T., Iwanaga S. Lipopolysaccharide sensitive serine-protease zymogen (Factor C) found in Limulus hemocytes: isolation and characterization. Eur J Biochem 1986; 154:511-521.
9. Muta T., Miyata T., Misumi Y.et al.Limulus Factor C: an endotoxin sensitive serine protease zymogen with a mosaic structure of complement-like, epidermal growth factor-like and lectin-like domains. J Biol Chem 1991; 266: 6554-6561.
10. Ding J.L., Navas M.A.A., Ho B. Molecular cloning and sequence analysis of Factor C cDNA from the Singapore horseshoe crab, Carcinoscorpius rotundicauda. Mol Marine Biol Biotechnol 1995; 4: 90-103.
11. Hadfield C., Raina K.K., Shashi-Menon K., Mount R.C. The expression and performance of cloned genes in yeast. Mycol Res 1993; 8: 897-944.
12. Baldari C., Murray J.A.H., Ghiara P., Cesareni G., Galeotti C. L. A novel leader peptide which allows efficient secretion of a fragment of human interleukin 1β in Saccharomyces cerevisiae. EMBO J 1987; 6: 229-234.
13. Cesareni G., Murray J.A.H. Plasmid vectors carrying the replication origin of filamentous ss phages. In: Setlow J.K., Hollaender A. (eds) Genetic Engineering: Principles and Methods Vol. 9. New York: Plenum, 1987; 135-154.
14. Murray J.A.H., Scarpa M., Rossi N., Cesareni G. Antagonistic controls regulate copy number of the yeast 2μ plasmid. EMBO J 1987; 6: 4205-4212.
15. Roopashree S.D., Chai C., Ho B., Ding J.L. Expression of Carcinoscorpius rotundicauda Factor C CDNA. Biochem Mol Biol Int 1995; 35: 841-849.
16. Sambrook J., Fritsch E.F., Maniatis T. Molecular Cloning: A Laboratory Manual, 2nd edn. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory, 1989.
17. Schiestl R.H., Gietz R.D. High-efficiency transformation of intact yeast cells using single-stranded nucleic-acids as a carrier. Curr Genet 1989; 16: 339-346.
18. Treco D.A. In: Ausubel M., Brent R., Kingston R.E.et al.(eds) Current Protocols in Molecular Biology. Greene Publishing Associates and Wiley-Interscience 1989; 2: Unit 13.
19. Selden R.F. In: Ausubel M., Brent R., Kingston R.E.et al.(eds) Current Protocols in Molecular Biology. Greene Publishing Associates and Wiley-Interscience 1987; 1: Unit 4.
20. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970; 227: 680-684.
21. Struhl K. Promoters, activator proteins, and the mechanism of transcriptional initiation in yeast. Cell 1987; 49: 295-297.
22. Baim S.B., Sherman F. mRNA structures influencing translation in the yeast Saccharomyces cerevisiae. Mol Cell Biol 1988; 8: 1591-1601.
23. Clements J.M., Laz T.M., Sherman F. Efficiency of translation initiation by non-AUG codons in Saccharomyces cerevisiae. Mol Cell Biol 1988; 8: 4533-4536.
24. Kozak M. Bifunctional messenger RNAs in eukaryotes. Cell 1986; 44: 283-292.
25. Cigan A.M., Pabich E.K., Donahue T.F. Mutational analysis of the HIS4 translational initiator region in Saccharomyces cerevisiae. Mol Cell Biol 1988; 8: 2964-2975.
26. Miura Y., Tokunaga F., Miyata T., Moriasu M., Yoshikawa K., Iwanaga S. Preparation and properties of monoclonal antibodies against lipopolysaccharide-sensitive serine protease zymogen, Factor C from the horseshoe crab (Tachypleus tridentatus) hemocytes. J Biochem 1992; 112: 476-481.