Recombinant baculoviruses expressing

Assenga, S.P, You, M., Shy, C.H. et al. (2006) The use of a recombinant baculovirus expressing a chitinase from the hard tick Haemaphysalis longicornis and its potential application as a bioacaricide for tick control. Parasitology Research, 98 (2), 111-118. 

Kitts, R A. and Possee, R. D. (1993). A method for producing recombinant baculovirus expression vectors at high frequency. Biotechniques 14,810-817. 

Hota-Mitchell, S., Siddiqui, A.A., Dekaban, C.A., Smith, J., Tognon, C. and Podesta, R.B. (1997) Protection against Schistosoma mansoni infection with a recombinant baculovirus-expressed subunit of calpain. Vaccine 15, 1631-1640. 

French TJ, Roy P (1990), Synthesis of bluetongue virus (BTV) core-like particles by a recombinant baculovirus expressing the two major structural core proteins of BTV, J. Virol. 64 1530-1536. 

Recombinant Baculovirus Expressing an Insect-Selective Neurotoxin... 

Recombinant Baculoviruses Expressing Insect Toxins. The first attempt to modify a NPV for increased insecticidal activity was conducted by Carbonell et al 33) in which an insect-specific toxin (BelT) from the scorpion Buthus eupus was incorporated into the AcNPV genome. Although low levels of toxin expression were confirmed, the recombinant NPV did not result in quicker killing rates of host insects. Failure to improve killing activity may be due to an insufficient level of toxin expression by AcNPV, an incorrect sequence of toxin DNA, and/or insufficient or incorrect folding of the toxin following expression. 

It is well documented that certain arthropods produce neurotoxins, which are highly specific for insects. We selected the insect-selective neurotoxin, AalT, for expression in AcNPV primarily because AalT was the most thoroughly characterized of the insect-selective toxins isolated to date. This resource of information was instrumental in augmenting our toxicological characterization of the recombinant baculovirus expressing AalT. 

Insect Control by Use of Recombinant Baculoviruses Expressing JuvenUe Hormone... 

Table m. Bioassay Data for Recombinant Baculoviruses Expressing JHE... 

The plethora of literature that deals with hormonal regulation of insect development gives some indication of the complexities involved. The role of JHE varies between species during the early larval instars, and the reduced sensitivity of tissues to anti-JH effects via JHE in later instars (54) may well be limiting the insecticidal efficacy of the recombinant baculoviruses expressing JHE. 

Bryant Yes, although we didn t use purified IDGF, but recombinant IDGF produced from a baculovirus expression system. These are clone 8 cells from an imaginal disc we haven t tried growing the whole imaginal disc. 

Zhang, F., Saarinen, M.A., Itle, L.J. et al. (2002) The effect of dissolved oxygen (DO) concentration on the glycosylation of recombinant protein produced by the insect cell-baculovirus expression system. Biotechnology and Bioengineering, 11 (2), 219-224. 

Insect cells in culture are also hosts for recombinant protein production. Production of recombinant proteins in the baculovirus expression vector system is the most common system. Titers of recombinant protein as high as 11 g/L have been obtained. 

Baculovirus expression is the most frequently used method for expression in insect cells and employs Autographa californica nuclear polyhedrosis virus (AcNPV), a double stranded (ds) DNA virus that infects arthropods. The baculovirus expression system utilizes features of the viral life cycle to introduce recombinant DNA coding the gene of interest into insect cells (Miller, 1988 O Reilly et al, 1992). 

Paul A. K., Martin D. A., and Robert D. P. (1990) Linearization of baculovirus DNA enhances the recovery of recombinant virus expression vectors. Nucleic Acids Kes. 18, 5667-5672. 

Jayakumar A, Kang Y, Mitsudo K, et al. Expression of LEKTI domains 6-9 in the baculovirus expression system Recombinant LEKTI domains 6-9 inhibit trypsin and subtilisin A. Protein Expr Purif 2004 35 93-101. 

Detailed structure-function analysis of a-LTX is impossible without generating mutants. The difficulty inherent to this approach is to ensure proper folding of this large protein. Two groups relied on baculovirus expression and successfully purified active recombinant toxins. Ichtchenko et al. (1998) used two 8-histidine tags for purification, whereas Volynski et al. (1999, 2003) utilized a monoclonal antibody. 

Germann UA, Willingham MC, Pastan I, et al. Expression of the human multidrug transporter in insect cells by a recombinant baculovirus. Biochemistry 1990 29 (9) 2295-2303. 

Condreay JP, Witherspoon SM, Clay WC, Kost TA (1999), Transient and stable gene expression in mammalian cells transduced with a recombinant baculovirus vector, Proc. Natl Acad. Sci. USA 96 127-132. 

Kulakosky PC, Shuler ML, Wood HA (1998), N-Glycosylation of a baculovirus-expressed recombinant glycoprotein in three insect cell lines, In Vitro Cell. Dev. Biol. 34 101-108. 

The values of qp can vary significantly as a function of the expression system used and of the recombinant protein product. In general, values in the range of 1 —30 pg cell-1 day-1 are reported for stably transfected cell lines. However, Chico and Jager (2000) have reported values as high as 85 pg cell-1 day-1 for the expression of a protein using the insect cell-baculovirus expression vector system. This value approaches the maximum theoretical value that is expected for animal cells, which is 100 pg cell-1 day-1 (Ozturk, 1990). 

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