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Novel recombinant feline interferon carrying N-glycans with reduced allergy risk produced by a transgenic silkworm system
- Source :
- BMC Veterinary Research, Vol 14, Iss 1, Pp 1-9 (2018), BMC Veterinary Research
- Publication Year :
- 2018
- Publisher :
- BMC, 2018.
-
Abstract
- Background The generation of recombinant proteins for commercialisation must be cost-effective. Despite the cost-effective production of recombinant feline interferon (rFeIFN) by a baculovirus expression system, this rFeIFN carries insect-type N-glycans, with core α 1,3 fucosyl residues that act as potential allergens. An alternative method of production may yield recombinant glycoproteins with reduced antigenicity. Results A cDNA clone encoding the fifteenth subtype of FeIFN-α (FeIFN-α15) was isolated from a Japanese domestic cat. This clone encoded a protein of 189 amino acids with a molecular mass of 21.1 kDa. The rFeIFN-α15 was expressed using a transgenic silkworm system, which was expected to yield an N-glycan structure with reduced antigenicity compared with the protein produced by the baculovirus system. The resulting rFeIFN-α15 accumulated in the sericin layer of silk fibres and was easily extracted and purified by column chromatography. The N-terminal amino acid sequence of purified rFeIFN-α15 was identical to the mature form of natural sequence. Moreover, its N-glycans did not include detectable core α 1,3 fucosyl residues. Its anti-vesicular stomatitis virus activity (2.6 × 108 units/mg protein) was comparable to that of the baculovirus-expressed rFeIFN. Conclusions The lower allergy risk of rFeIFN produced by the transgenic silkworm system than by the baculovirus expression system is due to the former lacking core α 1,3 fucosyl residues in its N-glycans. The rFeIFN-α15 produced by the transgenic silkworm system may be a prospective candidate for the next generation of rFeIFN in veterinary medicine.
- Subjects :
- 0301 basic medicine
Antigenicity
Silk
Fucose
Transgenic
law.invention
Animals, Genetically Modified
03 medical and health sciences
chemistry.chemical_compound
Polysaccharides
Bombyx mori
law
Complementary DNA
Silkworm
Animals
Amino Acid Sequence
Peptide sequence
Core α 1,3 fucosyl residues
chemistry.chemical_classification
lcsh:Veterinary medicine
030102 biochemistry & molecular biology
General Veterinary
biology
General Medicine
Bombyx
biology.organism_classification
Recombinant Proteins
Amino acid
Feline interferon
030104 developmental biology
Biochemistry
chemistry
N-glycan
Cats
Recombinant DNA
lcsh:SF600-1100
Interferons
Glycoprotein
Research Article
Subjects
Details
- Language :
- English
- ISSN :
- 17466148
- Volume :
- 14
- Issue :
- 1
- Database :
- OpenAIRE
- Journal :
- BMC Veterinary Research
- Accession number :
- edsair.doi.dedup.....a3f7770f6404caf1996d4c809637356d