N-linked glycan structures of mouse interferon-β produced by Bombyx mori larvae

Misaki, Ryo; Nagaya, Hidekazu; Fujiyama, Kazuhito; Yanagihara, Itaru; Honda, Takeshi; Seki, Tatsuji

doi:10.1016/j.bbrc.2003.10.094

Cited by 27 publications

(11 citation statements)

References 32 publications

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“…It should also be examined whether the structural characteristics of the recombinant GTH affect its biological potency compared with native GTH. Native GTH is a heterodimeric glycoprotein with sialic acid but our recombinant GTH is a single-chain glycoprotein with mannose [26,27]. Studies on these matters are now in progress.…”

Section: Discussionmentioning

confidence: 99%

Induction of spermatogenesis in Japanese eel by recombinant goldfish gonadotropins

Hayakawa¹,

Nagaya

Kaki

et al. 2008

Fish Sci

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We previously demonstrated the biological activities of single-chain recombinant gonadotropins (scGTHs) of goldfish Carrassius auratus follicle-stimulating hormone (scFSH) and luteinizing hormone (scLH), produced by a baculovirus-silkworm larvae system, by using in vivo bioassays with some fishes including Japanese eel Anguilla japonica. Among the bioassays, we succeeded in induction of spermatogenesis of sexually immature male Japanese eels by both scFSH and scLH, especially resulting in the occurrence of spermatozoa in scLH-administered males. However, those recombinant hormones did not induce enlargement of testes. In order to further confirm the potency of recombinant GTHs for use in aquaculture species, we administered scFSH and scLH to males of Japanese eel at higher dosage and frequency (eight times with 2-5 days interval) than those of the previous study (five or six times with 7 days intervals), including combination of scFSH and scLH administration (scFSH-scLH). Gonadosomatic indices (GSI) of scLH-and scFSH-scLH-administered males were larger than those of initial control males and of control males that were injected with saline. Enlargement of testes was also confirmed by measurement of testicular lobe size in scFSH-, scLH-, and scFSH-scLH-administered males. By histological observation, occurrence of spermatozoa was confirmed in scLH-and scFSH-scLH-administered eels. Although milt production was not induced, higher dosage and frequency of scGTH administration was effective in promoting testicular development of immature eels. Thus, single-chain fish GTHs produced by the baculovirus-silkworm larvae system could be a useful tool for promotion of gonadal maturation in aquaculture fishes.

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Section: Discussionmentioning

confidence: 99%

Induction of spermatogenesis in Japanese eel by recombinant goldfish gonadotropins

Hayakawa¹,

Nagaya

Kaki

et al. 2008

Fish Sci

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“…These patterns contained fucose ␣1,6-linked to the innermost GlcNAc residue. Misaki et al (2003) reported the presence of Man␣1-6Man␤1-4GlcNAc␤1-4GlcNAc (6.4%) and Man␣1-6(Man␣1-3)Man␤1-4GlcNAc␤1-4(Fuc␣1-6) GlcNAc (1.1%) in N-linked glycan structures of mouse interferon-␤ produced by B. mori larvae. Man␣1-6(Man␣1-3)Man␤1-4GlcNAc␤1-4(Fuc␣1-6)GlcNAc may be derived from GlcNAcMan 5 GlcNAc 2 through mannosidase-mediated excision of ␣-linked mannosyl residues, followed by GlcNAcase-mediated deletion of a ␤-1,2-linked terminal GlcNAc residue (Watanabe et al, 2002).…”

Section: Discussionmentioning

confidence: 98%

Human IgG1 expression in silkworm larval hemolymph using BmNPV bacmids and its N-linked glycan structure

Park

Ishikiriyama

Nishina

et al. 2009

Journal of Biotechnology

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A Bombyx mori nucleopolyhedrovirus (BmNPV) bacmid expressing heavy and light chains of human 29IJ6 IgG was constructed and used to secrete recombinant antibody into silkworm larval hemolymph. Fifth instar silkworm larvae were reared and injected into the dorsum of the larvae with recombinant cysteine protease- and chitinase-deficient BmNPV (BmNPV-CP(-)-Chi(-)) bacmid/29IJ6 IgG and harvested after approximately 6 days. The total yield of recombinant 29IJ6 IgG was 36 microg/larvae, which is equivalent to 8 mg/kg of larvae. The recombinant antibody was purified to homogeneity using a HiTrap rProtein A FF column with a purification yield of 83.1%. The purified protein was identified by Western blot and ELISA experiments. The N-linked glycan structure of the purified protein was determined by the HPLC mapping method. The N-glycans of the 29IJ6 IgG glycoprotein produced in, and secreted by the silkworm larvae were composed exclusively of two kinds of paucimannose-type oligosaccharides, Manalpha1-6Manbeta1-4GlcNAcbeta1-4(Fucalpha1-6)GlcNAc and Manalpha1-6(Manalpha1-3)Manbeta1-4GlcNAcbeta1-4(Fucalpha1-6)GlcNAc.

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“…These data suggest that the N-glycans of rFeIFN-ω had a typical insect-type profile, with FM2 (Man2GlcNAc2Fuc) thought to be a main N-glycan [14]. The N-glycan structures of recombinant mouse IFN-β produced by the baculovirus expression system were reported to consist of 20% high-mannose-type (more than M6), 51% paucimannose-type, and 12% core α 1,3-fucosylated glycans [29]. Thus, the N-glycan pattern of rFeIFN-α15 synthesised in silk glands in this study differed from those of previously reported rIFNs synthesised in the baculovirus expression system, in which recombinant proteins were expressed in baculovirus-infected organs, such as fat bodies or haemolymph except silk glands.…”

Section: Discussionmentioning

confidence: 99%

Novel recombinant feline interferon carrying N-glycans with reduced allergy risk produced by a transgenic silkworm system

et al. 2018

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BackgroundThe 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.ResultsA 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.ConclusionsThe 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.

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N-linked glycan structures of mouse interferon-β produced by Bombyx mori larvae

Cited by 27 publications

References 32 publications

Induction of spermatogenesis in Japanese eel by recombinant goldfish gonadotropins

Induction of spermatogenesis in Japanese eel by recombinant goldfish gonadotropins

Human IgG1 expression in silkworm larval hemolymph using BmNPV bacmids and its N-linked glycan structure

Novel recombinant feline interferon carrying N-glycans with reduced allergy risk produced by a transgenic silkworm system

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