Background: To obtain human papillomavirus type 16(HPV 16) major capsid protein L1 with baculovirus expression system.
Methods: Using pFb1 as a vector,a recombinant baculovirus expressing plasmid,which contains HPV16L1 gene sequence,was generated. The constructed virus was infected into an insect cell line Sf9.
Results: After incubating at 27 degrees for 72 hours, the infected cells were collected and total cellular poteins were extracted. SDS-PAGE assay revealed a roughly 56 000 expressed protein and Western blot confirmed that the expressed protein arose from HPV16L1.
Conclusions: HPV16 later protein L1 could be efficiently expressed with baculovirus expression system,and the expressed L1 protein remains to have good immunoreactivity. This study may supply a basic work for preparing virus-like particle and prophylactic HPV subunit vaccines.
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Biotechnol Bioeng
January 2025
Instituto de Biologia Experimental e Tecnológica (iBET), Oeiras, Portugal.
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ICAR-Indian Veterinary Research Institute, Bangalore, Karnataka 560024, India.
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Guangdong Laboratory for Lingnan Modern Agriculture, Guangdong Provincial Key Laboratory of Agro-animal Genomics and Molecular Breeding, College of Animal Science, South China Agricultural University, Guangzhou 510642, China; Guangdong Provincial Sericulture and Mulberry Engineering Research Center, College of Animal Science, South China Agricultural University, Guangzhou 510642, China. Electronic address:
Baculovirus causes lethal nuclear polyhedrosis in insects, whereas its regulatory mechanism on host transcription has not been fully illustrated. Herein, Bombyx mori nucleopolyhedrovirus (BmNPV) infection caused dephosphorylation and thus cytoplasmic-nucleo translocation of transcription factor EB (BmTFEB) by inhibiting Mechanistic target of rapamycin complex 1 (MTORC1), while upregulating Adenosine monophosphate-activated protein kinase (AMPK) signaling to promote self-proliferation through the rival protein kinase 1 in Bombyx mori. Significantly, B.
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Recombinant macromolecular complexes are often produced by the baculovirus system, using multigene expression vectors. Yet, the construction of baculovirus-compatible multigene expression vectors is complicated and time-consuming. Furthermore, while the baculovirus and yeast are popular protein expression systems, no single method for multigene vector construction is compatible with both.
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