Abstract：
:Human papillomaviruses (HPVs) are responsible for the most common human sexually transmitted viral infections. Infection with high-risk HPVs, particularly HPV16, is associated with the development of cervical cancer. The papillomavirus L1 major capsid protein, the basis of the currently marketed vaccines, self-assembles into virus-like particles (VLPs). Here, we describe the expression, purification and characterization of recombinant HPV16 L1 produced by a methylotrophic yeast. A codon-optimized HPV16 L1 gene was cloned into a non-integrative expression vector under the regulation of a methanol-inducible promoter and used to transform competent Pichia pastoris cells. Purification of L1 protein from yeast extracts was performed using heparin-sepharose chromatography, followed by a disassembly/reassembly step. VLPs could be assembled from the purified L1 protein, as demonstrated by electron microscopy. The display of conformational epitopes on the VLPs surface was confirmed by hemagglutination and hemagglutination inhibition assays and by immuno-electron microscopy. This study has implications for the development of an alternative platform for the production of a papillomavirus vaccine that could be provided by public health programs, especially in resource-poor areas, where there is a great demand for low-cost vaccines.
journal_name
Arch Viroljournal_title
Archives of virologyauthors
Bazan SB,de Alencar Muniz Chaves A,Aires KA,Cianciarullo AM,Garcea RL,Ho PLdoi
10.1007/s00705-009-0484-8subject
Has Abstractpub_date
2009-01-01 00:00:00pages
1609-17issue
10eissn
0304-8608issn
1432-8798journal_volume
154pub_type
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journal_title：Archives of virology
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journal_title：Archives of virology
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