Expression of vaccinia recombinant HPV 16 L1 and L2 ORF proteins in epithelial cells is sufficient for assembly of HPV virion-like particles

Zhou, Jiang; Sun, Xueying; Stenzel, Deborah; Frazer, Ian H.

doi:10.1016/0042-6822(91)90772-4

Cited by 468 publications

(253 citation statements)

References 31 publications

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“…L2 is required for infectivity and required for egress of viral genomes from endosomes, while L1 does not appear to exit the endosomal compartment [12,13]. Following endosomal escape, L2 accompanies the viral DNA to the nucleus.…”

Section: Viral Entry In the Basal Cellsmentioning

confidence: 99%

“…L1 is the major capsid protein of HPV, forming 72 pentamers of five L1 molecules in addition to one L2 molecule. L1 has the capacity to self-assemble into virus-like particles (VLPs) when expressed as a eukaryotic recombinant protein [12,31], which is used in the production of prophylactic HPV vaccines. L2 is needed for capsidation of HPV DNA, because L2 protein but not L1 protein, can bind HPV DNA.…”

Section: Hpv Particles and Their Releasementioning

confidence: 99%

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Biology of Human Papillomavirus Infections in Head and Neck Carcinogenesis

Rautava

Syrjänen

2012

Head and Neck Pathol

127

135

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Section: Viral Entry In the Basal Cellsmentioning

confidence: 99%

Section: Hpv Particles and Their Releasementioning

confidence: 99%

Biology of Human Papillomavirus Infections in Head and Neck Carcinogenesis

Rautava

Syrjänen

2012

Head and Neck Pathol

127

135

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“…We and others have recently succeeded in producing empty virus-like particles (VLP) of various papillomavirus types by synthesizing the L1 protein alone or in combination with the L2 protein, using vaccinia virus (Zhou et al, 1991 ;Hagensee et al, 1993) or baculovirus recombinants (Rose et al, 1993;Kirnbauer et al, 1992;Volpers et al, 1994). Both spherical particles of 50-60 nm diameter and tubular structures of 25-30nm and 50-60 nm diameter of numerous lengths have been obtained.…”

mentioning

confidence: 99%

Organization of the major and minor capsid proteins in human papillomavirus type 33 virus-like particles

Sapp¹,

Volpers²,

Müller

et al. 1995

Journal of General Virology

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The organization of the major (L1) and minor (L2) proteins in the human papillomavirus capsid is still largely unknown. In this study we analysed the disulphide bonding between L1 proteins and the association of L2 proteins with capsomers using virus-like particles obtained in insect cells by co-expression of the L1 and L2 genes of human papillomavirus type 33. About 50% of the L1 protein molecules in these particles (1.29 g/cm z) formed disulphide-bonded trimers. Reduction of the intermolecular disulphide bonds by dithiothreitol (DTT) treatment caused disassembly of virus-like particles into capsomers. This indicates that disulphide bonds between capsomers at the threefold symmetry positions of the capsid are essential for the assembly of the papiUomavirus capsid. In contrast, the L2 protein was not engaged in intermolecular disulphide bonding. The L2 protein remained associated with capsomers on disassembly by treatment with DTT. When the disassembly was carried out in 0"65 u-NaC1, complete L2 protein molecules bound preferentially to capsomer oligomers, whereas truncated L2 protein molecules bound only to monomers. In 0.15 u-NaCl only complete L2 protein molecules remained bound to capsomers. This indicates that different regions of the L2 protein molecule are differentially involved in the association of the papillomavirus capsid.Papillomaviruses are a subfamily of the papovaviruses. The properties shared by these viruses include a circular dsDNA genome, a nonenveloped virion and an icosahedral capsid. Papillomaviruses have a specific tropism for epithelial cells and have been found in a great variety of species. More than 70 types of human papillomavirus (HPV) have been recognized but only a few, e.g. HPV-I (which induces cutaneous warts), can be isolated as virus particles. The other HPVs, e.g. HPV-16 or HPV-33 (which are associated with genital carcinoma), have only been identified by cloning their genomes from epithelial lesions. Moreover, no system exists for the efficient propagation of HPVs in vitro.

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“…VLP of Papillomaviruses are formed from the over expression of the major capsid protein L1. [10][11][12] These particles are highly immunogenic and are able to stimulate both humoral and cell mediated immune responses. [13][14][15] Human Papillomavirus (HPV) is the leading cause of cervical cancer.…”

Section: Vlps Produced For Structurally Simple Non-enveloped Virusesmentioning

confidence: 99%

Virus‑like particles as a vaccine delivery system: Myths and facts

Roy¹,

Noad²

2008

Human Vaccines

151

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Vaccines against viral disease have traditionally relied on attenuated virus strains or inactivation of infectious virus. Subunit vaccines based on viral proteins expressed in heterologous systems have been effective for some pathogens, but have often suffered from poor immunogenicity due to incorrect protein folding or modification. In this review we focus on a specific class of viral subunit vaccine that mimics the overall structure of virus particles and thus preserves the native antigenic conformation of the immunogenic proteins. These virus-like particles (VLPs) have been produced for a wide range of taxonomically and structurally distinct viruses, and have unique advantages in terms of safety and immunogenicity over previous approaches. With new VLP vaccines for papillomavirus beginning to reach the marketplace we argue that this technology has now 'come-of-age' and must be considered a viable vaccine strategy.

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Expression of vaccinia recombinant HPV 16 L1 and L2 ORF proteins in epithelial cells is sufficient for assembly of HPV virion-like particles

Cited by 468 publications

References 31 publications

Biology of Human Papillomavirus Infections in Head and Neck Carcinogenesis

Biology of Human Papillomavirus Infections in Head and Neck Carcinogenesis

Organization of the major and minor capsid proteins in human papillomavirus type 33 virus-like particles

Virus‑like particles as a vaccine delivery system: Myths and facts

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