Cited by 65Viral Infections and Immunology ResearchPoxvirus research and outbreaksVirology and Viral Diseases

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Coinfection with recombinant vaccinia viruses expressing poliovirus P1 and P3 proteins results in polyprotein processing and formation of empty capsid structures

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Ansardi, D C, Porter, D C, Morrow, C D·1991·Journal of Virology

DOI 10.1128/jvi.65.4.2088-2092.1991PMC PMC240068

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Abstract

The assembly process of poliovirus occurs via an ordered proteolytic processing of the capsid precursor protein, P1, by the virus-encoded proteinase 3CD. To further delineate this process, we have isolated a recombinant vaccinia virus which expresses, upon infection, the poliovirus P1 capsid precursor polyprotein with an authentic carboxy terminus. Coinfection of HeLa cells with the P1-expressing vaccinia virus and with a second recombinant vaccinia virus which expresses the poliovirus proteinase 3CD resulted in the correct processing of P1 to yield the three individual capsid proteins VP0, VP3, and VP1. When extracts from coinfected cells were fractionated on sucrose density gradients, the VP0, VP3, and VP1 capsid proteins were immunoprecipitated with type 1 poliovirus antisera from fractions corresponding to a sedimentation consistent for poliovirus 75S procapsids. Examination of these fractions by electron microscopy revealed structures which lacked electron-dense cores and which corresponded in size and shape to those expected for poliovirus empty capsids. We conclude that the expression of the two poliovirus proteins P1 and 3CD in coinfected cells is sufficient for the correct processing of the capsid precursor to VP0, VP3, and VP1 as well as for the assembly of poliovirus empty capsid-like structures.

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Authors: Ansardi, D. C., Porter, D. C., & Morrow, C. D.
Affiliations: University of Alabama at Birmingham (US)
ORCID: Porter, D C
Morrow, C D
Venue: Journal of Virology
Publisher: American Society for Microbiology
Published: 1991-04
Volume: 65
Issue: 4
Pages: 2088-2092
ISSN: 0022-538X (ISSN-L)
1098-5514
DOI: 10.1128/jvi.65.4.2088-2092.1991
PMC: PMC240068
OpenAlex: W1535818125
Cited by: 64
References: 28
Citations by year: 2026: 1 · 2025: 2 · 2024: 3 · 2023: 1 · 2022: 3 · 2021: 1 · 2020: 2 · 2019: 1 · 2018: 1 · 2016: 1 · 2015: 2 · 2014: 3 · 2013: 1
FWCI: 4.75
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: journals.asm.org/non-commercial-tdm-license (tdm)
Locations: Journal of Virology (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health
National Institute of Allergy and Infectious Diseases (AI 07150, AI-25005, T32AI007150)
Topics: Health Sciences › Medicine › Infectious Diseases › Viral Infections and Immunology Research
Life Sciences › Immunology and Microbiology › Virology › Poxvirus research and outbreaks
Health Sciences › Medicine › Epidemiology › Virology and Viral Diseases
Keywords: poliovirus, co-infection, recombinant vaccinia virus, polyprotein processing, empty capsids, capsid assembly, VP0, VP3, VP1, HeLa cells
MeSH terms: 3C Viral Proteases, Base Sequence, Capsid, Cloning, Molecular, Cysteine Endopeptidases, DNA, Viral, Genes, Viral, HeLa Cells, Humans, Molecular Sequence Data, Poliomyelitis, Protein Processing, Post-Translational, Recombination, Genetic, Vaccinia virus, Viral Proteins, Gene Expression, Poliovirus, Capsid Proteins

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Coinfection with recombinant vaccinia viruses expressing poliovirus P1 and P3 proteins results in polyprotein processing and formation of empty capsid structures

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