In Vitro Assembly of Virus-Like Particles of a Gammaretrovirus, the Murine Leukemia Virus XMRV

Hadravová, Romana; de Marco, Alex; Ulbrich, Pavel; Štokrová, Jitka; Doležal, Michal; Pichová, Iva; Ruml, Tomáš; Briggs, John A. G.; Rumlová, Michaela

doi:10.1128/jvi.05564-11

Cited by 27T-cell and Retrovirus StudiesHIV Research and TreatmentVirus-based gene therapy research

In Vitro Assembly of Virus-Like Particles of a Gammaretrovirus, the Murine Leukemia Virus XMRV

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Hadravová, Romana, de Marco, Alex, Ulbrich, Pavel, Štokrová, Jitka, Doležal, Michal, Pichová, Iva, Ruml, Tomáš, Briggs, John A. G. +1 more·2012·Journal of Virology

DOI 10.1128/jvi.05564-11PMC PMC3264384

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Abstract

Immature retroviral particles are assembled by self-association of the structural polyprotein precursor Gag. During maturation the Gag polyprotein is proteolytically cleaved, yielding mature structural proteins, matrix (MA), capsid (CA), and nucleocapsid (NC), that reassemble into a mature viral particle. Proteolytic cleavage causes the N terminus of CA to fold back to form a β-hairpin, anchored by an internal salt bridge between the N-terminal proline and the inner aspartate. Using an in vitro assembly system of capsid-nucleocapsid protein (CANC), we studied the formation of virus-like particles (VLP) of a gammaretrovirus, the xenotropic murine leukemia virus (MLV)-related virus (XMRV). We show here that, unlike other retroviruses, XMRV CA and CANC do not assemble tubular particles characteristic of mature assembly. The prevention of β-hairpin formation by the deletion of either the N-terminal proline or 10 initial amino acids enabled the assembly of ΔProCANC or Δ10CANC into immature-like spherical particles. Detailed three-dimensional (3D) structural analysis of these particles revealed that below a disordered N-terminal CA layer, the C terminus of CA assembles a typical immature lattice, which is linked by rod-like densities with the RNP.

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Although previous low-resolution structures showed a similar immature lattice spacing of 80 A and suggested a conserved CA-NTD arrangement, the arrangement of the CA-NTD domains was different in all three viruses when observed at higher resolution.
“Unexpectedly, although previous low-resolution structures had showed a similar immature lattice spacing of 80 A ˚ and suggested a conserved CA-NTD arrangement [33,34], the arrangement of the CA-NTD domains was in fact different in all three viruses when observed at higher-resolution.”
From Retrovirus maturation-an extraordinary structural transformation (2016) · cites this paper as [34]

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Authors: Hadravová, R., de Marco, A., Ulbrich, P., Štokrová, J., Doležal, M., Pichová, I., Ruml, T., Briggs, J. A. G., & Rumlová, M.
Affiliations: Czech Academy of Sciences (CZ)
Structural and Computational Unit, European Molecular Biology Laboratory, Heidelberg, Germany
University of Chemistry and Technology, Prague (CZ)
European Molecular Biology Laboratory (DE)
ORCID: Hadravová, Romana
Ulbrich, Pavel
Doležal, Michal
Pichová, Iva
Ruml, Tomáš
Briggs, John A. G.
Rumlová, Michaela
Venue: Journal of Virology
Publisher: American Society for Microbiology
Published: 2012-02
Volume: 86
Issue: 3
Pages: 1297-1306
ISSN: 0022-538X (ISSN-L)
1098-5514
DOI: 10.1128/jvi.05564-11
PMC: PMC3264384
OpenAlex: W2106298056
Cited by: 26
References: 68
Citations by year: 2026: 1 · 2024: 1 · 2021: 1 · 2020: 1 · 2019: 1 · 2018: 4 · 2017: 2 · 2016: 5 · 2015: 3 · 2014: 3 · 2013: 2 · 2012: 2
FWCI: 0.99
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: journals.asm.org/non-commercial-tdm-license (tdm)
Locations: Journal of Virology (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
ASEP (submittedVersion, public-domain)
Funders: Deutsche Forschungsgemeinschaft
Grantová Agentura České Republiky
National Institutes of Health
National Cancer Institute (R37CA027834, R01CA027834, CA27834)
Topics: Life Sciences › Immunology and Microbiology › Immunology › T-cell and Retrovirus Studies
Life Sciences › Immunology and Microbiology › Virology › HIV Research and Treatment
Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Virus-based gene therapy research
Keywords: XMRV, gammaretrovirus, virus-like particle assembly, capsid protein, beta-hairpin formation, N-terminal proline, Gag protein, in vitro assembly, three-dimensional structure
MeSH terms: Amino Acid Sequence, Base Sequence, Escherichia coli, Fourier Analysis, Molecular Sequence Data, Leukemia Virus, Murine, Viral Proteins, Virion, Polymerase Chain Reaction, Sequence Homology, Amino Acid, DNA Primers, Virus Assembly, Cryoelectron Microscopy, Microscopy, Electron, Transmission, Proteolysis

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In Vitro Assembly of Virus-Like Particles of a Gammaretrovirus, the Murine Leukemia Virus XMRV

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