ArticleJournal of molecular biology2011
A retroviral chimeric capsid protein reveals the role of the N-terminal β-hairpin in mature core assembly.
Article in Journal of molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 33 citations in OpenAlex.
- Article
- Virus specificity and nucleoporin requirements for MX2 activity are affected by GTPase function and capsid-CypA interactions.PLoS pathogens · 2024Article
- Fluorescence, Circular Dichroism and Mass Spectrometry as Tools to Study Virus Structure.Sub-cellular biochemistry · 2024Review
- Virus specificity and nucleoporin requirements for MX2 activity are affected by GTPase function and capsid-CypA interactions.bioRxiv : the preprint server for biology · 2023Article
- A cell-free antigen processing system informs HIV-1 epitope selection and vaccine design.The Journal of experimental medicine · 2023Article
- Changes in dynamic and static structures of the HIV-1 p24 capsid protein N-domain caused by amino-acid substitution are associated with its viral viability.Protein science : a publication of the Protein Society · 2021Article
- Article
- Maturation of retroviruses.Current opinion in virology · 2019Review
- Nuclear pore heterogeneity influences HIV-1 infection and the antiviral activity of MX2.eLife · 2018Article
- Article
- In vitro assembly of the Rous Sarcoma Virus capsid protein into hexamer tubes at physiological temperature.Scientific reports · 2017Article
- Comparison of Biochemical Properties of HIV-1 and HIV-2 Capsid Proteins.Frontiers in microbiology · 2017Article
- Integrated analysis of residue coevolution and protein structures capture key protein sectors in HIV-1 proteins.PloS one · 2015Article
- Assessment of differences in the conformational flexibility of hepatitis B virus core-antigen and e-antigen by hydrogen deuterium exchange-mass spectrometry.Protein science : a publication of the Protein Society · 2014Article
- Second site reversion of a mutation near the amino terminus of the HIV-1 capsid protein.Virology · 2013Article
- Epitope-distal effects accompany the binding of two distinct antibodies to hepatitis B virus capsids.Journal of the American Chemical Society · 2013Article
- The maturational refolding of the β-hairpin motif of equine infectious anemia virus capsid protein extends its helix α1 at capsid assembly locus.The Journal of biological chemistry · 2013Article
- Biophysical characterization of the feline immunodeficiency virus p24 capsid protein conformation and in vitro capsid assembly.PloS one · 2013Article
- Interaction of the HIV-1 intasome with transportin 3 protein (TNPO3 or TRN-SR2).The Journal of biological chemistry · 2012Article
- Value of MR contrast media in image-guided body interventions.World journal of radiology · 2012Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 2 countries.
Funding
Abstract
The human immunodeficiency virus (HIV) is an enveloped virus constituted by two monomeric RNA molecules that encode for 15 proteins. Among these are the structural proteins that are translated as the gag polyprotein. In order to become infectious, HIV must undergo a maturation process mediated by the proteolytic cleavage of gag to give rise to the isolated structural protein matrix, capsid (CA), nucleocapsid as well as p6 and spacer peptides 1 and 2. Upon maturation, the 13 N-terminal residues from CA fold into a β-hairpin, which is stabilized mainly by a salt bridge between Pro1 and Asp51. Previous reports have shown that non-formation of the salt bridge, which potentially disrupts proper β-hairpin arrangement, generates noninfectious virus or aberrant cores. To date, however, there is no consensus on the role of the β-hairpin. In order to shed light in this subject, we have generated mutations in the hairpin region to examine what features would be crucial for the β-hairpin's role in retroviral mature core formation. These features include the importance of the proline at the N-terminus, the amino acid sequence, and the physical structure of the β-hairpin itself. The presented experiments provide biochemical evidence that β-hairpin formation plays an important role in regard to CA protein conformation required to support proper mature core arrangement. Hydrogen/deuterium exchange and in vitro assembly reactions illustrated the importance of the β-hairpin structure, its dynamics, and its influence on the orientation of helix 1 for the assembly of the mature CA lattice.
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Registered trials
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