ArticleThe Journal of biological chemistry2013
The maturational refolding of the β-hairpin motif of equine infectious anemia virus capsid protein extends its helix α1 at capsid assembly locus.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 13 citations in OpenAlex.
- Article
- Structures of immature EIAV Gag lattices reveal a conserved role for IP6 in lentivirus assembly.PLoS pathogens · 2020Article
- In vitro assembly of the Rous Sarcoma Virus capsid protein into hexamer tubes at physiological temperature.Scientific reports · 2017Article
- Analysis of the functional compatibility of SIV capsid sequences in the context of the FIV gag precursor.PloS one · 2017Article
- NMR profiling of biomolecules at natural abundance using 2D 1H-15N and 1H-13C multiplicity-separated (MS) HSQC spectra.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2015Article
- Stabilization of the β-hairpin in Mason-Pfizer monkey virus capsid protein- a critical step for infectivity.Retrovirology · 2014Article
- Article
- The HIVToolbox 2 web system integrates sequence, structure, function and mutation analysis.PloS one · 2014Article
- Second site reversion of a mutation near the amino terminus of the HIV-1 capsid protein.Virology · 2013Article
- Determining interdomain structure and dynamics of a retroviral capsid protein in the presence of oligomerization: implication for structural transition in capsid assembly.Biochemistry · 2013Article
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
Abstract
A retroviral capsid (CA) protein consists of two helical domains, CA(N) and CA(C), which drive hexamer and dimer formations, respectively, to form a capsid lattice. The N-terminal 13 residues of CA refold to a β-hairpin motif upon processing from its precursor polyprotein Gag. The β-hairpin is essential for correct CA assembly but unexpectedly it is not within any CA oligomeric interfaces. To understand the β-hairpin function we studied the full-length CA protein from equine infectious anemia virus (EIAV), a lentivirus sharing the same cone-shaped capsid core as HIV-1. Solution NMR spectroscopy is perfectly suited to study EIAV-CA that dimerizes weaker than HIV-1-CA. Comparison between the wild-type (wt) EIAV-CA and a variant lacking the β-hairpin structure demonstrated that folding of the β-hairpin specifically extended the N terminus of helix α1 from Tyr(20) to Pro(17). This coil to helix transition involves the conserved sequence of Thr(16)-Pro(17)-Arg(18) (Ser(16)-Pro(17)-Arg(18) in HIV-1-CA). The extended region of helix α1 constituted an expanded EIAV-CA(N) oligomeric interface and overlapped with the HIV-1-CA hexamer-core residue Arg(18), helical in structure and pivotal in assembly. Therefore we propose the function of the maturational refolding of the β-hairpin in CA assembly is to extend helix α1 at the N terminus to enhance the CA(N) oligomerization along the capsid assembly core interface. In addition, NMR resonance line broadening indicated the presence of micro-millisecond exchange kinetics due to the EIAV-CA(N) domain oligomerization, independent to the faster EIAV-CA(C) domain dimerization.
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