Crystal Structure of the Full-Length Feline Immunodeficiency Virus Capsid Protein Shows an N-Terminal β-Hairpin in the Absence of N-Terminal Proline

Folio, Christelle; Sierra, Natalia; Dujardin, Marie; Alvarez, Guzman; Guillon, Christophe

doi:10.3390/v9110335

Submit to this Journal Review for this Journal Edit a Special Issue

Article Menu

...

Open AccessArticle

Crystal Structure of the Full-Length Feline Immunodeficiency Virus Capsid Protein Shows an N-Terminal β-Hairpin in the Absence of N-Terminal Proline

¹,

²,

¹,

and

^1,*

Equipe Rétrovirus et Biochimie Structurale, Université de Lyon, CNRS, MMSB, UMR 5086 CNRS/Université de Lyon, IBCP, Lyon 69367 CEDEX 07, France

Laboratorio de Moléculas Bioactivas, Centro Universitario Regional Litoral Norte, Universidad de la República, Paysandú 60000, Uruguay

Author to whom correspondence should be addressed.

Viruses 2017, 9(11), 335; https://doi.org/10.3390/v9110335

Received: 22 September 2017 / Revised: 3 November 2017 / Accepted: 8 November 2017 / Published: 9 November 2017

(This article belongs to the Section Animal Viruses)

View Full-Text Download PDF

Browse Figures

Citation Export

Abstract

Feline immunodeficiency virus (FIV) is a member of the Retroviridae family. It is the causative agent of an acquired immunodeficiency syndrome (AIDS) in cats and wild felines. Its capsid protein (CA) drives the assembly of the viral particle, which is a critical step in the viral replication cycle. Here, the first atomic structure of full-length FIV CA to 1.67 Å resolution is determined. The crystallized protein exhibits an original tetrameric assembly, composed of dimers which are stabilized by an intermolecular disulfide bridge induced by the crystallogenesis conditions. The FIV CA displays a standard α-helical CA topology with two domains, separated by a linker shorter than other retroviral CAs. The β-hairpin motif at its amino terminal end, which interacts with nucleotides in HIV-1, is unusually long in FIV CA. Interestingly, this functional β-motif is formed in this construct in the absence of the conserved N-terminal proline. The FIV CA exhibits a cis Arg–Pro bond in the CypA-binding loop, which is absent in known structures of lentiviral CAs. This structure represents the first tri-dimensional structure of a functional, full-length FIV CA. View Full-Text

Keywords: feline immunodeficiency virus; FIV; capsid protein; crystal structure

▼ Show Figures

Graphical abstract

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Supplementary Material

Supplementary File 1:
PDF-Document (PDF, 657 KiB)

Share and Cite

MDPI and ACS Style

Folio, C.; Sierra, N.; Dujardin, M.; Alvarez, G.; Guillon, C. Crystal Structure of the Full-Length Feline Immunodeficiency Virus Capsid Protein Shows an N-Terminal β-Hairpin in the Absence of N-Terminal Proline. Viruses 2017, 9, 335. https://doi.org/10.3390/v9110335

AMA Style

Folio C, Sierra N, Dujardin M, Alvarez G, Guillon C. Crystal Structure of the Full-Length Feline Immunodeficiency Virus Capsid Protein Shows an N-Terminal β-Hairpin in the Absence of N-Terminal Proline. Viruses. 2017; 9(11):335. https://doi.org/10.3390/v9110335

Chicago/Turabian Style

Folio, Christelle, Natalia Sierra, Marie Dujardin, Guzman Alvarez, and Christophe Guillon. 2017. "Crystal Structure of the Full-Length Feline Immunodeficiency Virus Capsid Protein Shows an N-Terminal β-Hairpin in the Absence of N-Terminal Proline" Viruses 9, no. 11: 335. https://doi.org/10.3390/v9110335

Find Other Styles

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Article Metrics

Abstract views Pdf views Html views

Article Menu

Crystal Structure of the Full-Length Feline Immunodeficiency Virus Capsid Protein Shows an N-Terminal β-Hairpin in the Absence of N-Terminal Proline

Abstract

Supplementary Material

Share and Cite

Article Metrics

Article Access Statistics

Article Access Map by Country/Region

Further Information

Guidelines

MDPI Initiatives

Follow MDPI