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Properties and Functions of Feline Immunodeficiency Virus Gag Domains in Virion Assembly and Budding

Feline immunodeficiency virus (FIV) is an important cat pathogen worldwide whose biological and pathophysiological properties resemble those of human immunodeficiency virus type 1 (HIV-1). Therefore, the study of FIV not only benefits its natural host but is also useful for the development of antivi...

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Autores principales: González, Silvia A., Affranchino, José L.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5977254/
https://www.ncbi.nlm.nih.gov/pubmed/29772651
http://dx.doi.org/10.3390/v10050261
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author González, Silvia A.
Affranchino, José L.
author_facet González, Silvia A.
Affranchino, José L.
author_sort González, Silvia A.
collection PubMed
description Feline immunodeficiency virus (FIV) is an important cat pathogen worldwide whose biological and pathophysiological properties resemble those of human immunodeficiency virus type 1 (HIV-1). Therefore, the study of FIV not only benefits its natural host but is also useful for the development of antiviral strategies directed against HIV-1 infections in humans. FIV assembly results from the multimerization of a single but complex viral polypeptide, the Gag precursor. In this review, we will first give an overview of the current knowledge of the proteins encoded by the FIV pol, env, rev, vif, and orf-A genes, and then we will describe and discuss in detail the critical roles that each of the FIV Gag domains plays in virion morphogenesis. Since retroviral assembly is an attractive target for therapeutic interventions, gaining a better understanding of this process is highly desirable.
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spelling pubmed-59772542018-06-01 Properties and Functions of Feline Immunodeficiency Virus Gag Domains in Virion Assembly and Budding González, Silvia A. Affranchino, José L. Viruses Review Feline immunodeficiency virus (FIV) is an important cat pathogen worldwide whose biological and pathophysiological properties resemble those of human immunodeficiency virus type 1 (HIV-1). Therefore, the study of FIV not only benefits its natural host but is also useful for the development of antiviral strategies directed against HIV-1 infections in humans. FIV assembly results from the multimerization of a single but complex viral polypeptide, the Gag precursor. In this review, we will first give an overview of the current knowledge of the proteins encoded by the FIV pol, env, rev, vif, and orf-A genes, and then we will describe and discuss in detail the critical roles that each of the FIV Gag domains plays in virion morphogenesis. Since retroviral assembly is an attractive target for therapeutic interventions, gaining a better understanding of this process is highly desirable. MDPI 2018-05-16 /pmc/articles/PMC5977254/ /pubmed/29772651 http://dx.doi.org/10.3390/v10050261 Text en © 2018 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
González, Silvia A.
Affranchino, José L.
Properties and Functions of Feline Immunodeficiency Virus Gag Domains in Virion Assembly and Budding
title Properties and Functions of Feline Immunodeficiency Virus Gag Domains in Virion Assembly and Budding
title_full Properties and Functions of Feline Immunodeficiency Virus Gag Domains in Virion Assembly and Budding
title_fullStr Properties and Functions of Feline Immunodeficiency Virus Gag Domains in Virion Assembly and Budding
title_full_unstemmed Properties and Functions of Feline Immunodeficiency Virus Gag Domains in Virion Assembly and Budding
title_short Properties and Functions of Feline Immunodeficiency Virus Gag Domains in Virion Assembly and Budding
title_sort properties and functions of feline immunodeficiency virus gag domains in virion assembly and budding
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5977254/
https://www.ncbi.nlm.nih.gov/pubmed/29772651
http://dx.doi.org/10.3390/v10050261
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