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Membrane Association and Topology of Citrus Leprosis Virus C2 Movement and Capsid Proteins

Although citrus leprosis disease has been known for more than a hundred years, one of its causal agents, citrus leprosis virus C2 (CiLV-C2), is poorly characterized. This study described the association of CiLV-C2 movement protein (MP) and capsid protein (p29) with biological membranes. Our findings...

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Autores principales: Leastro, Mikhail Oliveira, Freitas-Astúa, Juliana, Kitajima, Elliot Watanabe, Pallás, Vicente, Sánchez-Navarro, Jesús Á.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7922530/
https://www.ncbi.nlm.nih.gov/pubmed/33671330
http://dx.doi.org/10.3390/microorganisms9020418
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author Leastro, Mikhail Oliveira
Freitas-Astúa, Juliana
Kitajima, Elliot Watanabe
Pallás, Vicente
Sánchez-Navarro, Jesús Á.
author_facet Leastro, Mikhail Oliveira
Freitas-Astúa, Juliana
Kitajima, Elliot Watanabe
Pallás, Vicente
Sánchez-Navarro, Jesús Á.
author_sort Leastro, Mikhail Oliveira
collection PubMed
description Although citrus leprosis disease has been known for more than a hundred years, one of its causal agents, citrus leprosis virus C2 (CiLV-C2), is poorly characterized. This study described the association of CiLV-C2 movement protein (MP) and capsid protein (p29) with biological membranes. Our findings obtained by computer predictions, chemical treatments after membrane fractionation, and biomolecular fluorescence complementation assays revealed that p29 is peripherally associated, while the MP is integrally bound to the cell membranes. Topological analyses revealed that both the p29 and MP expose their N- and C-termini to the cell cytoplasmic compartment. The implications of these results in the intracellular movement of the virus were discussed.
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spelling pubmed-79225302021-03-03 Membrane Association and Topology of Citrus Leprosis Virus C2 Movement and Capsid Proteins Leastro, Mikhail Oliveira Freitas-Astúa, Juliana Kitajima, Elliot Watanabe Pallás, Vicente Sánchez-Navarro, Jesús Á. Microorganisms Communication Although citrus leprosis disease has been known for more than a hundred years, one of its causal agents, citrus leprosis virus C2 (CiLV-C2), is poorly characterized. This study described the association of CiLV-C2 movement protein (MP) and capsid protein (p29) with biological membranes. Our findings obtained by computer predictions, chemical treatments after membrane fractionation, and biomolecular fluorescence complementation assays revealed that p29 is peripherally associated, while the MP is integrally bound to the cell membranes. Topological analyses revealed that both the p29 and MP expose their N- and C-termini to the cell cytoplasmic compartment. The implications of these results in the intracellular movement of the virus were discussed. MDPI 2021-02-17 /pmc/articles/PMC7922530/ /pubmed/33671330 http://dx.doi.org/10.3390/microorganisms9020418 Text en © 2021 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 Communication
Leastro, Mikhail Oliveira
Freitas-Astúa, Juliana
Kitajima, Elliot Watanabe
Pallás, Vicente
Sánchez-Navarro, Jesús Á.
Membrane Association and Topology of Citrus Leprosis Virus C2 Movement and Capsid Proteins
title Membrane Association and Topology of Citrus Leprosis Virus C2 Movement and Capsid Proteins
title_full Membrane Association and Topology of Citrus Leprosis Virus C2 Movement and Capsid Proteins
title_fullStr Membrane Association and Topology of Citrus Leprosis Virus C2 Movement and Capsid Proteins
title_full_unstemmed Membrane Association and Topology of Citrus Leprosis Virus C2 Movement and Capsid Proteins
title_short Membrane Association and Topology of Citrus Leprosis Virus C2 Movement and Capsid Proteins
title_sort membrane association and topology of citrus leprosis virus c2 movement and capsid proteins
topic Communication
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7922530/
https://www.ncbi.nlm.nih.gov/pubmed/33671330
http://dx.doi.org/10.3390/microorganisms9020418
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