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Phosphorylation of the Hepatitis B Virus Large Envelope Protein
We here establish the phosphorylation sites in the human hepatitis B virus (HBV) large envelope protein (L). L is involved in several functionally important interactions in the viral life cycle, including with the HBV cellular receptor, HBV capsid, Hsc70 chaperone, and cellular membranes during fusi...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Frontiers Media S.A.
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8904964/ https://www.ncbi.nlm.nih.gov/pubmed/35282608 http://dx.doi.org/10.3389/fmolb.2021.821755 |
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author | Fogeron, Marie-Laure Lecoq, Lauriane Cole, Laura Montserret, Roland David, Guillaume Page, Adeline Delolme, Frédéric Nassal, Michael Böckmann, Anja |
author_facet | Fogeron, Marie-Laure Lecoq, Lauriane Cole, Laura Montserret, Roland David, Guillaume Page, Adeline Delolme, Frédéric Nassal, Michael Böckmann, Anja |
author_sort | Fogeron, Marie-Laure |
collection | PubMed |
description | We here establish the phosphorylation sites in the human hepatitis B virus (HBV) large envelope protein (L). L is involved in several functionally important interactions in the viral life cycle, including with the HBV cellular receptor, HBV capsid, Hsc70 chaperone, and cellular membranes during fusion. We have recently shown that cell-free synthesis of the homologous L protein of duck HBV in wheat germ extract results in very similar phosphorylation events to those previously observed in animal cells. Here, we used mass spectrometry and NMR to establish the phosphorylation patterns of human HBV L protein produced by both in vitro cell-free synthesis and in E. coli with the co-expression of the human MAPK14 kinase. While in the avian virus the phosphorylation of L has been shown to be dispensable for infectivity, the identified locations in the human virus protein, both in the PreS1 and PreS2 domains, raise the intriguing possibility that they might play a functional role, since they are found at strategic sites predicted to be involved in L interactions. This would warrant the further investigation of a possible function in virion formation or cell entry. |
format | Online Article Text |
id | pubmed-8904964 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-89049642022-03-10 Phosphorylation of the Hepatitis B Virus Large Envelope Protein Fogeron, Marie-Laure Lecoq, Lauriane Cole, Laura Montserret, Roland David, Guillaume Page, Adeline Delolme, Frédéric Nassal, Michael Böckmann, Anja Front Mol Biosci Molecular Biosciences We here establish the phosphorylation sites in the human hepatitis B virus (HBV) large envelope protein (L). L is involved in several functionally important interactions in the viral life cycle, including with the HBV cellular receptor, HBV capsid, Hsc70 chaperone, and cellular membranes during fusion. We have recently shown that cell-free synthesis of the homologous L protein of duck HBV in wheat germ extract results in very similar phosphorylation events to those previously observed in animal cells. Here, we used mass spectrometry and NMR to establish the phosphorylation patterns of human HBV L protein produced by both in vitro cell-free synthesis and in E. coli with the co-expression of the human MAPK14 kinase. While in the avian virus the phosphorylation of L has been shown to be dispensable for infectivity, the identified locations in the human virus protein, both in the PreS1 and PreS2 domains, raise the intriguing possibility that they might play a functional role, since they are found at strategic sites predicted to be involved in L interactions. This would warrant the further investigation of a possible function in virion formation or cell entry. Frontiers Media S.A. 2022-02-23 /pmc/articles/PMC8904964/ /pubmed/35282608 http://dx.doi.org/10.3389/fmolb.2021.821755 Text en Copyright © 2022 Fogeron, Lecoq, Cole, Montserret, David, Page, Delolme, Nassal and Böckmann. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Molecular Biosciences Fogeron, Marie-Laure Lecoq, Lauriane Cole, Laura Montserret, Roland David, Guillaume Page, Adeline Delolme, Frédéric Nassal, Michael Böckmann, Anja Phosphorylation of the Hepatitis B Virus Large Envelope Protein |
title | Phosphorylation of the Hepatitis B Virus Large Envelope Protein |
title_full | Phosphorylation of the Hepatitis B Virus Large Envelope Protein |
title_fullStr | Phosphorylation of the Hepatitis B Virus Large Envelope Protein |
title_full_unstemmed | Phosphorylation of the Hepatitis B Virus Large Envelope Protein |
title_short | Phosphorylation of the Hepatitis B Virus Large Envelope Protein |
title_sort | phosphorylation of the hepatitis b virus large envelope protein |
topic | Molecular Biosciences |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8904964/ https://www.ncbi.nlm.nih.gov/pubmed/35282608 http://dx.doi.org/10.3389/fmolb.2021.821755 |
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