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Human Cytomegalovirus Nuclear Egress Complex Subunit, UL53, Associates with Capsids and Myosin Va, but Is Not Important for Capsid Localization towards the Nuclear Periphery

After herpesviruses encapsidate their genomes in replication compartments (RCs) within the nuclear interior, capsids migrate to the inner nuclear membrane (INM) for nuclear egress. For human cytomegalovirus (HCMV), capsid migration depends at least in part on nuclear myosin Va. It has been reported...

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Autores principales: Wilkie, Adrian R., Sharma, Mayuri, Coughlin, Margaret, Pesola, Jean M., Ericsson, Maria, Lawler, Jessica L., Fernandez, Rosio, Coen, Donald M.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8949324/
https://www.ncbi.nlm.nih.gov/pubmed/35336886
http://dx.doi.org/10.3390/v14030479
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author Wilkie, Adrian R.
Sharma, Mayuri
Coughlin, Margaret
Pesola, Jean M.
Ericsson, Maria
Lawler, Jessica L.
Fernandez, Rosio
Coen, Donald M.
author_facet Wilkie, Adrian R.
Sharma, Mayuri
Coughlin, Margaret
Pesola, Jean M.
Ericsson, Maria
Lawler, Jessica L.
Fernandez, Rosio
Coen, Donald M.
author_sort Wilkie, Adrian R.
collection PubMed
description After herpesviruses encapsidate their genomes in replication compartments (RCs) within the nuclear interior, capsids migrate to the inner nuclear membrane (INM) for nuclear egress. For human cytomegalovirus (HCMV), capsid migration depends at least in part on nuclear myosin Va. It has been reported for certain herpesviruses that the nucleoplasmic subunit of the viral nuclear egress complex (NEC) is important for this migration. To address whether this is true for HCMV, we used mass spectrometry and multiple other methods to investigate associations among the HCMV NEC nucleoplasmic subunit, UL53, myosin Va, major capsid protein, and/or capsids. We also generated complementing cells to derive and test HCMV mutants null for UL53 or the INM NEC subunit, UL50, for their importance for these associations and, using electron microscopy, for intranuclear distribution of capsids. We found modest associations among the proteins tested, which were enhanced in the absence of UL50. However, we found no role for UL53 in the interactions of myosin Va with capsids or the percentage of capsids outside RC-like inclusions in the nucleus. Thus, UL53 associates somewhat with myosin Va and capsids, but, contrary to reports regarding its homologs in other herpesviruses, is not important for migration of capsids towards the INM.
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spelling pubmed-89493242022-03-26 Human Cytomegalovirus Nuclear Egress Complex Subunit, UL53, Associates with Capsids and Myosin Va, but Is Not Important for Capsid Localization towards the Nuclear Periphery Wilkie, Adrian R. Sharma, Mayuri Coughlin, Margaret Pesola, Jean M. Ericsson, Maria Lawler, Jessica L. Fernandez, Rosio Coen, Donald M. Viruses Article After herpesviruses encapsidate their genomes in replication compartments (RCs) within the nuclear interior, capsids migrate to the inner nuclear membrane (INM) for nuclear egress. For human cytomegalovirus (HCMV), capsid migration depends at least in part on nuclear myosin Va. It has been reported for certain herpesviruses that the nucleoplasmic subunit of the viral nuclear egress complex (NEC) is important for this migration. To address whether this is true for HCMV, we used mass spectrometry and multiple other methods to investigate associations among the HCMV NEC nucleoplasmic subunit, UL53, myosin Va, major capsid protein, and/or capsids. We also generated complementing cells to derive and test HCMV mutants null for UL53 or the INM NEC subunit, UL50, for their importance for these associations and, using electron microscopy, for intranuclear distribution of capsids. We found modest associations among the proteins tested, which were enhanced in the absence of UL50. However, we found no role for UL53 in the interactions of myosin Va with capsids or the percentage of capsids outside RC-like inclusions in the nucleus. Thus, UL53 associates somewhat with myosin Va and capsids, but, contrary to reports regarding its homologs in other herpesviruses, is not important for migration of capsids towards the INM. MDPI 2022-02-26 /pmc/articles/PMC8949324/ /pubmed/35336886 http://dx.doi.org/10.3390/v14030479 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/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 (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Wilkie, Adrian R.
Sharma, Mayuri
Coughlin, Margaret
Pesola, Jean M.
Ericsson, Maria
Lawler, Jessica L.
Fernandez, Rosio
Coen, Donald M.
Human Cytomegalovirus Nuclear Egress Complex Subunit, UL53, Associates with Capsids and Myosin Va, but Is Not Important for Capsid Localization towards the Nuclear Periphery
title Human Cytomegalovirus Nuclear Egress Complex Subunit, UL53, Associates with Capsids and Myosin Va, but Is Not Important for Capsid Localization towards the Nuclear Periphery
title_full Human Cytomegalovirus Nuclear Egress Complex Subunit, UL53, Associates with Capsids and Myosin Va, but Is Not Important for Capsid Localization towards the Nuclear Periphery
title_fullStr Human Cytomegalovirus Nuclear Egress Complex Subunit, UL53, Associates with Capsids and Myosin Va, but Is Not Important for Capsid Localization towards the Nuclear Periphery
title_full_unstemmed Human Cytomegalovirus Nuclear Egress Complex Subunit, UL53, Associates with Capsids and Myosin Va, but Is Not Important for Capsid Localization towards the Nuclear Periphery
title_short Human Cytomegalovirus Nuclear Egress Complex Subunit, UL53, Associates with Capsids and Myosin Va, but Is Not Important for Capsid Localization towards the Nuclear Periphery
title_sort human cytomegalovirus nuclear egress complex subunit, ul53, associates with capsids and myosin va, but is not important for capsid localization towards the nuclear periphery
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8949324/
https://www.ncbi.nlm.nih.gov/pubmed/35336886
http://dx.doi.org/10.3390/v14030479
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