Recombinant human cytomegalovirus (HCMV) RL13 binds human immunoglobulin G Fc.

The human cytomegalovirus (HCMV) protein RL13 has recently been described to be present in all primary isolates but rapidly mutated in culture adapted viruses. Although these data suggest a crucial role for this gene product in HCMV primary infection, no function has so far been assigned to this pro...

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Autores principales:	Mirko Cortese, Stefano Calò, Romina D'Aurizio, Anders Lilja, Nicola Pacchiani, Marcello Merola
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2012
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/cf162a5be70a40a68db9ecec89b9269b
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spelling	oai:doaj.org-article:cf162a5be70a40a68db9ecec89b9269b2021-11-18T08:06:55ZRecombinant human cytomegalovirus (HCMV) RL13 binds human immunoglobulin G Fc.1932-620310.1371/journal.pone.0050166https://doaj.org/article/cf162a5be70a40a68db9ecec89b9269b2012-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23226246/?tool=EBIhttps://doaj.org/toc/1932-6203The human cytomegalovirus (HCMV) protein RL13 has recently been described to be present in all primary isolates but rapidly mutated in culture adapted viruses. Although these data suggest a crucial role for this gene product in HCMV primary infection, no function has so far been assigned to this protein. Working with RL13 expressed in isolation in transfected human epithelial cells, we demonstrated that recombinant RL13 from the clinical HCMV isolates TR and Merlin have selective human immunoglobulin (Ig)-binding properties towards IgG1 and IgG2 subtypes. An additional Fc binding protein, RL12, was also identified as an IgG1 and IgG2 binding protein but not further characterized. The glycoprotein RL13 trafficked to the plasma membrane where it bound and internalized exogenous IgG or its constant fragment (Fcγ). Analysis of RL13 ectodomain mutants suggested that the RL13 Ig-like domain is responsible for the Fc binding activity. Ligand-dependent internalization relied on a YxxL endocytic motif located in the C-terminal tail of RL13. Additionally, we showed that the tyrosine residue could be replaced by phenylalanine but not by alanine, indicating that the internalization signal was independent from phosphorylation events. In sum, RL13 binds human IgG and may contribute to HCMV immune evasion in the infected host, but this function does not readily explain the instability of the RL13 gene during viral propagation in cultured cells.Mirko CorteseStefano CalòRomina D'AurizioAnders LiljaNicola PacchianiMarcello MerolaPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 7, Iss 11, p e50166 (2012)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Mirko Cortese Stefano Calò Romina D'Aurizio Anders Lilja Nicola Pacchiani Marcello Merola Recombinant human cytomegalovirus (HCMV) RL13 binds human immunoglobulin G Fc.
description	The human cytomegalovirus (HCMV) protein RL13 has recently been described to be present in all primary isolates but rapidly mutated in culture adapted viruses. Although these data suggest a crucial role for this gene product in HCMV primary infection, no function has so far been assigned to this protein. Working with RL13 expressed in isolation in transfected human epithelial cells, we demonstrated that recombinant RL13 from the clinical HCMV isolates TR and Merlin have selective human immunoglobulin (Ig)-binding properties towards IgG1 and IgG2 subtypes. An additional Fc binding protein, RL12, was also identified as an IgG1 and IgG2 binding protein but not further characterized. The glycoprotein RL13 trafficked to the plasma membrane where it bound and internalized exogenous IgG or its constant fragment (Fcγ). Analysis of RL13 ectodomain mutants suggested that the RL13 Ig-like domain is responsible for the Fc binding activity. Ligand-dependent internalization relied on a YxxL endocytic motif located in the C-terminal tail of RL13. Additionally, we showed that the tyrosine residue could be replaced by phenylalanine but not by alanine, indicating that the internalization signal was independent from phosphorylation events. In sum, RL13 binds human IgG and may contribute to HCMV immune evasion in the infected host, but this function does not readily explain the instability of the RL13 gene during viral propagation in cultured cells.
format	article
author	Mirko Cortese Stefano Calò Romina D'Aurizio Anders Lilja Nicola Pacchiani Marcello Merola
author_facet	Mirko Cortese Stefano Calò Romina D'Aurizio Anders Lilja Nicola Pacchiani Marcello Merola
author_sort	Mirko Cortese
title	Recombinant human cytomegalovirus (HCMV) RL13 binds human immunoglobulin G Fc.
title_short	Recombinant human cytomegalovirus (HCMV) RL13 binds human immunoglobulin G Fc.
title_full	Recombinant human cytomegalovirus (HCMV) RL13 binds human immunoglobulin G Fc.
title_fullStr	Recombinant human cytomegalovirus (HCMV) RL13 binds human immunoglobulin G Fc.
title_full_unstemmed	Recombinant human cytomegalovirus (HCMV) RL13 binds human immunoglobulin G Fc.
title_sort	recombinant human cytomegalovirus (hcmv) rl13 binds human immunoglobulin g fc.
publisher	Public Library of Science (PLoS)
publishDate	2012
url	https://doaj.org/article/cf162a5be70a40a68db9ecec89b9269b
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Recombinant human cytomegalovirus (HCMV) RL13 binds human immunoglobulin G Fc.

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