Chemokine binding protein M3 of murine gammaherpesvirus 68 modulates the host response to infection in a natural host.

Murine γ-herpesvirus 68 (MHV-68) infection of Mus musculus-derived strains of mice is an attractive model of γ-herpesvirus infection. Surprisingly, however, ablation of expression of MHV-68 M3, a secreted protein with broad chemokine-binding properties in vitro, has no discernable effect during expe...

Descripción completa

Guardado en:
Detalles Bibliográficos
Autores principales: David J Hughes, Anja Kipar, Gail H Leeming, Elaine Bennett, Deborah Howarth, Joanne A Cummerson, Rita Papoula-Pereira, Brian F Flanagan, Jeffery T Sample, James P Stewart
Formato: article
Lenguaje:EN
Publicado: Public Library of Science (PLoS) 2011
Materias:
Acceso en línea:https://doaj.org/article/360f7cdf33d348258884c797c13ee8d6
Etiquetas: Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
id oai:doaj.org-article:360f7cdf33d348258884c797c13ee8d6
record_format dspace
spelling oai:doaj.org-article:360f7cdf33d348258884c797c13ee8d62021-11-18T06:03:31ZChemokine binding protein M3 of murine gammaherpesvirus 68 modulates the host response to infection in a natural host.1553-73661553-737410.1371/journal.ppat.1001321https://doaj.org/article/360f7cdf33d348258884c797c13ee8d62011-03-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/21445235/pdf/?tool=EBIhttps://doaj.org/toc/1553-7366https://doaj.org/toc/1553-7374Murine γ-herpesvirus 68 (MHV-68) infection of Mus musculus-derived strains of mice is an attractive model of γ-herpesvirus infection. Surprisingly, however, ablation of expression of MHV-68 M3, a secreted protein with broad chemokine-binding properties in vitro, has no discernable effect during experimental infection via the respiratory tract. Here we demonstrate that M3 indeed contributes significantly to MHV-68 infection, but only in the context of a natural host, the wood mouse (Apodemus sylvaticus). Specifically, M3 was essential for two features unique to the wood mouse: virus-dependent inducible bronchus-associated lymphoid tissue (iBALT) in the lung and highly organized secondary follicles in the spleen, both predominant sites of latency in these organs. Consequently, lack of M3 resulted in substantially reduced latency in the spleen and lung. In the absence of M3, splenic germinal centers appeared as previously described for MHV-68-infected laboratory strains of mice, further evidence that M3 is not fully functional in the established model host. Finally, analyses of M3's influence on chemokine and cytokine levels within the lungs of infected wood mice were consistent with the known chemokine-binding profile of M3, and revealed additional influences that provide further insight into its role in MHV-68 biology.David J HughesAnja KiparGail H LeemingElaine BennettDeborah HowarthJoanne A CummersonRita Papoula-PereiraBrian F FlanaganJeffery T SampleJames P StewartPublic Library of Science (PLoS)articleImmunologic diseases. AllergyRC581-607Biology (General)QH301-705.5ENPLoS Pathogens, Vol 7, Iss 3, p e1001321 (2011)
institution DOAJ
collection DOAJ
language EN
topic Immunologic diseases. Allergy
RC581-607
Biology (General)
QH301-705.5
spellingShingle Immunologic diseases. Allergy
RC581-607
Biology (General)
QH301-705.5
David J Hughes
Anja Kipar
Gail H Leeming
Elaine Bennett
Deborah Howarth
Joanne A Cummerson
Rita Papoula-Pereira
Brian F Flanagan
Jeffery T Sample
James P Stewart
Chemokine binding protein M3 of murine gammaherpesvirus 68 modulates the host response to infection in a natural host.
description Murine γ-herpesvirus 68 (MHV-68) infection of Mus musculus-derived strains of mice is an attractive model of γ-herpesvirus infection. Surprisingly, however, ablation of expression of MHV-68 M3, a secreted protein with broad chemokine-binding properties in vitro, has no discernable effect during experimental infection via the respiratory tract. Here we demonstrate that M3 indeed contributes significantly to MHV-68 infection, but only in the context of a natural host, the wood mouse (Apodemus sylvaticus). Specifically, M3 was essential for two features unique to the wood mouse: virus-dependent inducible bronchus-associated lymphoid tissue (iBALT) in the lung and highly organized secondary follicles in the spleen, both predominant sites of latency in these organs. Consequently, lack of M3 resulted in substantially reduced latency in the spleen and lung. In the absence of M3, splenic germinal centers appeared as previously described for MHV-68-infected laboratory strains of mice, further evidence that M3 is not fully functional in the established model host. Finally, analyses of M3's influence on chemokine and cytokine levels within the lungs of infected wood mice were consistent with the known chemokine-binding profile of M3, and revealed additional influences that provide further insight into its role in MHV-68 biology.
format article
author David J Hughes
Anja Kipar
Gail H Leeming
Elaine Bennett
Deborah Howarth
Joanne A Cummerson
Rita Papoula-Pereira
Brian F Flanagan
Jeffery T Sample
James P Stewart
author_facet David J Hughes
Anja Kipar
Gail H Leeming
Elaine Bennett
Deborah Howarth
Joanne A Cummerson
Rita Papoula-Pereira
Brian F Flanagan
Jeffery T Sample
James P Stewart
author_sort David J Hughes
title Chemokine binding protein M3 of murine gammaherpesvirus 68 modulates the host response to infection in a natural host.
title_short Chemokine binding protein M3 of murine gammaherpesvirus 68 modulates the host response to infection in a natural host.
title_full Chemokine binding protein M3 of murine gammaherpesvirus 68 modulates the host response to infection in a natural host.
title_fullStr Chemokine binding protein M3 of murine gammaherpesvirus 68 modulates the host response to infection in a natural host.
title_full_unstemmed Chemokine binding protein M3 of murine gammaherpesvirus 68 modulates the host response to infection in a natural host.
title_sort chemokine binding protein m3 of murine gammaherpesvirus 68 modulates the host response to infection in a natural host.
publisher Public Library of Science (PLoS)
publishDate 2011
url https://doaj.org/article/360f7cdf33d348258884c797c13ee8d6
work_keys_str_mv AT davidjhughes chemokinebindingproteinm3ofmurinegammaherpesvirus68modulatesthehostresponsetoinfectioninanaturalhost
AT anjakipar chemokinebindingproteinm3ofmurinegammaherpesvirus68modulatesthehostresponsetoinfectioninanaturalhost
AT gailhleeming chemokinebindingproteinm3ofmurinegammaherpesvirus68modulatesthehostresponsetoinfectioninanaturalhost
AT elainebennett chemokinebindingproteinm3ofmurinegammaherpesvirus68modulatesthehostresponsetoinfectioninanaturalhost
AT deborahhowarth chemokinebindingproteinm3ofmurinegammaherpesvirus68modulatesthehostresponsetoinfectioninanaturalhost
AT joanneacummerson chemokinebindingproteinm3ofmurinegammaherpesvirus68modulatesthehostresponsetoinfectioninanaturalhost
AT ritapapoulapereira chemokinebindingproteinm3ofmurinegammaherpesvirus68modulatesthehostresponsetoinfectioninanaturalhost
AT brianfflanagan chemokinebindingproteinm3ofmurinegammaherpesvirus68modulatesthehostresponsetoinfectioninanaturalhost
AT jefferytsample chemokinebindingproteinm3ofmurinegammaherpesvirus68modulatesthehostresponsetoinfectioninanaturalhost
AT jamespstewart chemokinebindingproteinm3ofmurinegammaherpesvirus68modulatesthehostresponsetoinfectioninanaturalhost
_version_ 1718424658699616256