Gutenberg Open Science: The p36 isoform of murine cytomegalovirus m152 protein suffices for mediating innate and adaptive immune evasion

Please use this identifier to cite or link to this item: http://doi.org/10.25358/openscience-8134

Full metadata record

DC Field	Value	Language
dc.contributor.author	Fink, Annette	-
dc.contributor.author	Renzaho, Angelique	-
dc.contributor.author	Reddehase, Matthias J.	-
dc.contributor.author	Lemmermann, Niels	-
dc.date.accessioned	2022-10-21T07:09:14Z	-
dc.date.available	2022-10-21T07:09:14Z	-
dc.date.issued	2013	-
dc.identifier.uri	https://openscience.ub.uni-mainz.de/handle/20.500.12030/8149	-
dc.description.abstract	The MHC-class I (MHC-I)-like viral (MHC-Iv) m152 gene product of murine cytomegalovirus (mCMV) was the first immune evasion molecule described for a member of the beta-subfamily of herpesviruses as a paradigm for analogous functions of human cytomegalovirus proteins. Notably, by interacting with classical MHC-I molecules and with MHC-I-like RAE1 family ligands of the activatory natural killer (NK) cell receptor NKG2D, it inhibits presentation of antigenic peptides to CD8 T cells and the NKG2D-dependent activation of NK cells, respectively, thus simultaneously interfering with adaptive and innate immune recognition of infected cells. Although the m152 gene product exists in differentially glycosylated isoforms whose individual contributions to immune evasion are unknown, it has entered the scientific literature as m152/gp40, based on the quantitatively most prominent isoform but with no functional justification. By construction of a recombinant mCMV in which all three N-glycosylation sites are mutated (N61Q, N208Q, and N241Q), we show here that N-linked glycosylation is not essential for functional interaction of the m152 immune evasion protein with either MHC-I or RAE1. These data add an important functional detail to recent structural analysis of the m152/RAE1g complex that has revealed N-glycosylations at positions Asn61 and Asn208 of m152 distant from the m152/RAE1g interface.	en_GB
dc.description.sponsorship	DFG, Open Access-Publizieren Universität Mainz / Universitätsmedizin	de
dc.language.iso	eng	de
dc.rights	CC BY	*
dc.rights.uri	https://creativecommons.org/licenses/by/3.0/	*
dc.subject.ddc	570 Biowissenschaften	de_DE
dc.subject.ddc	570 Life sciences	en_GB
dc.title	The p36 isoform of murine cytomegalovirus m152 protein suffices for mediating innate and adaptive immune evasion	en_GB
dc.type	Zeitschriftenaufsatz	de
dc.identifier.doi	http://doi.org/10.25358/openscience-8134	-
jgu.type.dinitype	article	en_GB
jgu.type.version	Published version	de
jgu.type.resource	Text	de
jgu.organisation.department	FB 04 Medizin	de
jgu.organisation.number	2700	-
jgu.organisation.name	Johannes Gutenberg-Universität Mainz	-
jgu.rights.accessrights	openAccess	-
jgu.journal.title	Viruses	de
jgu.journal.volume	5	de
jgu.journal.issue	12	de
jgu.pages.start	3171	de
jgu.pages.end	3191	de
jgu.publisher.year	2013	-
jgu.publisher.name	MDPI	de
jgu.publisher.place	Basel	de
jgu.publisher.uri	http://dx.doi.org/10.3390/v5123171	de
jgu.publisher.issn	1999-4915	de
jgu.organisation.place	Mainz	-
jgu.identifier.pmid	24351798	-
jgu.subject.ddccode	570	de
opus.date.modified	2018-07-30T10:10:33Z	-
opus.subject.dfgcode	04-204	-
opus.organisation.string	FB 04: Medizin: Institut für Virologie	de_DE
opus.identifier.opusid	25204	-
opus.importsource	pubmed	-
opus.institute.number	0409	-
opus.metadataonly	false	-
opus.type.contenttype	Keine	de_DE
opus.type.contenttype	None	en_EN
opus.affiliated	Reddehase, Matthias J.	-
opus.affiliated	Lemmermann, Niels	-
jgu.publisher.doi	10.3390/v5123171	de
jgu.organisation.ror	https://ror.org/023b0x485	-
Appears in collections:	DFG-OA-Publizieren (2012 - 2017)

Files in This Item:

	File	Description	Size	Format
	the_p36_isoform_of_murine_cyt-20220925175438902.pdf		1.88 MB	Adobe PDF	View/Open

Show simple item record