Viruses 2013, 5(12), 3171-3191; doi:10.3390/v5123171
Article

The p36 Isoform of Murine Cytomegalovirus m152 Protein Suffices for Mediating Innate and Adaptive Immune Evasion

Institute for Virology, University Medical Center of the Johannes Gutenberg-University Mainz, Obere Zahlbacher Str. 67, Mainz D-55131, Germany
* Authors to whom correspondence should be addressed.
Received: 4 November 2013; in revised form: 6 December 2013 / Accepted: 10 December 2013 / Published: 16 December 2013
(This article belongs to the Special Issue Recent CMV Research)
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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 β-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.
Keywords: antigen presentation; BAC mutagenesis; CD8 T cells; cytomegalovirus; viral immune evasion; natural killer (NK) cells; N-linked glycosylation

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MDPI and ACS Style

Fink, A.; Renzaho, A.; Reddehase, M.J.; Lemmermann, N.A.W. The p36 Isoform of Murine Cytomegalovirus m152 Protein Suffices for Mediating Innate and Adaptive Immune Evasion. Viruses 2013, 5, 3171-3191.

AMA Style

Fink A, Renzaho A, Reddehase MJ, Lemmermann NAW. The p36 Isoform of Murine Cytomegalovirus m152 Protein Suffices for Mediating Innate and Adaptive Immune Evasion. Viruses. 2013; 5(12):3171-3191.

Chicago/Turabian Style

Fink, Annette; Renzaho, Angeliqué; Reddehase, Matthias J.; Lemmermann, Niels A.W. 2013. "The p36 Isoform of Murine Cytomegalovirus m152 Protein Suffices for Mediating Innate and Adaptive Immune Evasion." Viruses 5, no. 12: 3171-3191.

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