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Journal of Virology, September 2002, p. 8596-8608, Vol. 76, No. 17
0022-538X/02/$04.00+0     DOI: 10.1128/JVI.76.17.8596-8608.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Identification and Expression of Human Cytomegalovirus Transcription Units Coding for Two Distinct Fc Receptor Homologs

Ramazan Atalay,¹ Albert Zimmermann,¹ Markus Wagner,² Eva Borst,^2, Christine Benz,² Martin Messerle,^2,1 and Hartmut Hengel^1*

Robert Koch-Institut, Fachgebiet Virale Infektionen, 13353 Berlin,¹ Max von Pettenkofer-Institut, Lehrstuhl Virologie, 81377 München, Germany²

Received 16 April 2002/ Accepted 5 June 2002

Cellular receptors for the Fc domain of immunoglobulin G (IgG) (FcRs) comprise a family of surface receptors on immune cells connecting humoral and cellular immune responses. Several herpesviruses induce FcR activities in infected cells. Here we identify two distinct human cytomegalovirus (HCMV)-encoded vFcR glycoproteins of 34 and 68 kDa. A panel of HCMV strains exhibited a slight molecular microheterogeneity between Fc-binding proteins, suggesting their viral origin. To locate the responsible genes within the HCMV genome, a large set of targeted HCMV deletion mutants was constructed. The mutant analysis allowed the identification of a spliced UL119-UL118 mRNA to encode vFcR gp68 and TRL11/IRL11 to encode vFcR gp34. Both vFcRs are surface resident type I transmembrane glycoproteins. Significant relatedness of sequences in the extracellular chain of gpUL119-118 and gpTRL11 with particular immunoglobulin supergene family domains present in FcR I and FcRs II/III, respectively, indicates a different ancestry and function of gpUL119-118 and gpTRL11. The HCMV-encoded vFcRs highlight an impressive diversification and redundancy of FcR structures.

Present address: Zentrum für Angewandte Medizinische Forschung, Universität Halle-Wittenberg, 06120 Halle, Germany.

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