In:
Journal of Virology, American Society for Microbiology, Vol. 76, No. 17 ( 2002-09), p. 8596-8608
Abstract:
Cellular receptors for the Fc domain of immunoglobulin G (IgG) (FcγRs) comprise a family of surface receptors on immune cells connecting humoral and cellular immune responses. Several herpesviruses induce FcγR activities in infected cells. Here we identify two distinct human cytomegalovirus (HCMV)-encoded vFcγR glycoproteins of 34 and 68 kDa. A panel of HCMV strains exhibited a slight molecular microheterogeneity between Fcγ-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 vFcγR gp68 and TRL11/IRL11 to encode vFcγR gp34. Both vFcγRs 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 FcγR I and FcγRs II/III, respectively, indicates a different ancestry and function of gpUL119-118 and gpTRL11. The HCMV-encoded vFcγRs highlight an impressive diversification and redundancy of FcγR structures.
Type of Medium:
Online Resource
ISSN:
0022-538X
,
1098-5514
DOI:
10.1128/JVI.76.17.8596-8608.2002
Language:
English
Publisher:
American Society for Microbiology
Publication Date:
2002
detail.hit.zdb_id:
1495529-5
