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Cloning and epitope mapping of a functional partial fusion receptor for human cytomegalovirus gH

Molecular and Cell Biology Program¹ and Division of Infectious Diseases², Department of Medicine, University of Maryland School of Medicine, Baltimore, MD 21201, USA
Research Service, VA Maryland Health Care System, 10 N. Greene St, Rm 3B-184, Baltimore, MD 21201, USA³

Author for correspondence: Brenda R. Baldwin. Fax +1 410 605 7837. e-mail bbald001{at}umaryland.edu

A cDNA clone encoding a partial putative human cytomegalovirus (HCMV) gH fusion receptor (CMVFR) was previously identified. In this report, the cDNA sequence of CMVFR was determined and the role of this CMVFR in HCMV/cell fusion was confirmed by rendering fusion-incompetent MOLT-4 cells susceptible to fusion following transfection with receptor cDNA. Blocking experiments using recombinant gH or either of two MAbs (against recombinant gH or purified viral gH:gL) provided additional evidence for the role of gH binding to this protein in virus fusion. An HCMV-binding domain of 12 aa in the middle hydrophilic region of CMVFR was identified by fusion blocking studies using synthetic receptor peptides. The 1368 bp cDNA of CMVFR contained a predicted ORF of 345 aa with two potential membrane-spanning domains and several possible nuclear localization signals. A search of sequence databases indicated that CMVFR is a novel protein. Further characterization of this cell membrane protein that confers susceptibility to fusion with the viral envelope should provide important information about the mechanism by which HCMV infects cells.

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