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Viruses 2015, 7(7), 3857-3862;

A Viral Pilot for HCMV Navigation?

Max von Pettenkofer-Institute for Virology, Ludwig-Maximilians-University Munich, Pettenkoferstrasse 9a, 80336 Munich, Germany
Academic Editor: Rachel Van Duyne
Received: 15 May 2015 / Revised: 7 July 2015 / Accepted: 10 July 2015 / Published: 15 July 2015
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gH/gL virion envelope glycoprotein complexes of herpesviruses serve as entry complexes and mediate viral cell tropism. By binding additional viral proteins, gH/gL forms multimeric complexes which bind to specific host cell receptors. Both Epstein–Barr virus (EBV) and human cytomegalovirus (HCMV) express alternative multimeric gH/gL complexes. Relative amounts of these alternative complexes in the viral envelope determine which host cells are preferentially infected. Host cells of EBV can modulate the gH/gL complex complement of progeny viruses by cell type-dependent degradation of one of the associating proteins. Host cells of HCMV modulate the tropism of their virus progenies by releasing or not releasing virus populations with a specific gH/gL complex complement out of a heterogeneous pool of virions. The group of Jeremy Kamil has recently shown that the HCMV ER-resident protein UL148 controls integration of one of the HCMV gH/gL complexes into virions and thus creates a pool of virions which can be routed by different host cells. This first mechanistic insight into regulation of the gH/gL complex complement of HCMV progenies presents UL148 as a pilot candidate for HCMV navigation in its infected host. View Full-Text
Keywords: human cytomegalovirus; gH/gL glycoprotein complexes; virus navigation; UL148 human cytomegalovirus; gH/gL glycoprotein complexes; virus navigation; UL148

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Adler, B. A Viral Pilot for HCMV Navigation? Viruses 2015, 7, 3857-3862.

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