A Viral Pilot for HCMV Navigation?

Viruses

Barbara Adler¹ 

[1] Max von Pettenkofer-Institute for Virology, Ludwig-Maximilians-University Munich, Pettenkoferstrasse 9a, 80336 Munich, Germany;

关键词: human cytomegalovirus;    gH/gL glycoprotein complexes;    virus navigation;    UL148;   

DOI  :  10.3390/v7072801

来源: DOAJ

【 摘 要 】

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.

【 授权许可】

Unknown