The Murid Herpesvirus-4 gL regulates an entry-associated conformation change in gH.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 18665235.
- Also identified by DOI 10.1371/journal.pone.0002811 and PMC identifier 2481400.
- Licence recorded as CC BY.
- The licence permits redistribution, so the abstract is shown in full and the full text is available from the publisher.
Abstract
The glycoprotein H (gH)/gL heterodimer is crucial for herpesvirus membrane fusion. Yet how it functions is not well understood. The Murid Herpesvirus-4 gH, like that of other herpesviruses, adopts its normal virion conformation by associating with gL. However, gH switched back to a gL-independent conformation after virion endocytosis. This switch coincided with a conformation switch in gB and with capsid release. Virions lacking gL constitutively expressed the down-stream form of gH, prematurely switched gB to its down-stream form, and showed premature capsid release with poor infectivity. These data argue that gL plays a key role in regulating a gH and gB functional switch from cell binding to membrane fusion.
Medical subject headings
- Membrane Glycoproteins
- Molecular Chaperones
- Rhadinovirus
- Viral Envelope Proteins
- Viral Proteins