Stuck in the middle: structural insights into the role of gH/gL heterodimer in herpesvirus entry

Stampfer, Samuel D.; Heldwein, Ekaterina E.

doi:10.1016/j.coviro.2012.10.005

Back to Previous Page

- Add this to...
- Twitter
- Facebook
- Google Bookmarks
- LinkedIn

Stuck in the middle: structural insights into the role of gH/gL heterodimer in herpesvirus entry

Published Date:

Oct 26 2012

Publisher's site:

http://dx.doi.org/10.1016/j.coviro.2012.10.005 New Site Icon

Source:

Curr Opin Virol. 2012; 3(1):13-19.

[PDF-2.34 MB]

Details:

Alternative Title:

Curr Opin Virol

Personal Author:

Stampfer, Samuel D. ; Heldwein, Ekaterina E. ;

Description:

Enveloped viruses enter cells by fusing the viral and cellular membranes, and most use a single viral envelope protein that combines receptor-binding and fusogenic functions. In herpesviruses, these functions are distributed among multiple proteins: the conserved fusion protein gB, various non-conserved receptor-binding proteins, and the conserved gH/gL heterodimer that curiously lacks an apparent counterpart in other enveloped viruses. Recent structural studies of gH/gL from HSV-2 and EBV revealed a unique complex with no structural or functional similarity to other viral proteins. Here we analyzed gH/gL structures and highlighted important functional regions. We propose that gH/gL functions as an adaptor that transmits the triggering signals from various non-conserved inputs to the highly conserved fusion protein gB.

Subject:

[+]

Pubmed ID:

23107819

Pubmed Central ID:

PMC3562363

Document Type:

Journal Article

Funding:

1DP20D001996/DP/NCCDPHP CDC HHS/United States ; DP2 OD001996/OD/NIH HHS/United States ;

Collection(s):

CDC Public Access

Main Document Checksum:

[+]

Supporting Files:

	nihms-415073-f0001.gif	image/gif
	nihms-415073-f0001.jpg	image/jpeg
	nihms-415073-f0002.gif	image/gif
	nihms-415073-f0002.jpg	image/jpeg
	nihms-415073-f0003.gif	image/gif
	nihms-415073-f0003.jpg	image/jpeg
	nihms-415073.nxml	application/octet-stream

No Related Documents.

You May Also Like:

Crystal structure of the conserved herpesvirus fusion regulator complex gH–gL

Personal Author:

Chowdary, Tirumala K.; Cairns, Tina M.; Atanasiu, Doina; Cohen, Gary H.; Eisenberg, Roselyn J.; Heldwein, Ekaterina E.;

Published Date:

Jul 04 2010

Source:

Nat Struct Mol Biol. 17(7):882-888.

Description:

Herpesviruses, which cause many incurable diseases, infect cells by fusing viral and cellular membranes. Whereas most other enveloped viruses use a single viral catalyst called a fusogen, herpesviruses, inexplicably, require two conserved fusion-mach...

File Type:

[PDF - 4.93 MB]
Extensive mutagenesis of the HSV-1 gB ectodomain reveals remarkable stability of its postfusion form

Personal Author:

Vitu, Elvira; Sharma, Sapna; Stampfer, Samuel D.; Heldwein, Ekaterina E.;

Published Date:

Mar 13 2013

Source:

J Mol Biol. 2013; 425(11):2056-2071

Description:

Viral fusogens mediate the merger of the viral envelope and cellular membrane during viral entry. These proteins share little sequence similarity but all are thought to act by refolding through a series of conformational intermediates from the metast...

File Type:

[PDF - 2.03 MB]
HCMV gB shares structural and functional properties with gB proteins from other herpesviruses

Personal Author:

Sharma, Sapna; Wisner, Todd W.; Johnson, David C.; Heldwein, Ekaterina E.;

Published Date:

Oct 22 2012

Source:

Virology. 2012; 435(2):239-249

Description:

Glycoprotein B (gB) facilitates HCMV entry into cells by binding receptors and mediating membrane fusion. The crystal structures of gB ectodomains from HSV-1 and EBV are available, but little is known about the HCMV gB structure. Using multiangle lig...

File Type:

[PDF - 3.27 MB]
Human herpesvirus 6: An emerging pathogen.

Personal Author:

Campadelli-Fiume, G.; Mirandola, P.; Menotti, L.;

Published Date:

1999 May-Jun

Source:

Emerg Infect Dis. 5(3):353-366.

Description:

Infections with human herpesvirus 6 (HHV-6), a beta-herpesvirus of which two variant groups (A and B) are recognized, is very common, approaching 100% in seroprevalence. Primary infection with HHV-6B causes roseola infantum or exanthem subitum, a com...

File Type:

[PDF - 527.20 KB]
Atomic structure of the 26S proteasome lid reveals the mechanism of deubiquitinase inhibition

Personal Author:

Dambacher, Corey M; Worden, Evan J; Herzik, Mark A; Martin, Andreas; Lander, Gabriel C;

Source:

eLife. 2016; 5.

Description:

The 26S proteasome is responsible for the selective, ATP-dependent degradation of polyubiquitinated cellular proteins. Removal of ubiquitin chains from targeted substrates at the proteasome is a prerequisite for substrate processing and is accomplish...

File Type:

[PDF - 2.88 MB]