Article thumbnail

Inner tegument protein pUL37 of herpes simplex virus type 1 is involved in directing capsids to the trans-Golgi network for envelopment

By David Pasdeloup, Frauke Beilstein, Ashley P. E. Roberts, Marion McElwee, David McNab and Frazer J. Rixon


Secondary envelopment of herpes simplex virus type 1 has been demonstrated as taking place at the trans-Golgi network (TGN). The inner tegument proteins pUL36 and pUL37 and the envelope glycoproteins gD and gE are known to be important for secondary envelopment. We compared the cellular localizations of capsids from a virus mutant lacking the UL37 gene with those of a virus mutant lacking the genes encoding gD and gE. Although wild-type capsids accumulated at the TGN, capsids of the pUL37− mutant were distributed throughout the cytoplasm and showed no association with TGN-derived vesicles. This was in contrast to capsids from a gD−gE− mutant, which accumulated in the vicinity of TGN vesicles, but did not colocalize with them, suggesting that they were transported to the TGN but were unable to undergo envelopment. We conclude that the inner tegument protein pUL37 is required for directing capsids to the TGN, where secondary envelopment occurs

Topics: Animal
Publisher: Society for General Microbiology
OAI identifier:
Provided by: PubMed Central

To submit an update or takedown request for this paper, please submit an Update/Correction/Removal Request.

Suggested articles


  1. (1988). A herpes simplex virus mutant in which glycoprotein D sequences are replaced by b-galactosidase sequences binds to but is unable to penetrate into cells.
  2. (2001). A null mutation in the gene encoding the herpes simplex virus type 1 UL37 polypeptide abrogates virus maturation.
  3. (2000). A null mutation in the UL36 gene of herpes simplex virus type 1 results in accumulation of unenveloped DNAfilled capsids in the cytoplasm of infected cells.
  4. (1992). Assembly of enveloped tegument structures (L particles) can occur independently of virion maturation in herpes simplex virus type 1-infected cells.
  5. (1997). Capsid assembly and DNA packaging in herpes simplex virus.
  6. (2005). Determination of interactions between tegument proteins of herpes simplex virus type 1.
  7. (2009). Differing roles of inner tegument proteins pUL36 and pUL37 during entry of herpes simplex virus type 1.
  8. (2009). Effects of simultaneous deletion of pUL11 and glycoprotein M on virion maturation of herpes simplex virus type 1.
  9. Essential function of the pseudorabies virus UL36 gene product is D. Pasdeloup and others 2150 Journal of General Virology 91independent of its interaction with the UL37 protein.
  10. (2000). Evidence that herpes simplex virus VP16 is required for viral egress downstream of the initial envelopment event.
  11. (1993). Fragmentation and dispersal of Golgi proteins and redistribution of glycoproteins and glycolipids processed through theGolgiapparatusafterinfectionwithherpessimplexvirus1.ProcNatl Acad Sci
  12. (2003). Herpes simplex virus glycoproteins gD and gE/gI serve essential but redundant functions during acquisition of the virion envelope in the cytoplasm.
  13. (2009). Herpes simplex virus replication: roles of viral proteins and nucleoporins in capsid-nucleus attachment.
  14. (2005). Herpes simplex virus type 1 capsids transit by the trans-Golgi network, where viral glycoproteins accumulate independently of capsid egress.
  15. (2006). Herpesvirus assembly: a tale of two membranes.
  16. (2009). Herpesvirus capsid association with the nuclear pore complex and viral DNA release involve the nucleoporin CAN/Nup214 and the capsid protein pUL25.
  17. (2002). Human cytomegalovirus UL47 tegument protein functions after entry and before immediate-early gene expression.
  18. (1991). Identification and characterization of a novel non-infectious herpes simplex virusrelated particle.
  19. (2008). Identification of structural protein–protein interactions of herpes simplex virus type 1.
  20. (1998). Incorporation of the green fluorescent protein into the herpes simplex virus type 1 capsid.
  21. (1999). Inhibition of virion maturation by simultaneous deletion of glycoproteins E, I, and M of pseudorabies virus.
  22. (2008). Localization of herpes simplex virus type 1 UL37 in the Golgi complex requires UL36 but not capsid structures.
  23. other authors (2006). Herpesviral protein networks and their interaction with the human proteome.
  24. (2002). Pseudorabies virus UL36 tegument protein physically interacts with the UL37 protein.
  25. (2001). Pseudorabies virus UL37 gene product is involved in secondary envelopment.
  26. (2008). Simultaneous tracking of capsid, tegument, and envelope protein localization in living cells infected with triply fluorescent herpes simplex virus 1.
  27. (2007). The capsid and tegument of the alphaherpesviruses are linked by an interaction between the UL25 and VP1/2 proteins.
  28. (2003). The cytoplasmic tail of herpes simplex virus glycoprotein H binds to the tegument protein VP16 in vitro and in vivo.
  29. (2004). The herpes simplex virus type 1 UL20 protein modulates membrane fusion events during cytoplasmic virion morphogenesis and virusinduced cell fusion.
  30. (1994). The herpes simplex virus type 1 UL37 gene product is a component of virus particles.
  31. (2009). The major determinant for addition of tegument protein pUL48 (VP16) to capsids in herpes simplex virus type 1 is the presence of the major tegument protein pUL36 (VP1/2).
  32. (1992). The UL11 gene of herpes simplex virus 1 encodes a function that facilitates nucleocapsid envelopment and egress from cells.
  33. (1991). The UL20 gene of herpes simplex virus 1 encodes a function necessary for viral egress.
  34. (1978). Type-common CP-1 antigen of herpes simplex virus is associated with a 59,000-molecular-weight envelope glycoprotein.
  35. (2008). Virion-wide protein interactions of Kaposi’s sarcoma-associated herpesvirus.
  36. (1995). VP16 interacts via its activation domain with VP22, a tegument protein of herpes simplex virus, and is relocated to a novel macromolecular assembly in coexpressing cells.