This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Laquerre, S.
Right arrow Articles by Glorioso, J. C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Laquerre, S.
Right arrow Articles by Glorioso, J. C.

 Previous Article  |  Next Article 

J. Virol., Mar 1996, 1640-1650, Vol 70, No. 3
Copyright © 1996, American Society for Microbiology

Glycoprotein B of herpes simplex virus type 1 oligomerizes through the intermolecular interaction of a 28-amino-acid domain

S Laquerre, S Person and JC Glorioso
Department of Molecular Genetics and Biochemistry, University of Pittsburgh, Pennsylvania 15261, USA.

Herpes simplex virus type 1 glycoprotein B (gB) is an envelope component that plays an essential role in virus infection. The biologically active form of gB is an oligomer that contributes to the process of viral envelope fusion with the cell surface membrane, resulting in viral penetration and initiation of the replication cycle. In previous studies, two discontinuous sites for oligomer formation were identified: a nonessential upstream site located between residues 93 and 282 and an essential downstream site located between residues 596 and 711. In this study, in vitro-transcribed and -translated gB test molecules were used to characterize the more active essential membrane-proximal domain. A series of gB test polypeptides mutated in this downstream oligomerization domain were assayed for their abilities to form oligomers with a mutant gB capture polypeptide containing the analogous wild-type domain. Detection of oligomers was achieved by coimmunoprecipitation of two gB mutant molecules by using a monoclonal antibody specific for a hemagglutinin epitope tag introduced into the coding sequence of the capture polypeptide. Analysis of the immune- precipitated products by sodium dodecyl sulfate-polyacrylamide gel electrophoresis demonstrated that the downstream oligomerization domain resided within residues 626 to 676. This region was further resolved into two segments, residues 626 to 653 and 653 to 675, each of which was independently sufficient to form oligomers. However, residues 626 to 653 provided for a stronger interaction between gB monomers. Moreover, this stretch of 28 amino acids was shown to form oligomers when introduced into the carboxy-terminal region of gB monomers lacking this domain at the normal site, thus indicating that this domain was functionally independent of its natural location within the gB molecule. Further analysis of the sequence within residues 596 to 653 by using mutant test polypeptides altered in individual amino acids revealed that cysteines 9 and 10 located at positions 596 and 633, respectively, were not required for oligomer formation but contributed to dimer formation and/or stabilization. The results of this study suggest that oligomerization of gB monomers is induced by interactions between contiguous residues localized within the ectodomain near the site of molecule insertion into the viral envelope membrane.


This article has been cited by other articles:

  • Li, W., Minova-Foster, T. J., Norton, D. D., Muggeridge, M. I. (2006). Identification of functional domains in herpes simplex virus 2 glycoprotein B.. J. Virol. 80: 3792-3800 [Abstract] [Full Text]  
  • Britt, W. J., Jarvis, M. A., Drummond, D. D., Mach, M. (2005). Antigenic Domain 1 Is Required for Oligomerization of Human Cytomegalovirus Glycoprotein B. J. Virol. 79: 4066-4079 [Abstract] [Full Text]  
  • Melancon, J. M., Luna, R. E., Foster, T. P., Kousoulas, K. G. (2005). Herpes Simplex Virus Type 1 gK Is Required for gB-Mediated Virus-Induced Cell Fusion, While neither gB and gK nor gB and UL20p Function Redundantly in Virion De-Envelopment. J. Virol. 79: 299-313 [Abstract] [Full Text]  
  • Foster, T. P., Melancon, J. M., Olivier, T. L., Kousoulas, K. G. (2004). Herpes Simplex Virus Type 1 Glycoprotein K and the UL20 Protein Are Interdependent for Intracellular Trafficking and trans-Golgi Network Localization. J. Virol. 78: 13262-13277 [Abstract] [Full Text]  
  • Lopper, M., Compton, T. (2002). Disulfide Bond Configuration of Human Cytomegalovirus Glycoprotein B. J. Virol. 76: 6073-6082 [Abstract] [Full Text]  
  • Kingham, B. F., Zelnik, V., Kopácek, J., Majerciak, V., Ney, E., Schmidt, C. J. (2001). The genome of herpesvirus of turkeys: comparative analysis with Marek's disease viruses. J. Gen. Virol. 82: 1123-1135 [Abstract] [Full Text]  
  • Speckner, A., Kropff, B., Knör, S., Mach, M. (2000). The antigenic domain 1 of human cytomegalovirus glycoprotein B contains an intramolecular disulphide bond. J. Gen. Virol. 81: 2659-2663 [Abstract] [Full Text]  
  • Singh, J., Compton, T. (2000). Characterization of a Panel of Insertion Mutants in Human Cytomegalovirus Glycoprotein B. J. Virol. 74: 1383-1392 [Abstract] [Full Text]  
  • Wanas, E., Efler, S., Ghosh, K., Ghosh, H. P. (1999). Mutations in the conserved carboxy-terminal hydrophobic region of glycoprotein gB affect infectivity of herpes simplex virus. J. Gen. Virol. 80: 3189-3198 [Abstract] [Full Text]  
  • Laquerre, S., Anderson, D. B., Argnani, R., Glorioso, J. C. (1998). Herpes Simplex Virus Type 1 Glycoprotein B Requires a Cysteine Residue at Position 633 for Folding, Processing, and Incorporation into Mature Infectious Virus Particles. J. Virol. 72: 4940-4949 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»