This Article
Right arrow Full Text
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 Zhang, S. X.
Right arrow Articles by Blissard, G. W.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Zhang, S. X.
Right arrow Articles by Blissard, G. W.

 Previous Article  |  Next Article 

Journal of Virology, June 2003, p. 6265-6273, Vol. 77, No. 11
0022-538X/03/$08.00+0     DOI: 10.1128/JVI.77.11.6265-6273.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Palmitoylation of the Autographa californica Multicapsid Nucleopolyhedrovirus Envelope Glycoprotein GP64: Mapping, Functional Studies, and Lipid Rafts

Sandy Xiaoxin Zhang,1,2 Yu Han,1 and Gary W. Blissard1,2*

Boyce Thompson Institute,1 Department of Microbiology and Immunology, Cornell University, Ithaca, New York 148532

Received 20 December 2002/ Accepted 4 March 2003

Budded virions (BV) of the baculovirus Autographa californica multicapsid nucleopolyhedrovirus (AcMNPV) contain a major envelope glycoprotein known as GP64, which was previously shown to be palmitoylated. In the present study, we used truncation and amino acid substitution mutations to map the palmitoylation site to cysteine residue 503. Palmitoylation of GP64 was not detected when Cys503 was replaced with alanine or serine. Palmitoylation-minus forms of GP64 were used to replace wild-type GP64 in AcMNPV, and these viruses were used to examine potential functions of GP64 palmitoylation in the context of the infection cycle. Analysis by immunoprecipitation and cell surface studies revealed that palmitoylation of GP64 did not affect GP64 synthesis or its transport to the cell surface in Sf9 cells. GP64 proteins lacking palmitoylation also mediated low-pH-triggered membrane fusion in a manner indistinguishable from that of wild-type GP64. Cells infected with viruses expressing palmitoylation-minus forms of GP64 produced infectious virions at levels similar to those from cells infected with wild-type AcMNPV. In combination, these data suggest that virus entry and exit in Sf9 cells were not significantly affected by GP64 palmitoylation. To determine whether GP64 palmitoylation affected the association of GP64 with membrane microdomains, the potential association of GP64 with lipid raft microdomains was examined. These experiments showed that: (i) AcMNPV-infected Sf9 cell membranes contain lipid raft microdomains, (ii) GP64 association with lipid rafts was not detected in infected Sf9 cells, and (iii) GP64 palmitoylation did not affect the apparent exclusion of GP64 from lipid raft microdomains.

* Corresponding author. Mailing address: Boyce Thompson Institute at Cornell University, Tower Rd., Ithaca, NY 14853. Phone: (607) 254-1366. E-mail: gwb1{at}cornell.edu.

Journal of Virology, June 2003, p. 6265-6273, Vol. 77, No. 11
0022-538X/03/$08.00+0     DOI: 10.1128/JVI.77.11.6265-6273.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Li, Z., Blissard, G. W. (2009). The Autographa californica Multicapsid Nucleopolyhedrovirus GP64 Protein: Analysis of Transmembrane Domain Length and Sequence Requirements. J. Virol. 83: 4447-4461 [Abstract] [Full Text]  
  • Li, Z., Blissard, G. W. (2008). Functional Analysis of the Transmembrane (TM) Domain of the Autographa californica Multicapsid Nucleopolyhedrovirus GP64 Protein: Substitution of Heterologous TM Domains. J. Virol. 82: 3329-3341 [Abstract] [Full Text]  
  • Westenberg, M., Vlak, J. M. (2008). GP64 of group I nucleopolyhedroviruses cannot readily rescue infectivity of group II f-null nucleopolyhedroviruses. J. Gen. Virol. 89: 424-431 [Abstract] [Full Text]  
  • Zhou, J., Blissard, G. W. (2008). Display of Heterologous Proteins on gp64null Baculovirus Virions and Enhanced Budding Mediated by a Vesicular Stomatitis Virus G-Stem Construct. J. Virol. 82: 1368-1377 [Abstract] [Full Text]  
  • Long, G., Pan, X., Kormelink, R., Vlak, J. M. (2006). Functional entry of baculovirus into insect and Mammalian cells is dependent on clathrin-mediated endocytosis.. J. Virol. 80: 8830-8833 [Abstract] [Full Text]  
  • Thorp, E. B., Boscarino, J. A., Logan, H. L., Goletz, J. T., Gallagher, T. M. (2006). Palmitoylations on Murine Coronavirus Spike Proteins Are Essential for Virion Assembly and Infectivity. J. Virol. 80: 1280-1289 [Abstract] [Full Text]  
  • Sinn, P. L., Burnight, E. R., Hickey, M. A., Blissard, G. W., McCray, P. B. Jr. (2005). Persistent Gene Expression in Mouse Nasal Epithelia following Feline Immunodeficiency Virus-Based Vector Gene Transfer. J. Virol. 79: 12818-12827 [Abstract] [Full Text]  
  • Kitagawa, Y., Tani, H., Limn, C. K., Matsunaga, T. M., Moriishi, K., Matsuura, Y. (2005). Ligand-Directed Gene Targeting to Mammalian Cells by Pseudotype Baculoviruses. J. Virol. 79: 3639-3652 [Abstract] [Full Text]  
  • Hayashi, I., Urano, Y., Fukuda, R., Isoo, N., Kodama, T., Hamakubo, T., Tomita, T., Iwatsubo, T. (2004). Selective Reconstitution and Recovery of Functional {gamma}-Secretase Complex on Budded Baculovirus Particles. J. Biol. Chem. 279: 38040-38046 [Abstract] [Full Text]  
  • Oomens, A. G. P., Wertz, G. W. (2004). The Baculovirus GP64 Protein Mediates Highly Stable Infectivity of a Human Respiratory Syncytial Virus Lacking Its Homologous Transmembrane Glycoproteins. J. Virol. 78: 124-135 [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»