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

 Previous Article  |  Next Article 

J. Virol., Feb 1997, 1162-1172, Vol 71, No. 2
Copyright © 1997, American Society for Microbiology

Immunocytochemical analysis of Uukuniemi virus budding compartments: role of the intermediate compartment and the Golgi stack in virus maturation

J Jantti, P Hilden, H Ronka, V Makiranta, S Keranen and E Kuismanen
Department of Biosciences, University of Helsinki Biocenter, Finland.

Previous studies have suggested that Uukuniemi virus, a bunyavirus, matures at the membranes of the Golgi complex. In this study we have employed immunocytochemical techniques to analyze in detail the budding compartment(s) of the virus. Electron microscopy of infected BHK-21 cells showed that virus particles are found in the cisternae throughout the Golgi stack. Within the cisternae, the virus particles were located preferentially in the dilated rims. This would suggest that virus budding may begin at or before the cis Golgi membranes. The virus budding compartment was studied further by immunoelectron microscopy with a pre-Golgi intermediate compartment marker, p58, and a Golgi stack marker protein, mannosidase II (ManII). Virus particles and budding virus were detected in ManII-positive Golgi stack membranes and, interestingly, in both juxtanuclear and peripheral p58-positive elements of the intermediate compartment. In cells incubated at 15 degrees C the nucleocapsid and virus envelope proteins were seen to accumulate in the intermediate compartment. Immunoelectron microscopy demonstrated that at 15 degrees C the nucleocapsid is associated with membranes that show a characteristic distribution and tubulo-vesicular morphology of the pre-Golgi intermediate compartment. These membranes contained virus particles in the lumen. The results indicate that the first site of formation of Uukuniemi virus particles is the pre-Golgi intermediate compartment and that virus budding continues in the Golgi stack. The results raise questions about the intracellular transport pathway of the virus particles, which are 100 to 120 nm in diameter and are therefore too large to be transported in the 60-nm-diameter vesicles postulated to function in the intra-Golgi transport. The distribution of the virus in the Golgi stack may imply that the cisternae themselves have a role in the vectorial transport of virus particles.

This article has been cited by other articles:

• Ribeiro, D., Foresti, O., Denecke, J., Wellink, J., Goldbach, R., Kormelink, R. J. M. (2008). Tomato spotted wilt virus glycoproteins induce the formation of endoplasmic reticulum- and Golgi-derived pleomorphic membrane structures in plant cells. J. Gen. Virol. 89: 1811-1818 [Abstract] [Full Text]  
• Overby, A. K., Popov, V. L., Pettersson, R. F., Neve, E. P. A. (2007). The Cytoplasmic Tails of Uukuniemi Virus (Bunyaviridae) GN and GC Glycoproteins Are Important for Intracellular Targeting and the Budding of Virus-Like Particles. J. Virol. 81: 11381-11391 [Abstract] [Full Text]  
• Ramanathan, H. N., Chung, D.-H., Plane, S. J., Sztul, E., Chu, Y.-k., Guttieri, M. C., McDowell, M., Ali, G., Jonsson, C. B. (2007). Dynein-Dependent Transport of the Hantaan Virus Nucleocapsid Protein to the Endoplasmic Reticulum-Golgi Intermediate Compartment. J. Virol. 81: 8634-8647 [Abstract] [Full Text]  
• Overby, A. K., Pettersson, R. F., Neve, E. P. A. (2007). The Glycoprotein Cytoplasmic Tail of Uukuniemi Virus (Bunyaviridae) Interacts with Ribonucleoproteins and Is Critical for Genome Packaging. J. Virol. 81: 3198-3205 [Abstract] [Full Text]  
• Novoa, R. R., Calderita, G., Cabezas, P., Elliott, R. M., Risco, C. (2005). Key Golgi Factors for Structural and Functional Maturation of Bunyamwera Virus. J. Virol. 79: 10852-10863 [Abstract] [Full Text]  
• Salanueva, I. J., Novoa, R. R., Cabezas, P., Lopez-Iglesias, C., Carrascosa, J. L., Elliott, R. M., Risco, C. (2002). Polymorphism and Structural Maturation of Bunyamwera Virus in Golgi and Post-Golgi Compartments. J. Virol. 77: 1368-1381 [Abstract] [Full Text]  
• Nagata, T., Inoue-Nagata, A. K., van Lent, J., Goldbach, R., Peters, D. (2002). Factors determining vector competence and specificity for transmission of Tomato spotted wilt virus. J. Gen. Virol. 83: 663-671 [Abstract] [Full Text]  
• Ying, M, Flatmark, T, Saraste, J (2000). The p58-positive pre-golgi intermediates consist of distinct subpopulations of particles that show differential binding of COPI and COPII coats and contain vacuolar H(+)-ATPase. J. Cell Sci. 113: 3623-3638 [Abstract]  
• Hauri, H., Kappeler, F, Andersson, H, Appenzeller, C (2000). ERGIC-53 and traffic in the secretory pathway. J. Cell Sci. 113: 587-596 [Abstract]  
• Salanueva, I. J., Carrascosa, J. L., Risco, C. (1999). Structural Maturation of the Transmissible Gastroenteritis Coronavirus. J. Virol. 73: 7952-7964 [Abstract] [Full Text]  
• Andersson, A. M., Pettersson, R. F. (1998). Targeting of a Short Peptide Derived from the Cytoplasmic Tail of the G1 Membrane Glycoprotein of Uukuniemi Virus (Bunyaviridae) to the Golgi Complex. J. Virol. 72: 9585-9596 [Abstract] [Full Text]  
• Risco, C., Muntion, M., Enjuanes, L., Carrascosa, J. L. (1998). Two Types of Virus-Related Particles Are Found during Transmissible Gastroenteritis Virus Morphogenesis. J. Virol. 72: 4022-4031 [Abstract] [Full Text]  
• Cluett, E. B., Kuismanen, E., Machamer, C. E. (1997). Heterogeneous Distribution of the Unusual Phospholipid Semilysobisphosphatidic Acid through the Golgi Complex. Mol. Biol. Cell 8: 2233-2240 [Abstract] [Full Text]