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 Hansen, G. H.
Right arrow Articles by Norén, O.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Hansen, G. H.
Right arrow Articles by Norén, O.

 Previous Article  |  Next Article 

J. Virol., Jan 1998, 527-534, Vol 72, No. 1
Copyright © 1998, American Society for Microbiology

The coronavirus transmissible gastroenteritis virus causes infection after receptor-mediated endocytosis and acid-dependent fusion with an intracellular compartment

GH Hansen, B Delmas, L Besnardeau, LK Vogel, H Laude, H Sjostrom and O Noren
Department of Medical Biochemistry and Genetics, The Panum Institute, Copenhagen N, Denmark.

Aminopeptidase N is a species-specific receptor for transmissible gastroenteritis virus (TGEV), which infects piglets, and for the 229E virus, which infects humans. It is not known whether these coronaviruses are endocytosed before fusion with a membrane of the target cell, causing a productive infection, or whether they fuse directly with the plasma membrane. We have studied the interaction between TGEV and a cell line (MDCK) stably expressing recombinant pig aminopeptidase N (pAPN). By electron microscopy and flow cytometry, TGEV was found to be associated with the plasma membrane after adsorption to the pAPN-MDCK cells. TGEV was also observed in endocytic pits and apical vesicles after 3 to 10 min of incubation at 38 degrees C. The number of pits and apical vesicles was increased by the TGEV incubation, indicating an increase in endocytosis. After 10 min of incubation, a distinct TGEV-pAPN-containing population of large intracellular vesicles, morphologically compatible with endosomes, was found. A higher density of pAPN receptors was observed in the pits beneath the virus particles than in the surrounding plasma membrane, indicating that TGEV recruits pAPN receptors before endocytosis. Ammonium chloride and bafilomycin A1 markedly inhibited the TGEV infection as judged from virus production and protein biosynthesis analyses but did so only when added early in the course of the infection, i.e., about 1 h after the start of endocytosis. Together our results point to an acid intracellular compartment as the site of fusion for TGEV.


This article has been cited by other articles:

  • Van Hamme, E., Dewerchin, H. L., Cornelissen, E., Verhasselt, B., Nauwynck, H. J. (2008). Clathrin- and caveolae-independent entry of feline infectious peritonitis virus in monocytes depends on dynamin. J. Gen. Virol. 89: 2147-2156 [Abstract] [Full Text]  
  • Van Hamme, E., Dewerchin, H. L., Cornelissen, E., Nauwynck, H. J. (2007). Attachment and internalization of feline infectious peritonitis virus in feline blood monocytes and Crandell feline kidney cells. J. Gen. Virol. 88: 2527-2532 [Abstract] [Full Text]  
  • Petrovic, N., Schacke, W., Gahagan, J. R., O'Conor, C. A., Winnicka, B., Conway, R. E., Mina-Osorio, P., Shapiro, L. H. (2007). CD13/APN regulates endothelial invasion and filopodia formation. Blood 110: 142-150 [Abstract] [Full Text]  
  • Winter, C., Schwegmann-Wessels, C., Cavanagh, D., Neumann, U., Herrler, G. (2006). Sialic acid is a receptor determinant for infection of cells by avian Infectious bronchitis virus.. J. Gen. Virol. 87: 1209-1216 [Abstract] [Full Text]  
  • Chu, V. C., McElroy, L. J., Chu, V., Bauman, B. E., Whittaker, G. R. (2006). The Avian Coronavirus Infectious Bronchitis Virus Undergoes Direct Low-pH-Dependent Fusion Activation during Entry into Host Cells.. J. Virol. 80: 3180-3188 [Abstract] [Full Text]  
  • Hansen, G. H., Pedersen, E. D. K., Immerdal, L., Niels-Christiansen, L.-L., Danielsen, E. M. (2005). Anti-glycosyl antibodies in lipid rafts of the enterocyte brush border: a possible host defense against pathogens. Am. J. Physiol. Gastrointest. Liver Physiol. 289: G1100-G1107 [Abstract] [Full Text]  
  • Kramer, W., Girbig, F., Corsiero, D., Pfenninger, A., Frick, W., Jahne, G., Rhein, M., Wendler, W., Lottspeich, F., Hochleitner, E. O., Orso, E., Schmitz, G. (2005). Aminopeptidase N (CD13) Is a Molecular Target of the Cholesterol Absorption Inhibitor Ezetimibe in the Enterocyte Brush Border Membrane. J. Biol. Chem. 280: 1306-1320 [Abstract] [Full Text]  
  • Nomura, R., Kiyota, A., Suzaki, E., Kataoka, K., Ohe, Y., Miyamoto, K., Senda, T., Fujimoto, T. (2004). Human Coronavirus 229E Binds to CD13 in Rafts and Enters the Cell through Caveolae. J. Virol. 78: 8701-8708 [Abstract] [Full Text]  
  • Bonavia, A., Zelus, B. D., Wentworth, D. E., Talbot, P. J., Holmes, K. V. (2003). Identification of a Receptor-Binding Domain of the Spike Glycoprotein of Human Coronavirus HCoV-229E. J. Virol. 77: 2530-2538 [Abstract] [Full Text]  
  • Kuo, L., Godeke, G.-J., Raamsman, M. J. B., Masters, P. S., Rottier, P. J. M. (2000). Retargeting of Coronavirus by Substitution of the Spike Glycoprotein Ectodomain: Crossing the Host Cell Species Barrier. J. Virol. 74: 1393-1406 [Abstract] [Full Text]  
  • Salanueva, I. J., Carrascosa, J. L., Risco, C. (1999). Structural Maturation of the Transmissible Gastroenteritis Coronavirus. J. Virol. 73: 7952-7964 [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»