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 de Verdugo, U. R.
Right arrow Articles by Kandolf, R.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by de Verdugo, U. R.
Right arrow Articles by Kandolf, R.

 Previous Article  |  Next Article 

J. Virol., Nov 1995, 6751-6757, Vol 69, No. 11
Copyright © 1995, American Society for Microbiology

Characterization of a 100-kilodalton binding protein for the six serotypes of coxsackie B viruses

UR de Verdugo, HC Selinka, M Huber, B Kramer, J Kellermann, PH Hofschneider and R Kandolf
Max-Planck-Institute for Biochemistry, Martinsried, Germany.

Viral infection of host cells primarily depends on binding of the virus to a specific cell surface protein. In order to characterize the binding protein for group B coxsackieviruses (CVB), detergent- solubilized membrane proteins of different cell lines were tested in virus overlay protein-binding assays. A prominent virus-binding protein with a molecular mass of 100 kDa was detected in various CVB-permissive human and monkey cell lines but was not detected in nonpermissive cell lines. The specificity of CVB binding to the 100-kDa protein on permissive human cells was substantiated by binding of all six serotypes of CVB and by competition experiments. In contrast, poliovirus and Sendai virus did not bind to the 100-kDa CVB-specific protein. A fraction of HeLa membrane proteins enriched in the range of 100 kDa showed functional activity by transforming infectious CVB (160S) into A-particles (135S). In order to purify this CVB-binding protein, solubilized membrane proteins from HeLa cells were separated by preparative sodium dodecyl sulfate-polyacrylamide gel electrophoresis followed by elution of the 100-kDa protein. Amino acid sequence analysis of tryptic fragments of the CVB-binding protein indicated that this 100-kDa CVB-specific protein is a cell surface protein related to nucleolin. These results were confirmed by immunoprecipitations of the CVB-binding protein with nucleolin-specific antibodies, suggesting that a nucleolin-related membrane protein acts as a specific binding protein for the six serotypes of CVB.


This article has been cited by other articles:

  • Shi, H., Huang, Y., Zhou, H., Song, X., Yuan, S., Fu, Y., Luo, Y. (2007). Nucleolin is a receptor that mediates antiangiogenic and antitumor activity of endostatin. Blood 110: 2899-2906 [Abstract] [Full Text]  
  • Robinson, C. M., Sinclair, J. F., Smith, M. J., O'Brien, A. D. (2006). Shiga toxin of enterohemorrhagic Escherichia coli type O157:H7 promotes intestinal colonization. Proc. Natl. Acad. Sci. USA 103: 9667-9672 [Abstract] [Full Text]  
  • Shimakami, T., Honda, M., Kusakawa, T., Murata, T., Shimotohno, K., Kaneko, S., Murakami, S. (2006). Effect of Hepatitis C Virus (HCV) NS5B-Nucleolin Interaction on HCV Replication with HCV Subgenomic Replicon.. J. Virol. 80: 3332-3340 [Abstract] [Full Text]  
  • Hirano, K., Miki, Y., Hirai, Y., Sato, R., Itoh, T., Hayashi, A., Yamanaka, M., Eda, S., Beppu, M. (2005). A Multifunctional Shuttling Protein Nucleolin Is a Macrophage Receptor for Apoptotic Cells. J. Biol. Chem. 280: 39284-39293 [Abstract] [Full Text]  
  • Lee, C.-K., Kono, K., Haas, E., Kim, K.-S., Drescher, K. M., Chapman, N. M., Tracy, S. (2005). Characterization of an infectious cDNA copy of the genome of a naturally occurring, avirulent coxsackievirus B3 clinical isolate. J. Gen. Virol. 86: 197-210 [Abstract] [Full Text]  
  • Bose, S., Basu, M., Banerjee, A. K. (2004). Role of Nucleolin in Human Parainfluenza Virus Type 3 Infection of Human Lung Epithelial Cells. J. Virol. 78: 8146-8158 [Abstract] [Full Text]  
  • Sorokina, E. A., Wesson, J. A., Kleinman, J. G. (2004). An Acidic Peptide Sequence of Nucleolin-Related Protein Can Mediate the Attachment of Calcium Oxalate to Renal Tubule Cells. J. Am. Soc. Nephrol. 15: 2057-2065 [Abstract] [Full Text]  
  • Imajoh, M., Yagyu, K.-i., Oshima, S.-i. (2003). Early interactions of marine birnavirus infection in several fish cell lines. J. Gen. Virol. 84: 1809-1816 [Abstract] [Full Text]  
  • Shibata, Y., Muramatsu, T., Hirai, M., Inui, T., Kimura, T., Saito, H., McCormick, L. M., Bu, G., Kadomatsu, K. (2002). Nuclear Targeting by the Growth Factor Midkine. Mol. Cell. Biol. 22: 6788-6796 [Abstract] [Full Text]  
  • Nisole, S., Said, E. A., Mische, C., Prevost, M.-C., Krust, B., Bouvet, P., Bianco, A., Briand, J.-P., Hovanessian, A. G. (2002). The Anti-HIV Pentameric Pseudopeptide HB-19 Binds the C-terminal End of Nucleolin and Prevents Anchorage of Virus Particles in the Plasma Membrane of Target Cells. J. Biol. Chem. 277: 20877-20886 [Abstract] [Full Text]  
  • Triantafilou, K., Triantafilou, M., Takada, Y., Fernandez, N. (2000). Human Parechovirus 1 Utilizes Integrins alpha vbeta 3 and alpha vbeta 1 as Receptors. J. Virol. 74: 5856-5862 [Abstract] [Full Text]  
  • Pasch, A., Küpper, J.-H., Wolde, A., Kandolf, R., Selinka, H.-C. (1999). Comparative analysis of virus-host cell interactions of haemagglutinating and non-haemagglutinating strains of coxsackievirus B3. J. Gen. Virol. 80: 3153-3158 [Abstract] [Full Text]  
  • Srivastava, M., Pollard, H. B. (1999). Molecular dissection of nucleolin's role in growth and cell proliferation: new insights. FASEB J. 13: 1911-1922 [Abstract] [Full Text]  
  • Triantafilou, M., Triantafilou, K., Wilson, K. M., Takada, Y., Fernandez, N., Stanway, G. (1999). Involvement of {beta}2-microglobulin and integrin {alpha}v{beta}3 molecules in the coxsackievirus A9 infectious cycle. J. Gen. Virol. 80: 2591-2600 [Abstract] [Full Text]  
  • Sorokina, E. A., Kleinman, J. G. (1999). Cloning and Preliminary Characterization of a Calcium-binding Protein Closely Related to Nucleolin on the Apical Surface of Inner Medullary Collecting Duct Cells. J. Biol. Chem. 274: 27491-27496 [Abstract] [Full Text]  
  • Nisole, S., Krust, B., Callebaut, C., Guichard, G., Muller, S., Briand, J.-P., Hovanessian, A. G. (1999). The Anti-HIV Pseudopeptide HB-19 Forms a Complex with the Cell-surface-expressed Nucleolin Independent of Heparan Sulfate Proteoglycans. J. Biol. Chem. 274: 27875-27884 [Abstract] [Full Text]  
  • Fox, J. M., Bloom, M. E. (1999). Identification of a Cell Surface Protein from Crandell Feline Kidney Cells That Specifically Binds Aleutian Mink Disease Parvovirus. J. Virol. 73: 3835-3842 [Abstract] [Full Text]  
  • Vuorinen, T, Vainionpaa, R, Heino, J, Hyypia, T (1999). Enterovirus receptors and virus replication in human leukocytes. J. Gen. Virol. 80: 921-927 [Abstract]  
  • Ginisty, H, Sicard, H, Roger, B, Bouvet, P (1999). Structure and functions of nucleolin. J. Cell Sci. 112: 761-772 [Abstract]  
  • Liebermann, H., Mentel, R., Bauer, U., Pring-Akerblom, P., Dolling, R., Modrow, S., Seidel, W. (1998). Receptor Binding Sites and Antigenic Epitopes on the Fiber Knob of Human Adenovirus Serotype 3. J. Virol. 72: 9121-9130 [Abstract] [Full Text]  
  • Karnauchow, T. M., Dawe, S., Lublin, D. M., Dimock, K. (1998). Short Consensus Repeat Domain 1 of Decay-Accelerating Factor Is Required for Enterovirus 70 Binding. J. Virol. 72: 9380-9383 [Abstract] [Full Text]  
  • Callebaut, C., Blanco, J., Benkirane, N., Krust, B., Jacotot, E., Guichard, G., Seddiki, N., Svab, J., Dam, E., Muller, S., Briand, J.-P., Hovanessian, A. G. (1998). Identification of V3 Loop-binding Proteins as Potential Receptors Implicated in the Binding of HIV Particles to CD4+ Cells. J. Biol. Chem. 273: 21988-21997 [Abstract] [Full Text]  
  • Neff, S., Sa-Carvalho, D., Rieder, E., Mason, P. W., Blystone, S. D., Brown, E. J., Baxt, B. (1998). Foot-and-Mouth Disease Virus Virulent for Cattle Utilizes the Integrin alpha vbeta 3 as Its Receptor. J. Virol. 72: 3587-3594 [Abstract] [Full Text]  
  • Muir, P., Kammerer, U., Korn, K., Mulders, M. N., Poyry, T., Weissbrich, B., Kandolf, R., Cleator, G. M., van Loon, A. M. (1998). Molecular Typing of Enteroviruses: Current Status and Future Requirements. Clin. Microbiol. Rev. 11: 202-227 [Abstract] [Full Text]  
  • Pulli, T., Koivunen, E., Hyypia, T. (1997). Cell-surface Interactions of Echovirus 22. J. Biol. Chem. 272: 21176-21180 [Abstract] [Full Text]  
  • Gil, D., Gutierrez, D., Alarcon, B. (2001). Intracellular Redistribution of Nucleolin upon Interaction with the CD3epsilon Chain of the T Cell Receptor Complex. J. Biol. Chem. 276: 11174-11179 [Abstract] [Full Text]  
  • Sinclair, J. F., O'Brien, A. D. (2002). Cell Surface-localized Nucleolin Is a Eukaryotic Receptor for the Adhesin Intimin-gamma of Enterohemorrhagic Escherichia coli O157:H7. J. Biol. Chem. 277: 2876-2885 [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»