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

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.

[1]  R. Bates,et al.  Coxsackieviruses B1, B3, and B5 use decay accelerating factor as a receptor for cell attachment , 1995, Journal of virology.

[2]  F. Lottspeich,et al.  Purification and partial amino acid sequencing of a fructosyllysine-specific binding protein from cell membranes of the monocyte-like cell line U937. , 1995, Biochimica et biophysica acta.

[3]  J. Bergelson,et al.  Coxsackievirus B3 adapted to growth in RD cells binds to decay-accelerating factor (CD55) , 1995, Journal of virology.

[4]  J. Mohanty,et al.  Receptor proteins on newborn Balb/c mouse brain cells for coxsackievirus B3 are immunologically distinct from those on HeLa cells. , 1995, Virus research.

[5]  V. Kinzel,et al.  Major cell surface-located protein substrates of an ecto-protein kinase are homologs of known nuclear proteins. , 1994, Biochemistry.

[6]  P. Minor,et al.  Decay‐accelerating factor CD55 is identified as the receptor for echovirus 7 using CELICS, a rapid immuno‐focal cloning method. , 1994, The EMBO journal.

[7]  J. Bergelson,et al.  Decay-accelerating factor (CD55), a glycosylphosphatidylinositol-anchored complement regulatory protein, is a receptor for several echoviruses. , 1994, Proceedings of the National Academy of Sciences of the United States of America.

[8]  S. Huber.  VCAM-1 is a receptor for encephalomyocarditis virus on murine vascular endothelial cells , 1994, Journal of virology.

[9]  E. Kuechler,et al.  Members of the low density lipoprotein receptor family mediate cell entry of a minor-group common cold virus. , 1994, Proceedings of the National Academy of Sciences of the United States of America.

[10]  K. Klingel,et al.  Molecular pathogenesis of enterovirus-induced myocarditis: virus persistence and chronic inflammation. , 1993, Intervirology.

[11]  O. Elroy-Stein,et al.  The soluble form of two N-terminal domains of the poliovirus receptor is sufficient for blocking viral infection. , 1992, Virus research.

[12]  R. Colonno,et al.  Domains 1 and 2 of ICAM-1 are sufficient to bind human rhinoviruses. , 1992, Virus research.

[13]  K. Klingel,et al.  Ongoing enterovirus-induced myocarditis is associated with persistent heart muscle infection: quantitative analysis of virus replication, tissue damage, and inflammation. , 1992, Proceedings of the National Academy of Sciences of the United States of America.

[14]  H. Kleinman,et al.  Identification of a 110-kDa nonintegrin cell surface laminin-binding protein which recognizes an A chain neurite-promoting peptide. , 1991, Archives of biochemistry and biophysics.

[15]  A. Mcclelland,et al.  Mechanisms of receptor-mediated rhinovirus neutralization defined by two soluble forms of ICAM-1 , 1991, Journal of virology.

[16]  T. Hyypiä,et al.  RGD-dependent entry of coxsackievirus A9 into host cells and its bypass after cleavage of VP1 protein by intestinal proteases , 1991, Journal of virology.

[17]  E. Wimmer,et al.  Poliovirus can enter and infect mammalian cells by way of an intercellular adhesion molecule 1 pathway. , 1991, Proceedings of the National Academy of Sciences of the United States of America.

[18]  W. Willenbrink,et al.  Sendai virus protein-protein interactions studied by a protein-blotting protein-overlay technique: mapping of domains on NP protein required for binding to P protein , 1991, Journal of virology.

[19]  A. Görg,et al.  Two-dimensional electrophoresis , 1991, Nature.

[20]  C. Semenkovich,et al.  A protein partially expressed on the surface of HepG2 cells that binds lipoproteins specifically is nucleolin. , 1990, Biochemistry.

[21]  M. Yoshida,et al.  The poliovirus receptor protein is produced both as membrane‐bound and secreted forms. , 1990, The EMBO journal.

[22]  O. Mcbride,et al.  Genomic organization and chromosomal localization of the human nucleolin gene. , 1990, The Journal of biological chemistry.

[23]  P. Boulanger,et al.  Human adenovirus-host cell interactions: comparative study with members of subgroups B and C , 1990, Journal of virology.

[24]  G. Lopaschuk,et al.  Viral heart disease. , 1990, Chest.

[25]  M S Chapman,et al.  Modelling of the human intercellular adhesion molecule‐1, the human rhinovirus major group receptor , 1990, Proteins.

[26]  D. Krah.  Characterization of octyl glucoside-solubilized cell membrane receptors for binding measles virus. , 1989, Virology.

[27]  F. Lottspeich,et al.  Internal amino acid sequence analysis of proteins separated by gel electrophoresis after tryptic digestion in polyacrylamide matrix , 1989 .

[28]  H. Pollard,et al.  Cloning and sequencing of the human nucleolin cDNA , 1989, FEBS letters.

[29]  E. Wimmer,et al.  Cellular receptor for poliovirus: Molecular cloning, nucleotide sequence, and expression of a new member of the immunoglobulin superfamily , 1989, Cell.

[30]  A. Mcclelland,et al.  The major human rhinovirus receptor is ICAM-1 , 1989, Cell.

[31]  C. Lehner,et al.  Major nucleolar proteins shuttle between nucleus and cytoplasm , 1989, Cell.

[32]  H. Mischak,et al.  Detection of the human rhinovirus minor group receptor on renaturing Western blots. , 1988, The Journal of general virology.

[33]  D. Branton,et al.  Copper staining: a five-minute protein stain for sodium dodecyl sulfate-polyacrylamide gels. , 1987, Analytical biochemistry.

[34]  P. Hofschneider,et al.  In situ detection of enteroviral genomes in myocardial cells by nucleic acid hybridization: an approach to the diagnosis of viral heart disease. , 1987, Proceedings of the National Academy of Sciences of the United States of America.

[35]  L. Ashman,et al.  Biotinylation: an alternative to radioiodination for the identification of cell surface antigens in immunoprecipitates. , 1987, Molecular immunology.

[36]  C. Lehner,et al.  Nuclear substructure antigens. Monoclonal antibodies against components of nuclear matrix preparations. , 1986, Experimental cell research.

[37]  J. Mapoles,et al.  Purification of a HeLa cell receptor protein for group B coxsackieviruses , 1985, Journal of virology.

[38]  P. Hofschneider,et al.  Molecular cloning of the genome of a cardiotropic Coxsackie B3 virus: full-length reverse-transcribed recombinant cDNA generates infectious virus in mammalian cells. , 1985, Proceedings of the National Academy of Sciences of the United States of America.

[39]  P. Hofschneider,et al.  Coxsackie B3 virus can replicate in cultured human foetal heart cells and is inhibited by interferon. , 1985, Journal of molecular and cellular cardiology.

[40]  R. Dernick,et al.  Simplified method for silver staining of proteins in polyacrylamide gels and the mechanism of silver staining , 1985 .

[41]  J. Kyhse-Andersen.  Electroblotting of multiple gels: a simple apparatus without buffer tank for rapid transfer of proteins from polyacrylamide to nitrocellulose. , 1984, Journal of biochemical and biophysical methods.

[42]  F. Amalric,et al.  Interrelations between the maturation of a 100 kDa nucleolar protein and pre rRNA synthesis in CHO cells. , 1984, Nucleic acids research.

[43]  F. A. Anderer,et al.  Localization of phosphoprotein PP 105 in cell lines of various species. , 1983, Biochemical and biophysical research communications.

[44]  F. A. Anderer,et al.  Isolation and characterization of phosphoprotein pp 105 from simian virus 40-transformed mouse fibroblasts. , 1983, Biochimica et biophysica acta.

[45]  H. Bourbon,et al.  Detection and localization of a class of proteins immunologically related to a 100-kDa nucleolar protein. , 2005, European journal of biochemistry.

[46]  W. Hagmann,et al.  Cell adhesion-dependent differences in endogenous protein phosphorylation on the surface of various cell lines. , 1981, Biochimica et biophysica acta.

[47]  L. Philipson,et al.  Unrelated animal viruses share receptors , 1976, Nature.

[48]  W. Abelmann.  Viral myocarditis and its sequelae. , 1973, Annual review of medicine.

[49]  L. Philipson,et al.  Specific Alterations of Coxsackievirus B3 Eluted from Hela Cells , 1971, Journal of virology.

[50]  R Homma,et al.  [Cellular receptors for animal viruses]. , 1968, Tanpakushitsu kakusan koso. Protein, nucleic acid, enzyme.