| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
|
|
|
|||||||
|
|||||||||
1 Microbiology and Tumorbiology Centre, Karolinska Institute, 171 77 Stockholm, Sweden
and2 Institut für Molekularbiologie I, Universität Zürich, Hönggenberg, CH-8093 Zürich, Switzerland
The fusion (F) glycoprotein of measles virus, a structural component of the virion envelope, contains four potential sites for attachment of N-linked oligosaccharides. Three are located in the F2 subunit of the protein and one in the signal peptide. Four mutants were constructed by oligonucleotide-directed mutagenesis, in each case changing one N-linked glycosylation site from Asn-X-Ser/Thr to Ser-X-Ser/Thr. The wild-type and altered forms of the F protein were expressed in BHK-21 and HeLa T4 cells by use of the recombinant vaccinia virus-encoding T7 polymerase system. Analysis of these proteins revealed that three (residues 29, 61 and 67) potential sites for addition of N-linked glycans in the F2 subunit are actually utilized. The functional glycosylation sites were systematically removed in all possible combinations from the F protein to form a panel of mutants from which the role of carbohydrates, singly or in various combinations, could be evaluated. One singlesite mutant protein lacking the glycosylation site of Asn-67 was processed, transported to the cell surface and could induce cell fusion. However, the other two single-site mutant proteins with deletions of glycosylation sites Asn-29 or Asn-61 exhibited a defect in processing, were not transported to cell surface and thus induced no cell fusion. The absence of any two of the three or of all three glycosylation sites resulted in protein retention in the endoplasmic reticulum. Therefore, it appears that glycosylation of sites Asn-29 and Asn-61 has important roles in maintaining the native structure of the F protein.
* Author for correspondence. Fax +46 8 331399.
Received 25 July 1994;
accepted 28 October 1994.
This article has been cited by other articles:
|
|
 |
|
  G. Long, X. Pan, and J. M. Vlak Absence of N-linked glycans from the F2 subunit of the major baculovirus envelope fusion protein F enhances fusogenicity J. Gen. Virol., February 1, 2007; 88(2): 441 - 449. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 H. C. Aguilar, K. A. Matreyek, C. M. Filone, S. T. Hashimi, E. L. Levroney, O. A. Negrete, A. Bertolotti-Ciarlet, D. Y. Choi, I. McHardy, J. A. Fulcher, et al. N-Glycans on Nipah Virus Fusion Protein Protect against Neutralization but Reduce Membrane Fusion and Viral Entry. J. Virol., May 1, 2006; 80(10): 4878 - 4889. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
M. Moll, A. Kaufmann, and A. Maisner Influence of N-Glycans on Processing and Biological Activity of the Nipah Virus Fusion Protein J. Virol., July 1, 2004; 78(13): 7274 - 7278. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
V. von Messling and R. Cattaneo N-Linked Glycans with Similar Location in the Fusion Protein Head Modulate Paramyxovirus Fusion J. Virol., October 1, 2003; 77(19): 10202 - 10212. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
C. H. Woelk, O. G. Pybus, L. Jin, D. W. G. Brown, and E. C. Holmes Increased positive selection pressure in persistent (SSPE) versus acute measles virus infections J. Gen. Virol., June 1, 2002; 83(6): 1419 - 1430. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 R. K. Plemper, A. L. Hammond, and R. Cattaneo Measles Virus Envelope Glycoproteins Hetero-oligomerize in the Endoplasmic Reticulum J. Biol. Chem., November 16, 2001; 276(47): 44239 - 44246. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
G. Zimmer, I. Trotz, and G. Herrler N-Glycans of F Protein Differentially Affect Fusion Activity of Human Respiratory Syncytial Virus J. Virol., May 15, 2001; 75(10): 4744 - 4751. [Abstract] [Full Text]
|
|
|
|
|
|
A. Weidmann, A. Maisner, W. Garten, M. Seufert, V. ter Meulen, and S. Schneider-Schaulies Proteolytic Cleavage of the Fusion Protein but Not Membrane Fusion Is Required for Measles Virus-Induced Immunosuppression In Vitro J. Virol., February 15, 2000; 74(4): 1985 - 1993. [Abstract] [Full Text]
|
|
|
|
|
|
S. N. Manié, S. Debreyne, S. Vincent, and D. Gerlier Measles Virus Structural Components Are Enriched into Lipid Raft Microdomains: a Potential Cellular Location for Virus Assembly J. Virol., January 1, 2000; 74(1): 305 - 311. [Abstract] [Full Text]
|
|
|
|
 |
|
 F. Bouche, W. Ammerlaan, F. Berthet, S. Houard, F. Schneider, and C. P. Muller Immunosorbent Assay Based on Recombinant Hemagglutinin Protein Produced in a High-Efficiency Mammalian Expression System for Surveillance of Measles Immunity J. Clin. Microbiol., March 1, 1998; 36(3): 721 - 726. [Abstract] [Full Text]
|
|
|
|
|
|
P. Spielhofer, T. Bachi, T. Fehr, G. Christiansen, R. Cattaneo, K. Kaelin, M. A. Billeter, and H. Y. Naim Chimeric Measles Viruses with a Foreign Envelope J. Virol., March 1, 1998; 72(3): 2150 - 2159. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
T. Cathomen, H. Y. Naim, and R. Cattaneo Measles Viruses with Altered Envelope Protein Cytoplasmic Tails Gain Cell Fusion Competence J. Virol., February 1, 1998; 72(2): 1224 - 1234. [Abstract] [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| INT J SYST EVOL MICROBIOL | MICROBIOLOGY | J GEN VIROL |
| J MED MICROBIOL | ALL SGM JOURNALS | |
