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Publication Details
AFRICAN RESEARCH NEXUS
SHINING A SPOTLIGHT ON AFRICAN RESEARCH
immunology and microbiology
Use of recombinant fusion proteins and monoclonal antibodies to define linear and discontinuous antigenic sites on the dengue virus envelope glycoprotein
Virology, Volume 187, No. 2, Year 1992
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Description
Sixteen overlapping fragments of the dengue-2 virus envelope (E) protein, expressed as trpE-E fusion products in Escherichia coli, were used to map the epitopes defined by a panel of 20 monoclonal antibodies (MAbs) by immunoblotting. Using this technique, the amino acid sequence of six antigenic domains on the E protein was characterized. Nonneutralizing MAbs were found to define either linear-specific, subcomplex-specific (amino acids 22-58), and complex-specific (amino acids 304-332) epitopes or a subcomplex conformational-dependent epitope requiring the presence of two closely linked amino acid sequences from the E protein, 60-97 and 298-397. Neutralizing MAbs, however, defined either group-reactive epitopes present on two overlapping domains (amino acids 60-135; amino acids 60-205) or type-, subcomplex-, complex-, subgroup-, and group-specific determinants (amino acids 298-397). These neutralizing epitopes were all found to be dependent upon disulfide bridges. Our results suggest that the maintenance of a topographical arrangement of discontinuous antigenic domains in the flavivirus E-protein is necessary to induce neutralizing and protective antibodies. © 1992.
Authors & Co-Authors
Hugnot, Jean Philippe
France, Paris
Institut Pasteur, Paris
Falconar, Andrew Keith I.
United Kingdom, London
London School of Hygiene & Tropical Medicine
Morens, David Michael
United States, Honolulu
University of Hawaiʻi at Mānoa
Schlesinger, Jacob J.
United States, Rochester
Rochester General Hospital
Young, Paul R.
Australia, Brisbane
Royal Children's Hospital Brisbane
van Regenmortel, Marc H.V.
France, Strasbourg
Institut de Biologie Moléculaire et Cellulaire
Deubel, Vincent
France, Paris
Institut Pasteur, Paris
Statistics
Citations: 124
Authors: 7
Affiliations: 8
Identifiers
Doi:
10.1016/0042-6822(92)90450-4
ISSN:
00426822
Research Areas
Infectious Diseases