Detail Human monoclonal antibodies for the immunological characterization of a highly conserved protein domain of the hepatitis C virus glycoprotein E1 (from Clin Exp Immunol 1995, 101, 278-283) Bibliografi Author: Siemoneit, K. ; Cardoso, M. Da Silva ; Koerner, K. ; Wolpl, A. ; Kubanek, B. Topik: Human monoclonal antibodies; Hepatitis C virus; Validation ref - 9 Bahasa: (EN )     Penerbit: Blackwell Science     Tahun Terbit: 1995     Jenis: Article - diterbitkan di jurnal ilmiah internasional Fulltext: SIEMONEIT_et_al-1995-Clinical_&_Experimental_Immunology.pdf (1.29MB; 0 download) Abstract Although both envelope glycoproteins of the hepatitis C virus, EI and E2jNS I, show a high degree of sequence variation, the E1 protein includes a well conserved domain, which may be functionally important. We have analysed the human B cell response to a peptide fragment from amino acid residues 314-330 (EP3) covering the central conserved sequence of this domain. Anti-hepatitis C virus-positive blood donors were screened for anti-EP3 antibodies with an ELISA based on immobilized peptide. Thirty out of 92 (32%) RIBA-confirmed donors displayed a significant antibody response to EP3. From three of these blood donors we established four anti-EP3-producing heterohybridoma cell lines: Ul/F30 and Ul/F31 produced IgM-K, whereas Ul/F32 and Ul/F33 secreted the isotypes IgGl-(lamda) and IgGI-K, respectively. Epitope analysis with overlapping nonapeptides suggests the existence of different antigenic determinants within the EP3 fragment. Although both IgG antibodies Ul/F32 and Ul/F33 have dissociation constants to the peptide of ~ 10^-9 M, binding to recombinant E1 protein expressed in COS-7 cells was different. Only Ul/F33 detected envelope protein of ~24-35 kD in Western blot. This human MoAb will be useful for further investigations on the hepatitis C virus glycoprotein El. [validation ref - 9] Opini Anda Klik untuk menuliskan opini Anda tentang koleksi ini! Lihat Sejarah Pengadaan  Konversi Metadata   Kembali

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