Detection of human serum antibodies against type-specifically reactive peptides from the N-terminus of glycoprotein B of herpes simplex virus type 1 and type 2 by surface plasmon resonance
Autor: | Bodo R. Eing, Burkhard Fleckenstein, Joachim E. Kühn, Claus Wittekindt, Karl-Heinz Wiesmüller |
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Rok vydání: | 2000 |
Předmět: |
Herpesvirus 2
Human viruses Immunoblotting Enzyme-Linked Immunosorbent Assay Peptide Herpesvirus 1 Human Biology Antibodies Viral medicine.disease_cause Virus Serology Blood serum Antigen Virology medicine Humans Amino Acid Sequence Surface plasmon resonance Antigens Viral Glycoproteins chemistry.chemical_classification Herpes Simplex Surface Plasmon Resonance Molecular biology Peptide Fragments Herpes simplex virus chemistry Glycoprotein Sequence Alignment |
Zdroj: | Journal of Virological Methods. 87:133-144 |
ISSN: | 0166-0934 |
DOI: | 10.1016/s0166-0934(00)00160-9 |
Popis: | A single-step surface plasmon resonance protocol for the detection of antibodies against herpes simplex virus type 1 and type 2 (HSV-1, HSV-2) in human sera was established using the BIAcore system. Two peptides from corresponding segments of the N-terminus of HSV-1 and HSV-2 glycoprotein B (gB), i.e. peptide gB-1 (60–73) (GAAPTGDPKPKKNK) and peptide gB-2 (55–68) (SPATTKARKRKTKK), were identified as immunogenic. Employing both peptides as diagnostic antigens in the surface plasmon resonance assay, a sensitivity for the detection of HSV-1 and HSV-2 type-specific antibodies of 83 and 86%, respectively, was achieved as compared with immunoblotting as a reference method. Peptide gB-1 (60–73) allowed the discrimination between HSV-1 and HSV-2 type-specific antibodies with a specificity of 67%, whereas peptide gB-2 (55–68) reacted in a strictly HSV-2 type-specific manner. It is concluded that peptides from the N-terminus of gB-1 and gB-2 are recognized predominantly by human sera in an HSV-specific manner. Peptide gB-2 (55–68) can be employed successfully for the determination of type-specific antibodies against HSV-2. |
Databáze: | OpenAIRE |
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