B-cell epitopes of varicella-zoster virus glycoprotein II

B-cell epitopes of varicella-zoster virus glycoprotein II were mapped by means of solid phase ELISA, synthetic oligopeptides (constructed according to the Davison-Scott sequencing of the varicella-zoster virus genome) and sera from varicellae and herpes zoster patients. The individual pattern of ant...

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Bibliographic Details
Published in:Archives of virology 1996-01, Vol.141 (12), p.2465-2469
Main Authors: KJARTANSDOTTIR, A, LYCKE, E, NORRBY, S. R
Format: Article
Language:English
Subjects:
Adolescent
Adult
Aged
Amino Acid Sequence
Antibodies, Viral - immunology
Antigenic determinants, haptens, artificial antigens
Antigens
B-Lymphocytes - immunology
Biological and medical sciences
Chickenpox - blood
Chickenpox - genetics
Chickenpox - immunology
Epitope Mapping
Epitopes - immunology
Fundamental and applied biological sciences. Psychology
Fundamental immunology
Herpes Zoster - blood
Herpes Zoster - genetics
Herpes Zoster - immunology
Herpesvirus 3, Human - immunology
Humans
Infant
Integrin alpha2
Membrane Glycoproteins - genetics
Membrane Glycoproteins - immunology
Middle Aged
Molecular immunology
Molecular Sequence Data
Peptides - chemical synthesis
Peptides - genetics
Peptides - immunology
Varicella-zoster virus
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Description
Summary:B-cell epitopes of varicella-zoster virus glycoprotein II were mapped by means of solid phase ELISA, synthetic oligopeptides (constructed according to the Davison-Scott sequencing of the varicella-zoster virus genome) and sera from varicellae and herpes zoster patients. The individual pattern of antibody peptide binding varied considerably but at least 9 more reactive sites seemed discernible. A 31-mer-peptide corresponding to a hydrophilic segment of the glycoprotein (aa 417-447) was constructed. This peptide reacted with 2 out of 4 varicellae and 5 out of 9 zoster sera, respectively.
ISSN:0304-8608
1432-8798
DOI:10.1007/BF01718644