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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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| Published in: | Archives of virology 1996-01, Vol.141 (12), p.2465-2469 |
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| Main Authors: | , , |
| Format: | Article |
| Language: | English |
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| cites | cdi_FETCH-LOGICAL-c378t-240d0cb51ca01e75f99a50df3dcd6877437d9fd39a09a8975ff94cb4c1b6d9e63 |
| container_end_page | 2469 |
| container_issue | 12 |
| container_start_page | 2465 |
| container_title | Archives of virology |
| container_volume | 141 |
| creator | KJARTANSDOTTIR, A LYCKE, E NORRBY, S. R |
| description | 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. |
| doi_str_mv | 10.1007/BF01718644 |
| format | article |
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R</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>B-cell epitopes of varicella-zoster virus glycoprotein II</atitle><jtitle>Archives of virology</jtitle><addtitle>Arch Virol</addtitle><date>1996-01-01</date><risdate>1996</risdate><volume>141</volume><issue>12</issue><spage>2465</spage><epage>2469</epage><pages>2465-2469</pages><issn>0304-8608</issn><eissn>1432-8798</eissn><abstract>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. 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| fulltext | fulltext |
| identifier | ISSN: 0304-8608 |
| ispartof | Archives of virology, 1996-01, Vol.141 (12), p.2465-2469 |
| issn | 0304-8608 1432-8798 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_78763997 |
| source | Springer Nature - Connect here FIRST to enable access |
| 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 |
| title | B-cell epitopes of varicella-zoster virus glycoprotein II |
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