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Fine specificity and neutralizing activity of human serum antibodies directed to the major antigenic region on gp 116 of human cytomegalovirus

Silvestri, M.; Jäderling, F.; Rudén, U.; Ohlin, M. LU and Sundqvist, V. A. (1993) In Serodiagnosis and Immunotherapy in Infectious Disease 5(4). p.209-216
Abstract

The human antibody response to the conserved neutralization-related site on the gp 116 of human cytomegalovirus (HCMV) was investigated in healthy blood donors by the use of synthetic peptides. Anti-HCMV positive sera investigated in ELISA gave a reactivity of 48-56% with the peptide T7-13 (amino acids (aa) 67-86). Though epitope mapping revealed several individual fine specificities within this region, the average reactivity pattern was similar to that of the human monoclonal antibody (MAb) ITC88, the binding of which has been localized to aa 69-80. By the use of superparamagnetic Dynabeads coated with the peptide T7-13, serum antibodies were affinity isolated and the neutralizing activity was investigated. A clear reduction in... (More)

The human antibody response to the conserved neutralization-related site on the gp 116 of human cytomegalovirus (HCMV) was investigated in healthy blood donors by the use of synthetic peptides. Anti-HCMV positive sera investigated in ELISA gave a reactivity of 48-56% with the peptide T7-13 (amino acids (aa) 67-86). Though epitope mapping revealed several individual fine specificities within this region, the average reactivity pattern was similar to that of the human monoclonal antibody (MAb) ITC88, the binding of which has been localized to aa 69-80. By the use of superparamagnetic Dynabeads coated with the peptide T7-13, serum antibodies were affinity isolated and the neutralizing activity was investigated. A clear reduction in infectivity was seen only with antibodies from one out of four sera and this serum exhibited a fine specificity nearly identical to that of MAb ITC88. A complete adsorption of antibodies to this site was not achieved, yet the results imply that antibodies against this region do not constitute a major part of the HCMV-neutralizing activity in human serum. The potent complement-independent neutralizing activity of antibodies directed to this site nevertheless suggests that it will contribute beneficially to a subunit vaccine. © 1993.

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author
organization
publishing date
type
Contribution to journal
publication status
published
keywords
affinity isolation, antibody fine specificity, Dynabeads, ELISA, gB, gp 116, human cytomegalovirus, neutralizing antibodies, synthetic peptides
in
Serodiagnosis and Immunotherapy in Infectious Disease
volume
5
issue
4
pages
8 pages
publisher
Academic Press Inc.
external identifiers
  • Scopus:0027725222
ISSN
0888-0786
DOI
10.1016/0888-0786(93)90004-J
language
English
LU publication?
yes
id
d6757c4a-0cc3-4a00-a6cd-916612d3fafa
date added to LUP
2016-04-19 14:15:47
date last changed
2016-04-22 13:31:56
@misc{d6757c4a-0cc3-4a00-a6cd-916612d3fafa,
  abstract     = {<p>The human antibody response to the conserved neutralization-related site on the gp 116 of human cytomegalovirus (HCMV) was investigated in healthy blood donors by the use of synthetic peptides. Anti-HCMV positive sera investigated in ELISA gave a reactivity of 48-56% with the peptide T7-13 (amino acids (aa) 67-86). Though epitope mapping revealed several individual fine specificities within this region, the average reactivity pattern was similar to that of the human monoclonal antibody (MAb) ITC88, the binding of which has been localized to aa 69-80. By the use of superparamagnetic Dynabeads coated with the peptide T7-13, serum antibodies were affinity isolated and the neutralizing activity was investigated. A clear reduction in infectivity was seen only with antibodies from one out of four sera and this serum exhibited a fine specificity nearly identical to that of MAb ITC88. A complete adsorption of antibodies to this site was not achieved, yet the results imply that antibodies against this region do not constitute a major part of the HCMV-neutralizing activity in human serum. The potent complement-independent neutralizing activity of antibodies directed to this site nevertheless suggests that it will contribute beneficially to a subunit vaccine. © 1993.</p>},
  author       = {Silvestri, M. and Jäderling, F. and Rudén, U. and Ohlin, M. and Sundqvist, V. A.},
  issn         = {0888-0786},
  keyword      = {affinity isolation,antibody fine specificity,Dynabeads,ELISA,gB,gp 116,human cytomegalovirus,neutralizing antibodies,synthetic peptides},
  language     = {eng},
  number       = {4},
  pages        = {209--216},
  publisher    = {ARRAY(0x944dc00)},
  series       = {Serodiagnosis and Immunotherapy in Infectious Disease},
  title        = {Fine specificity and neutralizing activity of human serum antibodies directed to the major antigenic region on gp 116 of human cytomegalovirus},
  url          = {http://dx.doi.org/10.1016/0888-0786(93)90004-J},
  volume       = {5},
  year         = {1993},
}