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Different antibody response to a neutralizing epitope of human cytomegalovirus glycoprotein B among seropositive individuals
Author(s) -
Ayata Minoru,
Sugano Tohru,
Murayama Tsugiya,
Sakamuro Daitoku,
Takegami Tsutomu,
Matsumoto YohIchi,
Furukawa Toru
Publication year - 1994
Publication title -
journal of medical virology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 121
eISSN - 1096-9071
pISSN - 0146-6615
DOI - 10.1002/jmv.1890430412
Subject(s) - epitope , immunogenicity , virology , monoclonal antibody , human cytomegalovirus , linear epitope , antibody , glycoprotein , biology , neutralizing antibody , epitope mapping , immune system , microbiology and biotechnology , virus , immunology
The amino‐terminal portion of human cytomeg‐alovirus glycoprotein B (HCMV‐gB) was expressed as a fusion protein to analyze the neutralizing epitope recognized by human monoclonal antibody C23 and the humoral immune response to this epitope. The linear neutralizing epitope was further localized to the pep‐tide within 17 amino acids (position 68‐84) which were conserved between two HCMV laboratory strains. Ten out of 17 HCMV‐seropositive human sera contained the antibody against this epitope. Although seven sera were negative for reacting with the fusion protein, the viruses isolated from the same patients retained the epitope. The immunogenicity of the epitope and the possible application of C23 human monoclonal antibody for passive immunization against HCMV infections are discussed. © 1994 Wiley‐Liss, Inc.