DIFFERENT ANTIBODY-RESPONSE TO A NEUTRALIZING EPITOPE OF HUMAN CYTOMEGALOVIRUS GLYCOPROTEIN-B AMONG SEROPOSITIVE INDIVIDUALS

被引：12
作者：
AYATA, M
SUGANO, T
MURAYAMA, T
SAKAMURO, D
TAKEGAMI, T
MATSUMOTO, Y
FURUKAWA, T
机构：
[1] KANAZAWA MED UNIV, DEPT MICROBIOL, ISHIKAWA, JAPAN
[2] KANAZAWA MED UNIV, MED RES INST, DIV TROP MED, ISHIKAWA, JAPAN
[3] TEIJIN INST BIOMED RES, TOKYO, JAPAN
来源：
JOURNAL OF MEDICAL VIROLOGY | 1994年 / 43卷 / 04期
关键词：
CYTOMEGALOVIRUS IMMUNOLOGY; DIFFERENT RESPONSE; FUSION PROTEIN;
D O I：
10.1002/jmv.1890430412
中图分类号：
Q93 [微生物学];
学科分类号：
071005 ; 100705 ;
摘要：
The amino-terminal portion of human cytomegalovirus 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 peptide 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. (C) 1994 Wiley-Liss, Inc.
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收藏
页码：386 / 392
页数：7
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