Volume 43, Issue 4 pp. 386-392
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Different antibody response to a neutralizing epitope of human cytomegalovirus glycoprotein B among seropositive individuals

Minoru Ayata

Minoru Ayata

Department of Microbiology, Medical Research Institute, Kanazawa Medical University, Ishikawa, Tokyo, Japan

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Tohru Sugano

Tohru Sugano

Teijin Institute for Biomedical Research, Tokyo, Japan

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Tsugiya Murayama

Tsugiya Murayama

Department of Microbiology, Medical Research Institute, Kanazawa Medical University, Ishikawa, Tokyo, Japan

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Daitoku Sakamuro

Daitoku Sakamuro

Department of Microbiology, Medical Research Institute, Kanazawa Medical University, Ishikawa, Tokyo, Japan

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Tsutomu Takegami

Tsutomu Takegami

Division of Tropical Medicine, Medical Research Institute, Kanazawa Medical University, Ishikawa, Tokyo, Japan

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Yoh-Ichi Matsumoto

Yoh-Ichi Matsumoto

Teijin Institute for Biomedical Research, Tokyo, Japan

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Toru Furukawa M.D.

Corresponding Author

Toru Furukawa M.D.

Department of Microbiology, Medical Research Institute, Kanazawa Medical University, Ishikawa, Tokyo, Japan

Department of Microbiology, Kanazawa Medical University, Ishikawa, Japan===Search for more papers by this author
First published: August 1994
Citations: 10

Abstract

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.

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