Immune Reactivity of Human Sera to the Glycoprotein B of Human Herpesvirus 7

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Published inJournal of Clinical Microbiology Vol. 40; no. 1; pp. 44 - 51
Main Authors Franti, Michael, Aubin, Jean-Thierry, De Saint-Maur, Guillemette, Kosuge, Haruhiko, Yamanishi, Koichi, Gautheret-Dejean, Agnes, Garbarg-Chenon, Antoine, Huraux, Jean-Marie, Agut, Henri
Format Journal Article
LanguageEnglish
Published Washington, DC American Society for Microbiology 01.01.2002
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Abstract Article Usage Stats Services JCM Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue JCM About JCM Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy JCM RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 0095-1137 Online ISSN: 1098-660X Copyright © 2014 by the American Society for Microbiology.   For an alternate route to JCM .asm.org, visit: JCM       
AbstractList The glycoprotein B (gB) is highly conserved among distinct human herpesvirus 7 (HHV-7) strains. Similarly to other herpesvirus glycoproteins, gB has been assumed to induce a specific human immune response. However, it did not appear as an immunodominant protein in conventional immunoblot assays. Recombinant gB, obtained from either Escherichia coli or baculovirus expression systems, did react specifically with HHV-7-seropositive sera, and the main corresponding epitopes were located in its N-terminal part. A 24-amino-acid peptide, corresponding to a predicted hydrophilicity peak and presenting no extensive homology with other betaherpesvirus glycoproteins, was selected in this region at positions 129 to 152 of the gB sequence. When tested by enzyme-linked immunosorbent assay (ELISA), this peptide specifically reacted with HHV-7-seropositive sera. This reactivity was significantly inhibited by the preincubation of sera with the peptide itself, lysates of gB-expressing cells, or lysates of HHV-7-infected cells. The reactivity was not significantly modified when sera were preincubated with lysates of either human cytomegalovirus (HCMV)- or HHV-6-infected cells. In cross-sectional studies including both children and adults, 49 out of 61 serum samples (80%) were found to be positive by HHV-7 ELISA, independent of their reactivity to HCMV. A longitudinal serological study of 17 children during the first 4 years of life showed that the level of ELISA-detected antibodies significantly decreased within a few weeks after birth and then increased in the following months, likely reflecting, respectively, the loss of maternal antibodies and the occurrence of seroconversion. These results demonstrate that gB peptide ELISA might be a useful tool for the serological study of HHV-7 infection.
Article Usage Stats Services JCM Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue JCM About JCM Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy JCM RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 0095-1137 Online ISSN: 1098-660X Copyright © 2014 by the American Society for Microbiology.   For an alternate route to JCM .asm.org, visit: JCM       
ABSTRACT The glycoprotein B (gB) is highly conserved among distinct human herpesvirus 7 (HHV-7) strains. Similarly to other herpesvirus glycoproteins, gB has been assumed to induce a specific human immune response. However, it did not appear as an immunodominant protein in conventional immunoblot assays. Recombinant gB, obtained from either Escherichia coli or baculovirus expression systems, did react specifically with HHV-7-seropositive sera, and the main corresponding epitopes were located in its N-terminal part. A 24-amino-acid peptide, corresponding to a predicted hydrophilicity peak and presenting no extensive homology with other betaherpesvirus glycoproteins, was selected in this region at positions 129 to 152 of the gB sequence. When tested by enzyme-linked immunosorbent assay (ELISA), this peptide specifically reacted with HHV-7-seropositive sera. This reactivity was significantly inhibited by the preincubation of sera with the peptide itself, lysates of gB-expressing cells, or lysates of HHV-7-infected cells. The reactivity was not significantly modified when sera were preincubated with lysates of either human cytomegalovirus (HCMV)- or HHV-6-infected cells. In cross-sectional studies including both children and adults, 49 out of 61 serum samples (80%) were found to be positive by HHV-7 ELISA, independent of their reactivity to HCMV. A longitudinal serological study of 17 children during the first 4 years of life showed that the level of ELISA-detected antibodies significantly decreased within a few weeks after birth and then increased in the following months, likely reflecting, respectively, the loss of maternal antibodies and the occurrence of seroconversion. These results demonstrate that gB peptide ELISA might be a useful tool for the serological study of HHV-7 infection.
The glycoprotein B (gB) is highly conserved among distinct human herpesvirus 7 (HHV-7) strains. Similarly to other herpesvirus glycoproteins, gB has been assumed to induce a specific human immune response. However, it did not appear as an immunodominant protein in conventional immunoblot assays. Recombinant gB, obtained from either Escherichia coli or baculovirus expression systems, did react specifically with HHV-7-seropositive sera, and the main corresponding epitopes were located in its N-terminal part. A 24-amino-acid peptide, corresponding to a predicted hydrophilicity peak and presenting no extensive homology with other betaherpesvirus glycoproteins, was selected in this region at positions 129 to 152 of the gB sequence. When tested by enzyme-linked immunosorbent assay (ELISA), this peptide specifically reacted with HHV-7- seropositive sera. This reactivity was significantly inhibited by the preincubation of sera with the peptide itself, lysates of gB-expressing cells, or lysates of HHV-7-infected cells. The reactivity was not significantly modified when sera were preincubated with lysates of either human cytomegalovirus (HCMV)- or HHV-6-infected cells. In cross-sectional studies including both children and adults, 49 out of 61 serum samples (80%) were found to be positive by HHV-7 ELISA, independent of their reactivity to HCMV. A longitudinal serological study of 17 children during the first 4 years of life showed that the level of ELISA-detected antibodies significantly decreased within a few weeks after birth and then increased in the following months, likely reflecting, respectively, the loss of maternal antibodies and the occurrence of seroconversion. These results demonstrate that gB peptide ELISA might be a useful tool for the serological study of HHV-7 infection.
Author Haruhiko Kosuge
Henri Agut
Jean-Marie Huraux
Michael Franti
Jean-Thierry Aubin
Guillemette De Saint-Maur
Agnes Gautheret-Dejean
Antoine Garbarg-Chenon
Koichi Yamanishi
AuthorAffiliation Laboratoire de Virologie, C.E.R.V.I., UPRES EA 2387, Hôpital Pitié-Salpétrière, 75651 Paris Cedex 13, 1 Laboratoire de Microbiologie, Unité de Virologie, Hôpital Armand Trousseau, 75571 Paris Cedex 12, France, 2 Department of Microbiology, Osaka University Medical School, Suita, Osaka, Japan 3
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Corresponding author. Mailing address: Laboratoire de Virologie, C.E.R.V.I., Hôpital Pitié-Salpétrière, 83 bd de l’Hôpital, 75651 Paris Cedex 13, France. Phone: 33-1-42 17 74 01. Fax: 33-1-42 17 74 11. E-mail: henri.agut@psl.ap-hop-paris.fr.
Present address: LFB, Les Ulis, 91958 Courtaboeuf Cedex, France.
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Snippet Article Usage Stats Services JCM Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley...
The glycoprotein B (gB) is highly conserved among distinct human herpesvirus 7 (HHV-7) strains. Similarly to other herpesvirus glycoproteins, gB has been...
ABSTRACT The glycoprotein B (gB) is highly conserved among distinct human herpesvirus 7 (HHV-7) strains. Similarly to other herpesvirus glycoproteins, gB has...
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StartPage 44
SubjectTerms Adult
Antibodies, Viral - blood
Antibodies, Viral - immunology
Antigens, Viral - immunology
Biological and medical sciences
Carcinogenesis, carcinogens and anticarcinogens
Child, Preschool
Enzyme-Linked Immunosorbent Assay
Fundamental and applied biological sciences. Psychology
glycoprotein B
Herpesvirus 7, Human - immunology
Human herpesvirus 7
Human viral diseases
Humans
Immune Sera - immunology
Immunoblotting
Infant
Infectious diseases
Medical sciences
Microbiology
Peptides - chemical synthesis
Peptides - immunology
Recombinant Proteins - genetics
Recombinant Proteins - immunology
Roseolovirus Infections - diagnosis
Roseolovirus Infections - immunology
Tumors
Viral diseases
Viral diseases of the lymphoid tissue and the blood. Aids
Viral Envelope Proteins - chemistry
Viral Envelope Proteins - genetics
Viral Envelope Proteins - immunology
Virology
Viruses
Title Immune Reactivity of Human Sera to the Glycoprotein B of Human Herpesvirus 7
URI http://jcm.asm.org/content/40/1/44.abstract
https://www.ncbi.nlm.nih.gov/pubmed/11773091
https://search.proquest.com/docview/18238528
https://search.proquest.com/docview/71351731
https://pubmed.ncbi.nlm.nih.gov/PMC120084
Volume 40
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