Academic Journal
Vaccination with a replication-defective cytomegalovirus vaccine elicits a glycoprotein B-specific monoclonal antibody repertoire distinct from natural infection
العنوان: | Vaccination with a replication-defective cytomegalovirus vaccine elicits a glycoprotein B-specific monoclonal antibody repertoire distinct from natural infection |
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المؤلفون: | Valencia, Sarah M., Rochat, Eric, Harnois, Melissa J., Dennis, Maria, Webster, Helen S., Hora, Bhavna, Kumar, Amit, Wang, Hsuan-Yuan, Li, Leike, Freed, Daniel, Zhang, Ningyan, An, Zhiqiang, Wang, Dai, Permar, Sallie R. |
المساهمون: | Merck, U.S. Department of Health & Human Services | NIH | National Institute of Allergy and Infectious Diseases, Welch Foundation |
المصدر: | npj Vaccines ; volume 8, issue 1 ; ISSN 2059-0105 |
بيانات النشر: | Springer Science and Business Media LLC |
سنة النشر: | 2023 |
الوصف: | Human Cytomegalovirus (HCMV) is the leading infectious congenital infection globally and the most common viral infection in transplant recipients, therefore identifying a vaccine for HCMV is a top priority. Humoral immunity is a correlate of protection for HCMV infection. The most effective vaccine tested to date, which achieved 50% reduction in acquisition of HCMV, was comprised of the glycoprotein B protein given with an oil-in-water emulsion adjuvant MF59. We characterize gB-specific monoclonal antibodies isolated from individuals vaccinated with a disabled infectious single cycle (DISC) CMV vaccine, V160, and compare these to the gB-specific monoclonal antibody repertoire isolated from naturally-infected individuals. We find that vaccination with V160 resulted in gB-specific antibodies that bound homogenously to gB expressed on the surface of a cell in contrast to antibodies isolated from natural infection which variably bound to cell-associated gB. Vaccination resulted in a similar breadth of gB-specific antibodies, with binding profile to gB genotypes 1–5 comparable to that of natural infection. Few gB-specific neutralizing antibodies were isolated from V160 vaccinees and fewer antibodies had identifiable gB antigenic domain specificity compared to that of naturally-infected individuals. We also show that glycosylation of gB residue N73 may shield binding of gB-specific antibodies. |
نوع الوثيقة: | article in journal/newspaper |
اللغة: | English |
DOI: | 10.1038/s41541-023-00749-0 |
الاتاحة: | http://dx.doi.org/10.1038/s41541-023-00749-0 https://www.nature.com/articles/s41541-023-00749-0.pdf https://www.nature.com/articles/s41541-023-00749-0 |
Rights: | https://creativecommons.org/licenses/by/4.0 ; https://creativecommons.org/licenses/by/4.0 |
رقم الانضمام: | edsbas.446FD281 |
قاعدة البيانات: | BASE |
DOI: | 10.1038/s41541-023-00749-0 |
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