Academic Journal

Vaccination with a replication-defective cytomegalovirus vaccine elicits a glycoprotein B-specific monoclonal antibody repertoire distinct from natural infection

التفاصيل البيبلوغرافية
العنوان: Vaccination with a replication-defective cytomegalovirus vaccine elicits a glycoprotein B-specific monoclonal antibody repertoire distinct from natural infection
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
الوصف
DOI:10.1038/s41541-023-00749-0