1. Vaccine-induced neutralizing antibodies bind to the H protein of a historical measles virus
- Author
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Anne Zemella, Kerstin Beer, Franziska Ramm, Dana Wenzel, Ariane Düx, Kevin Merkel, Sebastien Calvignac-Spencer, Daniel Stern, Martin B. Dorner, Brigitte G. Dorner, Navena Widulin, Thomas Schnalke, Cornelia Walter, Anne Wolbert, Bernhard G. Schmid, Annette Mankertz, and Sabine Santibanez
- Subjects
Measles virus hemagglutinin ,Cell-free protein synthesis ,Microsomal membranes ,Neutralizing antibodies ,Monoclonal antibodies ,Neutralizing epitopes ,Microbiology ,QR1-502 ,Other systems of medicine ,RZ201-999 - Abstract
Measles is a highly contagious airborne viral disease. It can lead to serious complications and death and is preventable by vaccination. The live-attenuated measles vaccine (LAMV) derived from a measles virus (MV) isolated in 1954 has been in use globally for six decades and protects effectively by providing a durable humoral and cell-mediated immunity. Our study addresses the temporal stability of epitopes on the viral surface glycoprotein hemagglutinin (H) which is the major target of MV-neutralizing antibodies. We investigated the binding of seven vaccine-induced MV-H-specific monoclonal antibodies (mAbs) to cell-free synthesized MV-H proteins derived from the H gene sequences obtained from a lung specimen of a fatal case of measles pneumonia in 1912 and an isolate from a current case. The binding of four out of seven mAbs to the H protein of both MV strains provides evidence of epitopes that are stable for more than 100 years. The binding of the universally neutralizing mAbs RKI-MV-12b and RKI-MV-34c to the H protein of the 1912 MV suggests the long-term stability of highly conserved epitopes on the MV surface.
- Published
- 2024
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