Vaccine-induced neutralizing antibodies bind to the H protein of a historical measles virus

• Egile Nagusiak: Anne Zemella (Egilea), Kerstin Beer (Egilea), Franziska Ramm (Egilea), Dana Wenzel (Egilea), Ariane Düx (Egilea), Kevin Merkel (Egilea), Sebastien Calvignac-Spencer (Egilea), Daniel Stern (Egilea), Martin B. Dorner (Egilea), Brigitte G. Dorner (Egilea), Navena Widulin (Egilea), Thomas Schnalke (Egilea), Cornelia Walter (Egilea), Anne Wolbert (Egilea), Bernhard G. Schmid (Egilea), Annette Mankertz (Egilea), Sabine Santibanez (Egilea)
• Formatua: Liburua
• Argitaratua: Elsevier, 2024-03-01T00:00:00Z.
• Gaiak: article
• Sarrera elektronikoa: Connect to this object online.

Gaia

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.

Alearen deskribapena

1438-4221
10.1016/j.ijmm.2024.151607