Measles morbillivirus surface glycoproteins (MeV H and F)

The Measles morbillivirus surface glycoproteins, comprising the hemagglutinin (H) and fusion (F) proteins, are essential components of the viral envelope that mediate host cell entry. The H protein functions as the attachment factor, binding to cellular receptors such as signaling lymphocytic activation molecule (SLAM/CD150), nectin-4, and CD46. This binding event triggers a conformational change in the H protein that is transmitted to the F protein, which then undergoes a dramatic structural rearrangement from a metastable prefusion state to a stable postfusion state. This process facilitates the fusion of the viral and host cell membranes, allowing the viral ribonucleocapsid to enter the cytoplasm. These glycoproteins are the primary targets for neutralizing antibodies and are the basis for current live-attenuated vaccines. Therapeutic strategies under development include small-molecule fusion inhibitors like AS-48 and 3g, as well as peptides like FIP and neutralizing antibodies like mAb77, which aim to stabilize the prefusion state or block the fusion cascade.

Other names

Measles virus envelope glycoproteinsMeasles virus H and F proteinsHemagglutinin and Fusion proteinsMeV surface glycoproteins

Inhibition of viral attachment to host receptors and stabilization of the fusion protein in its prefusion state to prevent membrane fusion.