Prefusion-Stabilized Fusion (F) Glycoprotein Vaccine Immunogens For Human Metapneumovirus

Human metapneumovirus (hMPV) infections have been shown as a common cause of upper and lower respiratory diseases such as bronchiolitis and pneumonia in young children, the elderly, and other immunocompromised individuals. Studies show that infections by the non-segmented negative strand RNA virus begin with attachment and entry of viral glycoproteins that mediate fusion with host cellular membranes. Like for the human respiratory syncytial virus (hRSV), a viral entry is initiated by the fusion (F) protein. Given its role in hMPV entry, the F protein has thus been a target for eliciting neutralizing antibodies and development of novel protein-based therapeutic vaccines.Researchers at the Vaccine Research Center (VRC) of the National Institute of Allergy and Infectious Diseases (NIAID) developed improved recombinant human metapneumovirus (hMPV) F proteins stabilized in the prefusion conformation that can elicit potent neutralizing antibodies against infection. Double and triple stabilized candidates were designed with inter-and intraprotomer disulfide mutations that increase protein production and show improved antigenic recognition by prefusion-specific antibodies. These second-generation immunogens constitute an improvement over the first generation constructs and are characterized by additional stabilization that results in optimal neutralization responses.The second-generation stabilized prefusion hMPV F immunogens may be an ideal vaccine immunogen to elicit broad potent n...
Source: NIH OTT Licensing Opportunities - Category: Research Authors: Source Type: research