Analysis Biomolecular Interactions of Biotinylated Monomeric hMPV B2 F protein with Fabs (MPV458) by BLI (CAT#: STEM-MB-0125-CJ)

Introduction

Human metapneumovirus (hMPV) is a leading cause of viral respiratory infections in children, the majority of whom are seropositive for hMPV by five years of age. Although hMPV was discovered in 2001, there are no vaccines or therapeutics approved to prevent or treat viral infection. Similar to other respiratory pathogens, children, the elderly, and the immunocompromised are the major groups for which hMPV infection may require hospitalization. In addition, fatal hMPV has been observed in one child during an outbreak of hMPV in a daycare center. hMPV is also a significant cause of febrile respiratory illness in HIV-infected patients, and has been linked to exacerbations of chronic obstructive pulmonary disease. Co-circulation of hMPV was observed during the SARS outbreak of 2003, and similar observations have been made during the current SARS-CoV-2 pandemic, suggesting hMPV interacts with other circulating respiratory viruses.

hMPV circulates as two genotypes, A and B, and based on the sequence variability of the surface proteins, hMPV is further grouped into four subgroups, A1, A2, B1, and B2. hMPV has three surface glycoproteins, the small hydrophobic (SH), the attachment (G), and the fusion (F) proteins. The hMPV F protein contains a single site that is cleaved to convert the polypeptide F0 protein into the meta-stable disulfide-linked F1-F2 pre-fusion homotrimer. For hMPV F, the preponderance of hMPV F-specific human antibodies bind both pre-fusion and post-fusion F conformations, which has been proposed is due to differential glycan positioning on the head of the hMPV F protein.