Human Metapneumovirus (hMPV) belongs to the genus Metapneumovirus of the family Paramyxoviridae, which is an enveloped single-stranded negative-sense RNA virus. First isolated and identified from respiratory tract infection patient samples in 2001, this virus has an evolutionary origin related to avian metapneumovirus and formed strains specifically infecting humans after long-term species adaptation. hMPV has high host specificity, mainly infecting human respiratory epithelial cells, and is distributed in human populations worldwide. There are certain differences in genome sequences of strains from different regions, but the homology of core genes is relatively high. As a typical member of the Paramyxoviridae family, the core biological characteristics of hMPV include relying on the host cell's transcription and translation system for replication, being easy to survive in low-temperature environments, and the viral genome having a certain degree of variability, which can produce different genotypes through gene mutation.

hMPV viral particles are spherical or pleomorphic with a diameter of approximately 150-300 nm, and their structure consists of an envelope, a matrix protein layer, and a nucleocapsid from the outside to the inside. The outermost layer is a lipid bilayer envelope derived from the host cell membrane, embedded with three key glycoproteins: fusion protein (F protein), attachment protein (G protein), and small hydrophobic protein (SH protein). Among them, the F protein is responsible for mediating the fusion process between the viral envelope and the host cell membrane, the G protein is involved in the specific recognition and binding of the virus to the host cell, and the specific function of the SH protein has not been fully clarified, which is speculated to be involved in regulating the host's immune response. The inner side of the envelope is a matrix layer composed of M protein, which can maintain the morphological stability of the viral particles and provide a structural connection between the envelope and the nucleocapsid. The nucleocapsid has a helical symmetric structure, formed by the tight combination of nucleoprotein (N protein), phosphorylated protein (P protein), large protein (L protein), transcription elongation factor (M2-1 protein) and viral genomic RNA. Among them, the L protein has RNA polymerase activity and is a core enzyme for viral genome replication and transcription. The full length of the hMPV genome is approximately 13 kb, containing 8 open reading frames, which sequentially encode eight proteins: N, P, M, F, M2, SH, G, and L. The gene arrangement order has the typical characteristics of the Paramyxoviridae family.

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