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Characterization of the Fusion and Attachment Glycoproteins of Human Metapneumovirus and Human Serosurvey to Determine Reinfection Rates

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Technical Report

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Uniformed Services University Of The Health Sciences Bethesda United States

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Human metapneumovirus hMPV is a newly discovered virus that causes acute respiratory illness. It is found worldwide and most people are exposed before 5 years of age. It can cause severe illness and even death at extremes of age, and in those with immunocompromising states and underlying illnesses. Immunity after natural or experimental infection with hMPV is not lasting, although neutralizing antibodies develop to the virus. We have prepared and characterized soluble versions of the fusion F and attachment G surface glycoproteins of hMPV to further assess the ability of these viral components to induce and detect antibodies. Size exclusion chromatography and sucrose gradient analysis revealed that the sG glycoprotein is a dimer, and the sF glycoprotein a monomer, although other reported sF glycoproteins are trimers. Hamsters, rabbits and non-human primates immunized with hMPV develop antibodies reactive toboth the monomeric and trimeric sF glycoproteins, and animals immunized with the same genotype as the sG glycoprotein also demonstrate antibodies to sG, although at much lower levels than sF. Non-human primates immunized with hMPV do not develop cross reactive antibodies to respiratory syncytial virus RSV, the most closely related human viral pathogen.

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