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Parainfluenza virus type 1 (PIV1) neuraminidase (NA) was previously shown to be an important determinant of viral pathogenicity. In order to further investigate the relationship between the biological properties of NA and its antigenic structure, we have examined the reactivity of four different murine monoclonal antibodies (mAbs) with the NA protein of the three closely related human pathogenic PIV1 strains A2, N12, and L14 and with the non-pathogenic laboratory strain Ox (which is antigenically unrelated to the former two viruses). The results obtained with the mAbs in the Western blot (immunoblot) assay were compared with those obtained with the polyclonal antibody raised against the purified NA of strain Ox. Eighteen of the 19 NA fragments which were recognized by the polyclonal antibody and by mAb EL4 (which recognizes a conformational epitope on the NA protein) were also recognized by mAb J3B10 which recognizes an epitope on the surface of the globular head region of the NA molecule. This mAb was directed towards a region which is devoid of homology between the pathogenic strains, suggesting that the antigenic sites of NA are related to its biological properties. NA from the three clinical strains and from Ox differed from each other in being immunoreactive with mAb J