Localization of a Domain on the Paramyxovirus Attachment Protein Required for the Promotion of Cellular Fusion by Its Homologous Fusion Protein Spike

• Published in: Virology (New York, N.Y.) N.Y.), 1995-06, Vol.209 (2), p.457-469
• Main Authors: Deng, Ruitang, Wang, Zhiyu, Mirza, Anne M., Iorio, Ronald M.
• Format: Article
• Language: English
• Subjects: Animals; Base Sequence; Cell Fusion; Cell Line; Cricetinae; DNA Primers; HN Protein - biosynthesis; HN Protein - metabolism; Kidney; Molecular Sequence Data; Mutagenesis, Site-Directed; Oligodeoxyribonucleotides; parainfluenza virus; paramyxovirus; Receptors, Virus - metabolism; Recombinant Fusion Proteins - biosynthesis; Recombinant Fusion Proteins - metabolism; Respirovirus - physiology; Restriction Mapping; Substrate Specificity; Viral Fusion Proteins - biosynthesis; Viral Fusion Proteins - metabolism
• ISSN: 0042-6822; 1096-0341
• DOI: 10.1006/viro.1995.1278

The promotion of membrane fusion by the paramyxovirus hemagglutinin-neuraminidase (HN) and fusion (F) proteins requires that they be derived from homologous viruses, suggesting the possibility that the promotion of fusion requires a virus-specific communication between the two glycoprotein spikes. We have evaluated the ability of chimeric HN proteins, composed of domains from the HN proteins of two heterologous members of the group, human parainfluenza virus 3 (bPIV3) and Newcastle disease virus (NDV), to complement the F protein of each virus in the promotion of fusion. Specificity for the F protein of hPIV3 segregates with a segment composed of the transmembrane anchor and the first 82 residues of the ectodomain of its HN protein. Specificity of NDV HN for its homologous F protein is determined by a similar domain. These findings suggest that determinants specific to this segment of the attachment protein spike may be involved in the triggering of the fusion process.