title: Hydrophobic and charged residues in the central segment of the measles virus hemagglutinin stalk mediate transmission of the fusion-triggering signal.
abstract: The pH-independent measles virus membrane fusion process begins when the attachment protein H binds to a receptor. Knowing that the central segment of the tetrameric H stalk transmits the signal to the fusion protein trimer, we investigated how. We document that exact conservation of most residues in the 92 through 99 segment is essential for function. In addition, hydrophobic and charged residues in the 104 through 125 segment, arranged with helical periodicity, are critical for F protein interactions and signal transmission.
authors.affiliation: Department of Molecular Medicine, Mayo Clinic, and Virology and Gene Therapy Track, Mayo Graduate School, Rochester, Minnesota, USA.
authors.forename: Swapna
authors.initials: S
authors.lastname: Apte-Sengupta
authors.forename: Chanakha K
authors.initials: CK
authors.lastname: Navaratnarajah
authors.forename: Roberto
authors.initials: R
authors.lastname: Cattaneo
mesh_terms: D019943:Amino Acid Substitution; D004252:DNA Mutational Analysis; D008459:Measles virus / Q000502:physiology*; D011485:Protein Binding; D025941:Protein Interaction Mapping; D014760:Viral Fusion Proteins / Q000378:metabolism; D014764:Viral Proteins / Q000235:genetics / Q000378:metabolism*; D053586:Virus Internalization
chemical_list: D014760:Viral Fusion Proteins; D014764:Viral Proteins