Hydrophobic and charged residues in the central segment of the measles virus hemagglutinin stalk mediate transmission of the fusion-triggering signal

Swapna Apte-Sengupta, Chanakha K. Navaratnarajah, Roberto Cattaneo

Research output: Contribution to journalArticle

16 Citations (Scopus)

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.

Original languageEnglish (US)
Pages (from-to)10401-10404
Number of pages4
JournalJournal of Virology
Volume87
Issue number18
DOIs
StatePublished - 2013

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Measles virus
Hemagglutinins
hemagglutinins
Virus Internalization
Proteins
proteins
Periodicity
periodicity
receptors

ASJC Scopus subject areas

  • Immunology
  • Virology

Cite this

Hydrophobic and charged residues in the central segment of the measles virus hemagglutinin stalk mediate transmission of the fusion-triggering signal. / Apte-Sengupta, Swapna; Navaratnarajah, Chanakha K.; Cattaneo, Roberto.

In: Journal of Virology, Vol. 87, No. 18, 2013, p. 10401-10404.

Research output: Contribution to journalArticle

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