TY - JOUR
T1 - Hydrophobic and charged residues in the central segment of the measles virus hemagglutinin stalk mediate transmission of the fusion-triggering signal
AU - Apte-Sengupta, Swapna
AU - Navaratnarajah, Chanakha K.
AU - Cattaneo, Roberto
PY - 2013
Y1 - 2013
N2 - 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.
AB - 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.
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U2 - 10.1128/JVI.01547-13
DO - 10.1128/JVI.01547-13
M3 - Article
C2 - 23864629
AN - SCOPUS:84883261324
SN - 0022-538X
VL - 87
SP - 10401
EP - 10404
JO - Journal of virology
JF - Journal of virology
IS - 18
ER -