Hydrophobic and Charged Residues in the Central Segment of the Measles Virus Hemagglutinin Stalk Mediate Transmission of the Fusion-Triggering Signal | Zendy

Swapna Apte-Sengupta | Zendy; Chanakha K. Navaratnarajah | Zendy; Roberto Cattaneo | Zendy

Open Access

Hydrophobic and Charged Residues in the Central Segment of the Measles Virus Hemagglutinin Stalk Mediate Transmission of the Fusion-Triggering Signal

Author(s) -

Swapna Apte-Sengupta,

Chanakha K. Navaratnarajah,

Roberto Cattaneo

Publication year - 2013

Publication title -

journal of virology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.617

H-Index - 292

eISSN - 1070-6321

pISSN - 0022-538X

DOI - 10.1128/jvi.01547-13

Subject(s) - biology , measles virus , stalk , virology , hemagglutinin (influenza) , transmission (telecommunications) , virus , lipid bilayer fusion , morbillivirus , microbiology and biotechnology , paramyxoviridae , measles , vaccination , viral disease , horticulture , electrical engineering , engineering

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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