A toggle switch controls the low pH-triggered rearrangement and maturation of the dengue virus envelope proteins

Aihua Zheng, Fei Yuan, Lara M. Kleinfelter and Margaret Kielian ()
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Aihua Zheng: Albert Einstein College of Medicine
Fei Yuan: Albert Einstein College of Medicine
Lara M. Kleinfelter: Albert Einstein College of Medicine
Margaret Kielian: Albert Einstein College of Medicine

Nature Communications, 2014, vol. 5, issue 1, 1-9

Abstract: Abstract Immature dengue virus particles undergo a dramatic conformational change upon exposure to the acidic environment of the late secretory pathway. The interactions of the E fusion proteins and prM chaperone proteins on the virus envelope are reorganized to permit prM processing by a host protease, furin, thus priming virus for fusion and infection. Here we identify a pH-dependent toggle switch that controls this key conformational change during virus maturation. Our data show that the M region of prM interacts with E at neutral pH but is released at acidic pH, while the pr region interacts with E at acidic pH but is released at neutral pH. Alanine substitution of the conserved residue H98 in prM disrupts the switch by inhibiting dissociation of M from E at low pH, resulting in impaired prM processing and decreased virus infectivity. Thus, release of M–E interaction at low pH promotes formation of a furin-accessible intermediate.

Date: 2014
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DOI: 10.1038/ncomms4877

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