Structural basis of synergistic neutralization of Crimean-Congo hemorrhagic fever virus by human antibodies
Author(s) -
Akaash K. Mishra,
Jan Hellert,
Natália Freitas,
Pablo GuardadoCalvo,
Ahmed Haouz,
J. Maximilian Fels,
Daniel P. Maurer,
Dafna M. Abelson,
Zachary A. Bornholdt,
Laura M. Walker,
Kartik Chandran,
FrançoisLoïc Cosset,
Jason S. McLellan,
F.A. Rey
Publication year - 2022
Publication title -
science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 12.556
H-Index - 1186
eISSN - 1095-9203
pISSN - 0036-8075
DOI - 10.1126/science.abl6502
Subject(s) - virology , antibody , crimean–congo hemorrhagic fever , virus , neutralization , glycoprotein , tick , lipid bilayer fusion , biology , antigen , immunology , microbiology and biotechnology
A block to viral cell entry Crimean-Congo hemorrhagic fever virus is a tickborne virus that can cause severe disease and even death in humans. Disease occurrence is linked to the geographic range of the tick vector, and climate change may increase this range. Infection of host cells requires the fusion glycoprotein Gc, which is the main target of neutralizing antibodies. Mishraet al . build on previous work that identified a combination of two Gc-targeting antibodies that gave postexposure protection in an animal model. The authors determined the structure of the antigen-binding fragments of the two antibodies bound to a prefusion form of Gc and also the structure of Gc after the conformational change into the trimeric postfusion form. The structures show how the antibodies work together to block membrane fusion. —VV
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom