Harris et al. show that the envelope glycoproteins of a rare HIV-2UC1 strain evolved to balance low affinity to the CD4 receptor with an improved, long-lived, and readily triggerable molecular machinery to mediate virus entry.
Bibliographical noteFunding Information:
We thank Eva Perez-Greene for helping to prepare the revised manuscript, as well as Paula Cannon and Nick Llewellyn for providing the HIV-2 ROD10 and HIV-2 ROD14 Env-expressing plasmids. A.H. is the recipient of an amfAR Mathilde Krim Fellowship in Basic Biomedical Research ( 108501-53-RKNT ) and a phase II amfAR research grant ( 109285-58-RKVA ) for independent investigators. This work was supported by internal funds of the Department of Medicine at the University of Minnesota and by NIH/NIDA grant 1DP2DA049279-01 (to A.H.). N.T. was supported by NIH F32 DA007097 , and L.M.M. was supported by NIH R01 AI150468 . Molecular graphics and analyses were performed with UCSF Chimera, which is supported by NIH P41-GM103311 . The content is solely the responsibility of the authors and does not necessarily represent the official views of the NIH.
© 2020 The Author(s)
- HIV envelope glycoproteins
- binding kinetics
- long-lived activation state
- molecular mechanism of HIV entry
PubMed: MeSH publication types
- Journal Article
- Research Support, N.I.H., Extramural
- Research Support, Non-U.S. Gov't