Slow Receptor Binding of the Noncytopathic HIV-2UC1 Envs Is Balanced by Long-Lived Activation State and Efficient Fusion Activity

Miranda Harris, Sneha Ratnapriya, Angela Chov, Héctor Cervera, Alisha Block, Christopher Gu, Nathaniel Talledge, Louis M. Mansky, Joseph Sodroski, Alon Herschhorn

Research output: Contribution to journalArticlepeer-review


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.

Original languageEnglish (US)
Article number107749
JournalCell reports
Issue number10
StatePublished - Jun 9 2020

Bibliographical note

Funding 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.

Publisher Copyright:
© 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

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