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- W2791563806 abstract "We recently identified 2 sulfated tyrosines, Tys173 and Tys177, in the second variable (V2) region of HIV-1 gp120 and shown that they play a role in stabilizing the pre-fusion conformation of the envelope trimer. The sulfated region of V2 has a high similarity with the N-terminal domain of CCR5, which also contains sulfated tyrosines and interacts with V3-loop base of gp120, suggesting a potential intramolecular interaction mode between V2 and V3. Here, we employed a tyrosine- sulfated V2-derived peptide, pV2alpha-Tys, to investigate binding to gp120 and its functional consequences. A direct interaction was observed between peptide pV2alpha-Tys and the base of V3, with Tys177 playing a dominant role. Surface plasmon resonance showed that binding of the pV2alpha-Tys is enhanced by CD4-induced conformational changes in gp120, and the effect is even more significant with a soluble trimer. Functionally, pV2alpha-Tys inhibits HIV-1 entry and fusion by preventing CCR5 utilization, with a potency comparable to that of a sulfated CCR5 N-terminal peptide, pCCR5-Tys. These studies characterize the structural and functional features of the V2–V3 intramolecular interaction, providing new leads for the design of therapeutic and vaccine strategies for the control of HIV/AIDS." @default.
- W2791563806 created "2018-03-29" @default.
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- W2791563806 date "2016-01-01" @default.
- W2791563806 modified "2023-09-27" @default.
- W2791563806 title "P-D4 Tyrosine-sulfated peptides from the gp120 V2 domain block HIV-1 entry through CCR5 Mimicry" @default.
- W2791563806 doi "https://doi.org/10.1097/01.qai.0000479629.55268.bb" @default.
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