• 作者：Raffaello Cimbro^a ; ¹ ; Francis C. Peterson^b ; Qingbo Liu^a ; Christina Guzzo^a ; Peng Zhang^a ; Huiyi Miao^a ; Donald Van Ryk^a ; Xavier Ambroggio^c ; ² ; Darrell E. Hurt^c ; Luca De Gioia^d ; Brian F. Volkman^b ; Michael A. Dolan^c ; Paolo Lusso^a ; ^{plusso@niaid.nih.gov" class="auth_mail" title="E-mail the corresponding author}
• 关键词：HIV-1 ; Envelope ; Trimer ; Coreceptors ; Molecular mimicry ; Peptides ; Inhibitors ; Immune evasion
• 刊名：EBioMedicine
• 出版年：2016
• 出版时间：August 2016
• 年：2016
• 卷：10
• 期：Complete
• 页码：45-54
• 全文大小：1296 K

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Tyrosine-sulfated peptides derived from the V2 domain of HIV-1 gp120 mimic the N-terminal domain of the CCR5 coreceptor.

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Tyrosine-sulfated V2 peptides are potent and broad-spectrum inhibitors of HIV-1 infection.

Understanding how HIV-1 protects its outer envelope from the immune system may help devise effective strategies for treatment and vaccine. We derived synthetic peptides from the V2 loop of the external HIV-1 envelope glycoprotein, gp120, which contains sulfate-modified tyrosines that contribute to maintaining the envelope in an antibody-protected configuration. We found that these peptides mimic the structure and function of CCR5, a key cellular coreceptor for HIV-1, interacting with and occluding a major CCR5-binding site in gp120. Tyrosine-sulfated V2 peptides potently block HIV-1 entry and may serve as templates for the design of new antiviral inhibitors.