title: Peptides derived from HIV-1 gp120 co-receptor binding domain form amyloid fibrils and enhance HIV-1 infection.
abstract: Amyloid fibrils play important roles in HIV-1 infection. We found peptides derived from the HIV-1 gp120 co-receptor binding region, which are defined as enhancing peptides (EPs), could form amyloid fibrils and remarkably enhance HIV-1 infection. EPs bound to the virus and promoted the interaction between HIV-1 and target cells. The antiviral efficacy of antiretroviral drugs (ARVs) was substantially impaired in the presence of EPs. Epigallocatechin gallate (EGCG) could both inhibit the formation of fibrils composed of EPs and counteract the EP-mediated enhancement of HIV-1 infection. Our findings identify viral derived amyloid fibrils that hold potential for biochemical applications.
authors.affiliation: School of Pharmaceutical Sciences, Southern Medical University, Guangzhou, Guangdong, China; Lindsley F. Kimball Research Institute, New York Blood Center, New York, USA.
authors.forename: Suiyi
authors.initials: S
authors.lastname: Tan
authors.affiliation: School of Pharmaceutical Sciences, Southern Medical University, Guangzhou, Guangdong, China; Lindsley F. Kimball Research Institute, New York Blood Center, New York, USA.
authors.forename: Lin
authors.initials: L
authors.lastname: Li
authors.affiliation: Lindsley F. Kimball Research Institute, New York Blood Center, New York, USA; Key Laboratory of Medical Molecular Virology of the Ministries of Education & Health, Shanghai Medical College and Institute of Medical Microbiology, Fudan University, Shanghai, China.
authors.forename: Lu
authors.initials: L
authors.lastname: Lu
authors.affiliation: Lindsley F. Kimball Research Institute, New York Blood Center, New York, USA.
authors.forename: Chungen
authors.initials: C
authors.lastname: Pan
authors.affiliation: Lindsley F. Kimball Research Institute, New York Blood Center, New York, USA.
authors.forename: Hong
authors.initials: H
authors.lastname: Lu
authors.affiliation: Lindsley F. Kimball Research Institute, New York Blood Center, New York, USA.
authors.forename: Yelena
authors.initials: Y
authors.lastname: Oksov
authors.affiliation: School of Pharmaceutical Sciences, Southern Medical University, Guangzhou, Guangdong, China.
authors.forename: Xiaojuan
authors.initials: X
authors.lastname: Tang
authors.affiliation: School of Pharmaceutical Sciences, Southern Medical University, Guangzhou, Guangdong, China; Lindsley F. Kimball Research Institute, New York Blood Center, New York, USA; Key Laboratory of Medical Molecular Virology of the Ministries of Education & Health, Shanghai Medical College and Institute of Medical Microbiology, Fudan University, Shanghai, China. Electronic address: shibojiang@fudan.edu.cn.
authors.forename: Shibo
authors.initials: S
authors.lastname: Jiang
authors.affiliation: School of Pharmaceutical Sciences, Southern Medical University, Guangzhou, Guangdong, China. Electronic address: liusw@smu.edu.cn.
authors.forename: Shuwen
authors.initials: S
authors.lastname: Liu
mesh_terms: D000595:Amino Acid Sequence; D000682:Amyloid; D019380:Anti-HIV Agents / Q000494:pharmacology; D002392:Catechin / Q000031:analogs & derivatives / Q000494:pharmacology; D002460:Cell Line; D015699:HIV Envelope Protein gp120 / Q000737:chemistry* / Q000502:physiology; D015658:HIV Infections / Q000821:virology*; D015497:HIV-1 / Q000187:drug effects / Q000502:physiology*; D006801:Humans; D020128:Inhibitory Concentration 50; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry* / Q000502:physiology; D054730:Protein Interaction Domains and Motifs; D053586:Virus Internalization
chemical_list: D000682:Amyloid; D019380:Anti-HIV Agents; D015699:HIV Envelope Protein gp120; D010446:Peptide Fragments; C514793:gp120 protein, Human immunodeficiency virus 1; D002392:Catechin; C045651:epigallocatechin gallate
keywords: Amyloid fibrils; Antiretroviral drugs; EGCG; Enhancement of HIV-1 infection; HIV-1 gp120