Peptides derived from HIV-1 gp120 co-receptor binding domain form amyloid fibrils and enhance HIV-1 infection

Suiyi Tan; Lin Li; Lu Lu; Chungen Pan; Hong Lu; Yelena Oksov; Xiaojuan Tang; Shibo Jiang; Shuwen Liu

doi:10.1016/j.febslet.2014.03.016

Peptides derived from HIV-1 gp120 co-receptor binding domain form amyloid fibrils and enhance HIV-1 infection

FEBS Lett. 2014 May 2;588(9):1515-22. doi: 10.1016/j.febslet.2014.03.016. Epub 2014 Mar 18.

Authors

Suiyi Tan¹, Lin Li¹, Lu Lu², Chungen Pan³, Hong Lu³, Yelena Oksov³, Xiaojuan Tang⁴, Shibo Jiang⁵, Shuwen Liu⁶

Affiliations

¹ School of Pharmaceutical Sciences, Southern Medical University, Guangzhou, Guangdong, China; Lindsley F. Kimball Research Institute, New York Blood Center, New York, USA.
² 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.
³ Lindsley F. Kimball Research Institute, New York Blood Center, New York, USA.
⁴ School of Pharmaceutical Sciences, Southern Medical University, Guangzhou, Guangdong, China.
⁵ 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: [email protected].
⁶ School of Pharmaceutical Sciences, Southern Medical University, Guangzhou, Guangdong, China. Electronic address: [email protected].

PMID: 24657436
DOI: 10.1016/j.febslet.2014.03.016

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.

Keywords: Amyloid fibrils; Antiretroviral drugs; EGCG; Enhancement of HIV-1 infection; HIV-1 gp120.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amino Acid Sequence
Amyloid
Anti-HIV Agents / pharmacology
Catechin / analogs & derivatives
Catechin / pharmacology
Cell Line
HIV Envelope Protein gp120 / chemistry*
HIV Envelope Protein gp120 / physiology
HIV Infections / virology*
HIV-1 / drug effects
HIV-1 / physiology*
Humans
Inhibitory Concentration 50
Molecular Sequence Data
Peptide Fragments / chemistry*
Peptide Fragments / physiology
Protein Interaction Domains and Motifs
Virus Internalization

Substances

Amyloid
Anti-HIV Agents
HIV Envelope Protein gp120
Peptide Fragments
gp120 protein, Human immunodeficiency virus 1
Catechin
epigallocatechin gallate