title: A Peptide Derived from the HIV-1 gp120 Coreceptor-Binding Region Promotes Formation of PAP248-286 Amyloid Fibrils to Enhance HIV-1 Infection.
abstract: BACKGROUND
  Semen is a major vehicle for HIV transmission. Prostatic acid phosphatase (PAP) fragments, such as PAP248-286, in human semen can form amyloid fibrils to enhance HIV infection. Other endogenous or exogenous factors present during sexual intercourse have also been reported to promote the formation of seminal amyloid fibrils.
  
  
  RESULTS
  Here, we demonstrated that a synthetic 15-residue peptide derived from the HIV-1 gp120 coreceptor-binding region, designated enhancing peptide 2 (EP2), can rapidly self-assemble into nanofibers. These EP2-derivated nanofibers promptly accelerated the formation of semen amyloid fibrils by PAP248-286, as shown by Thioflavin T (ThT) and Congo red assays. The amyloid fibrils presented similar morphology, assessed via transmission electron microscopy (TEM), in the presence or absence of EP2. Circular dichroism (CD) spectroscopy revealed that EP2 accelerates PAP248-286 amyloid fibril formation by promoting the structural transition of PAP248-286 from a random coil into a cross-β-sheet. Newly formed semen amyloid fibrils effectively enhanced HIV-1 infection in TZM-bl cells and U87 cells by promoting the binding of HIV-1 virions to target cells.
  
  
  CONCLUSIONS
  Nanofibers composed of EP2 promote the formation of PAP248-286 amyloid fibrils and enhance HIV-1 infection.
authors.affiliation: School of Pharmaceutical Sciences, Southern Medical University, Guangzhou, China.
authors.forename: Jinquan
authors.initials: J
authors.lastname: Chen
authors.affiliation: School of Pharmaceutical Sciences, Southern Medical University, Guangzhou, China.
authors.forename: Ruxia
authors.initials: R
authors.lastname: Ren
authors.affiliation: School of Pharmaceutical Sciences, Southern Medical University, Guangzhou, China.
authors.forename: Suiyi
authors.initials: S
authors.lastname: Tan
authors.affiliation: School of Pharmaceutical Sciences, Southern Medical University, Guangzhou, China.
authors.forename: Wanyue
authors.initials: W
authors.lastname: Zhang
authors.affiliation: School of Pharmaceutical Sciences, Southern Medical University, Guangzhou, China.
authors.forename: Xuanxuan
authors.initials: X
authors.lastname: Zhang
authors.affiliation: Key Laboratory of Medical Molecular Virology of MOE/MOH, Shanghai Medical College and Institute of Medical Microbiology, Fudan University, Shanghai, China.
authors.forename: Fei
authors.initials: F
authors.lastname: Yu
authors.affiliation: School of Pharmaceutical Sciences, Southern Medical University, Guangzhou, China.
authors.forename: Tianrong
authors.initials: T
authors.lastname: Xun
authors.affiliation: Key Laboratory of Medical Molecular Virology of MOE/MOH, Shanghai Medical College and Institute of Medical Microbiology, Fudan University, Shanghai, China.|Lindsley F. Kimball Research Institute, New York Blood Center, New York, NY, United States of America.
authors.forename: Shibo
authors.initials: S
authors.lastname: Jiang
authors.affiliation: School of Pharmaceutical Sciences, Southern Medical University, Guangzhou, China.
authors.forename: Shuwen
authors.initials: S
authors.lastname: Liu
authors.affiliation: School of Pharmaceutical Sciences, Southern Medical University, Guangzhou, China.
authors.forename: Lin
authors.initials: L
authors.lastname: Li
mesh_terms: D000135:Acid Phosphatase / Q000378:metabolism*; D000682:Amyloid / Q000378:metabolism*; D002460:Cell Line; D015699:HIV Envelope Protein gp120 / Q000378:metabolism*; D015658:HIV Infections / Q000473:pathology*; D015497:HIV-1 / Q000378:metabolism; D006801:Humans; D010455:Peptides / Q000378:metabolism; D066263:Protein Aggregation, Pathological / Q000503:physiopathology*; D017434:Protein Structure, Tertiary
chemical_list: D000682:Amyloid; D015699:HIV Envelope Protein gp120; D010455:Peptides; C514793:gp120 protein, Human immunodeficiency virus 1; D000135:Acid Phosphatase; C428439:prostatic acid phosphatase