title: Morphology-Dependent HIV-Enhancing Effect of Semen-Derived Enhancer of Viral Infection.
abstract: PAP248-286 is a 39-residue fragment (residues 248 to 286) derived from protease cleavage of prostatic acidic phosphatase in semen. The amyloid fibrils formed in vitro by PAP248-286 can dramatically enhance human immunodeficiency virus (HIV) infection. To our knowledge, we present the first report that the HIV-enhancing potency of fibrils formed by PAP248-286 is morphology dependent. We identified pleomorphic fibrils by transmission electron microscopy in two buffer conditions. Our solid-state NMR data showed that these fibrils consist of molecules in distinct conformations. In agreement with NMR, fluorescence measurements confirmed that they are assembled along different pathways, with distinct molecular structures. Furthermore, our cell-based infectivity tests detected distinct HIV-enhancing potencies for fibrils in distinct morphologies. In addition, our transmission electron microscopy and NMR results showed that semen-derived enhancer of viral infection fibrils formed in sodium bicarbonate buffer remain stable over time, but semen-derived enhancer of viral infection fibrils formed in phosphate buffered saline keep evolving after the initial 7 days incubation period. Given time, most of the assemblies in phosphate buffered saline will turn into elongated thin fibrils. They have similar secondary structure but different packing than thin fibrils formed initially after 7 days incubation.
authors.affiliation: Department of Physics, University of Central Florida, Orlando, Florida.
authors.forename: Xin
authors.initials: X
authors.lastname: Qiao
authors.affiliation: Department of Physics, University of Central Florida, Orlando, Florida.
authors.forename: Jaekyun
authors.initials: J
authors.lastname: Jeon
authors.affiliation: Department of Molecular Biology and Microbiology, Burnett School of Biomedical Sciences, University of Central Florida, Orlando, Florida.
authors.forename: Amy L
authors.initials: AL
authors.lastname: Cole
authors.affiliation: Department of Physics, University of Central Florida, Orlando, Florida.
authors.forename: Jason O
authors.initials: JO
authors.lastname: Matos
authors.affiliation: Department of Physics, University of Central Florida, Orlando, Florida.
authors.forename: Stephany
authors.initials: S
authors.lastname: Bautista
authors.affiliation: Department of Physics, University of Central Florida, Orlando, Florida.
authors.forename: Justin
authors.initials: J
authors.lastname: Castillo
authors.affiliation: National High Magnetic Field Laboratory, Tallahassee, Florida.
authors.forename: Ivan
authors.initials: I
authors.lastname: Hung
authors.affiliation: National High Magnetic Field Laboratory, Tallahassee, Florida.
authors.forename: Zhehong
authors.initials: Z
authors.lastname: Gan
authors.affiliation: Department of Physics, University of Central Florida, Orlando, Florida.
authors.forename: Suren A
authors.initials: SA
authors.lastname: Tatulian
authors.affiliation: Department of Molecular Biology and Microbiology, Burnett School of Biomedical Sciences, University of Central Florida, Orlando, Florida.
authors.forename: Alexander M
authors.initials: AM
authors.lastname: Cole
authors.affiliation: Department of Physics, University of Central Florida, Orlando, Florida. Electronic address: bo.chen@ucf.edu.
authors.forename: Bo
authors.initials: B
authors.lastname: Chen
mesh_terms: D000135:Acid Phosphatase / Q000737:chemistry / Q000494:pharmacology*; D000682:Amyloid / Q000737:chemistry / Q000494:pharmacology*; D045744:Cell Line, Tumor; D015497:HIV-1 / Q000472:pathogenicity*; D006801:Humans; D010446:Peptide Fragments / Q000737:chemistry / Q000494:pharmacology; D014774:Virulence / Q000187:drug effects
chemical_list: D000682:Amyloid; D010446:Peptide Fragments; D000135:Acid Phosphatase; C428439:prostatic acid phosphatase