Structural Characterization of Semen Coagulum-Derived SEM1(86–107) Amyloid Fibrils That Enhance HIV‑1 Infection

SEM1­(86–107) is a 22-residue peptide corresponding to residues 86–107 in the semenogelin I protein. SEM1(86–107) is an abundant component of freshly liquefied semen and forms amyloid fibrils capable of enhancing HIV infection. To probe the factors affecting fibril formation and gain a better unders...

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Bibliographic Details
Published in:Biochemistry (Easton) 2014-05, Vol.53 (20), p.3267-3277
Main Authors: French, Kinsley C, Roan, Nadia R, Makhatadze, George I
Format: Article
Language:English
Subjects:
Accelerated Publication
Amino Acid Sequence
Amyloid - chemistry
Amyloid - genetics
HIV Infections - genetics
HIV Infections - metabolism
HIV-1
Human immunodeficiency virus 1
Humans
Male
Molecular Sequence Data
Semen - chemistry
Semen - physiology
Seminal Vesicle Secretory Proteins - chemistry
Seminal Vesicle Secretory Proteins - genetics
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Summary:SEM1­(86–107) is a 22-residue peptide corresponding to residues 86–107 in the semenogelin I protein. SEM1(86–107) is an abundant component of freshly liquefied semen and forms amyloid fibrils capable of enhancing HIV infection. To probe the factors affecting fibril formation and gain a better understanding of how differences in pH between semen and vaginal fluid affect fibril stability, this study determined the effect of pH on SEM1(86–107) fibril formation and dissociation. The SEM1(86–107) fibril structure (i.e., residues that comprise the fibrillar core) was also probed using hydrogen–deuterium exchange mass spectrometry (HDXMS) and hydroxyl radical-mediated protein modification. The average percent exposure to hydroxyl radical-mediated modification in the SEM1(86–107) fibrils was determined without requiring tandem mass spectrometry spectral acquisition or complete separation of modified peptides. It was found that the residue exposures calculated from HDXMS and hydroxyl radical-mediated modification were similar. These techniques demonstrated that three regions of SEM1­(86–107) comprise the amyloid fibril core and that positively charged residues are exposed, suggesting that electrostatic interactions between SEM1(86–107) and HIV or the cell surface may be responsible for mediating HIV infection enhancement by the SEM1(86–107) fibrils.
ISSN:0006-2960
1520-4995
DOI:10.1021/bi500427r