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Biochemistry. 2014 May 27;53(20):3267-77. doi: 10.1021/bi500427r. Epub 2014 May 12.

Structural characterization of semen coagulum-derived SEM1(86-107) amyloid fibrils that enhance HIV-1 infection.

Author information

1
Department of Biological Sciences and Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute , Troy, New York 12180, United States.

Abstract

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.

PMID:
24811874
PMCID:
PMC4039337
DOI:
10.1021/bi500427r
[Indexed for MEDLINE]
Free PMC Article

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