Journal
BIOPHYSICAL JOURNAL
Volume 100, Issue 5, Pages 1325-1334Publisher
CELL PRESS
DOI: 10.1016/j.bpj.2011.01.037
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Funding
- National Institutes of Health [R01 AI084111, T32AI049815]
- DuPont Young Professors Award
- Creative and Novel Ideas in HIV Research (CNIHR)
- National Science Foundation [CHE-0840410]
- Direct For Mathematical & Physical Scien
- Division Of Chemistry [0840410] Funding Source: National Science Foundation
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Semen-derived enhancer of viral infection (SEVI), an amyloid fibril formed from a cationic peptide fragment of prostatic acidic phosphatase (PAP), dramatically enhances the infectivity of human immunodeficiency virus type 1 (HIV-1). Insoluble, sedimentable fibrils contribute to SEVI-mediated enhancement of virus infection. However, the SEVI-forming PAP(248-286) peptide is able to produce infection-enhancing structures much more quickly than it forms amyloid fibrils. This suggests that soluble supramolecular assemblies may enhance HIV-1 infection. To address this question, non-SEVI amyloid-like fibrils were derived from general amphipathic peptides of sequence Ac-K-n(XKXE)(2)-NH2. These cationic peptides efficiently self-assembled to form soluble, fibril-like structures that were, in some cases, able to enhance HIV-1 infection even more efficiently than SEVI. Experiments were also performed to determine whether agents that efficiently shield the charged surface of SEVI fibrils block SEVI-mediated infection-enhancement. To do this, we generated self-assembling anionic peptides of sequence Ac-E-n(XKXE)(2)-NH2. One of these peptides completely abrogated SEVI-mediated enhancement of HIV-1 infection, without altering HIV-1 infectivity in the absence of SEVI. Collectively, these data suggest that soluble SEVI assemblies may mediate infection-enhancement, and that anionic peptide supramolecular assemblies have the potential to act as anti-SEVI microbicides.
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