Bacterial curli protein promotes the conversion of PAP248-286 into the amyloid SEVI: cross-seeding of dissimilar amyloid sequences
Fragments of prostatic acid phosphatase (PAP248-286) in human semen dramatically increase HIV infection efficiency by increasing virus adhesion to target cells. PAP248-286 only enhances HIV infection in the form of amyloid aggregates termed SEVI (Semen Enhancer of Viral Infection), however monomeric...
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PeerJ Inc.
2013-02-01
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| author | Kevin Hartman Jeffrey R. Brender Kazuaki Monde Akira Ono Margery L. Evans Nataliya Popovych Matthew R. Chapman Ayyalusamy Ramamoorthy |
| author_facet | Kevin Hartman Jeffrey R. Brender Kazuaki Monde Akira Ono Margery L. Evans Nataliya Popovych Matthew R. Chapman Ayyalusamy Ramamoorthy |
| author_sort | Kevin Hartman |
| collection | DOAJ |
| description | Fragments of prostatic acid phosphatase (PAP248-286) in human semen dramatically increase HIV infection efficiency by increasing virus adhesion to target cells. PAP248-286 only enhances HIV infection in the form of amyloid aggregates termed SEVI (Semen Enhancer of Viral Infection), however monomeric PAP248-286 aggregates very slowly in isolation. It has therefore been suggested that SEVI fiber formation in vivo may be promoted by exogenous factors. We show here that a bacterially-produced extracellular amyloid (curli or Csg) acts as a catalytic agent for SEVI formation from PAP248-286 at low concentrations in vitro, producing fibers that retain the ability to enhance HIV (Human Immunodeficiency Virus) infection. Kinetic analysis of the cross-seeding effect shows an unusual pattern. Cross-seeding PAP248-286 with curli only moderately affects the nucleation rate while significantly enhancing the growth of fibers from existing nuclei. This pattern is in contrast to most previous observations of cross-seeding, which show cross-seeding partially bypasses the nucleation step but has little effect on fiber elongation. Seeding other amyloidogenic proteins (IAPP (islet amyloid polypeptide) and Aβ1−40) with curli showed varied results. Curli cross-seeding decreased the lag-time of IAPP amyloid formation but strongly inhibited IAPP elongation. Curli cross-seeding exerted a complicated concentration dependent effect on Aβ1−40 fibrillogenesis kinetics. Combined, these results suggest that the interaction of amyloidogenic proteins with preformed fibers of a different type can take a variety of forms and is not limited to epitaxial nucleation between proteins of similar sequence. The ability of curli fibers to interact with proteins of dissimilar sequences suggests cross-seeding may be a more general phenomenon than previously supposed. |
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| issn | 2167-8359 |
| language | English |
| last_indexed | 2024-03-09T06:22:42Z |
| publishDate | 2013-02-01 |
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| spelling | doaj.art-45539cf7e24a4a6195aad9dc2c1ca9792023-12-03T11:32:45ZengPeerJ Inc.PeerJ2167-83592013-02-011e510.7717/peerj.55Bacterial curli protein promotes the conversion of PAP248-286 into the amyloid SEVI: cross-seeding of dissimilar amyloid sequencesKevin Hartman0Jeffrey R. Brender1Kazuaki Monde2Akira Ono3Margery L. Evans4Nataliya Popovych5Matthew R. Chapman6Ayyalusamy Ramamoorthy7Department of Chemistry, University of Michigan, USADepartment of Chemistry, University of Michigan, USADepartment of Microbiology and Immunology, University of Michigan Medical School, USADepartment of Microbiology and Immunology, University of Michigan Medical School, USADepartment of Molecular, Cellular, and Developmental Biology, University of Michigan, USADepartment of Chemistry, University of Michigan, USADepartment of Molecular, Cellular, and Developmental Biology, University of Michigan, USADepartment of Chemistry, University of Michigan, USAFragments of prostatic acid phosphatase (PAP248-286) in human semen dramatically increase HIV infection efficiency by increasing virus adhesion to target cells. PAP248-286 only enhances HIV infection in the form of amyloid aggregates termed SEVI (Semen Enhancer of Viral Infection), however monomeric PAP248-286 aggregates very slowly in isolation. It has therefore been suggested that SEVI fiber formation in vivo may be promoted by exogenous factors. We show here that a bacterially-produced extracellular amyloid (curli or Csg) acts as a catalytic agent for SEVI formation from PAP248-286 at low concentrations in vitro, producing fibers that retain the ability to enhance HIV (Human Immunodeficiency Virus) infection. Kinetic analysis of the cross-seeding effect shows an unusual pattern. Cross-seeding PAP248-286 with curli only moderately affects the nucleation rate while significantly enhancing the growth of fibers from existing nuclei. This pattern is in contrast to most previous observations of cross-seeding, which show cross-seeding partially bypasses the nucleation step but has little effect on fiber elongation. Seeding other amyloidogenic proteins (IAPP (islet amyloid polypeptide) and Aβ1−40) with curli showed varied results. Curli cross-seeding decreased the lag-time of IAPP amyloid formation but strongly inhibited IAPP elongation. Curli cross-seeding exerted a complicated concentration dependent effect on Aβ1−40 fibrillogenesis kinetics. Combined, these results suggest that the interaction of amyloidogenic proteins with preformed fibers of a different type can take a variety of forms and is not limited to epitaxial nucleation between proteins of similar sequence. The ability of curli fibers to interact with proteins of dissimilar sequences suggests cross-seeding may be a more general phenomenon than previously supposed.https://peerj.com/articles/5.pdfFunctional amyloidStrainKineticsSeedingHIV |
| spellingShingle | Kevin Hartman Jeffrey R. Brender Kazuaki Monde Akira Ono Margery L. Evans Nataliya Popovych Matthew R. Chapman Ayyalusamy Ramamoorthy Bacterial curli protein promotes the conversion of PAP248-286 into the amyloid SEVI: cross-seeding of dissimilar amyloid sequences PeerJ Functional amyloid Strain Kinetics Seeding HIV |
| title | Bacterial curli protein promotes the conversion of PAP248-286 into the amyloid SEVI: cross-seeding of dissimilar amyloid sequences |
| title_full | Bacterial curli protein promotes the conversion of PAP248-286 into the amyloid SEVI: cross-seeding of dissimilar amyloid sequences |
| title_fullStr | Bacterial curli protein promotes the conversion of PAP248-286 into the amyloid SEVI: cross-seeding of dissimilar amyloid sequences |
| title_full_unstemmed | Bacterial curli protein promotes the conversion of PAP248-286 into the amyloid SEVI: cross-seeding of dissimilar amyloid sequences |
| title_short | Bacterial curli protein promotes the conversion of PAP248-286 into the amyloid SEVI: cross-seeding of dissimilar amyloid sequences |
| title_sort | bacterial curli protein promotes the conversion of pap248 286 into the amyloid sevi cross seeding of dissimilar amyloid sequences |
| topic | Functional amyloid Strain Kinetics Seeding HIV |
| url | https://peerj.com/articles/5.pdf |
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