Evidence map›Paper›PMID 19995078›Full record

ArticleJournal of the American Chemical Society2009

NMR structure in a membrane environment reveals putative amyloidogenic regions of the SEVI precursor peptide PAP(248-286).

Ravi P R Nanga, Jeffrey R Brender, Subramanian Vivekanandan, Nataliya Popovych, Ayyalusamy Ramamoorthy

Open access · greenAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
2.4field-weighted citation impact, top 11% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

41 citing papers in PubMed, 69 citations in OpenAlex.

  1. Review
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  16. Impact of membrane curvature on amyloid aggregation.Biochimica et biophysica acta. Biomembranes · 2018
    Review
  17. Article
  18. Structure, function and antagonism of semen amyloids.Chemical communications (Cambridge, England) · 2018
    Review
  19. Article
  20. Epigallocatechin Gallate Inhibits Macaque SEVI-Mediated Enhancement of SIV or SHIV Infection.Journal of acquired immune deficiency syndromes (1999) · 2017
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Ravi P R NangaDepartment of Chemistry, University of Michigan, Ann Arbor, Michigan 48109-1055, USA.
Jeffrey R Brender
Subramanian Vivekanandan
Nataliya Popovych
Ayyalusamy Ramamoorthy
University of Michigan–Ann Arbor · US

Funding

Supplement: Investigation of Membrane-Bound Cytochromes-P450-b5 InteractionsR01GM084018 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI RAMAMOORTHY, AYYALUSAMY · 2009 to 2018
$3.8M
Purchase of a 500 MHz Solid State NMR SpectrometerS10RR023597 · NCRR · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI RAMAMOORTHY, AYYALUSAMY · 2007 to 2007
$500k
Membrane Interaction and Membrane Mediated Aggregation of AmylinR21DK078885 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI RAMAMOORTHY, AYYALUSAMY · 2009 to 2010
$411k
NCRR NIH HHS RR023597NCRR NIH HHS S10 RR023597NIDDK NIH HHS DK078885NIDDK NIH HHS R21 DK078885NIGMS NIH HHS GM084018NIGMS NIH HHS R01 GM084018
6 · The paper itself

Abstract

Semen is the main vector for HIV transmission worldwide. Recently, a peptide fragment (PAP(248-286)) has been isolated from seminal fluid that dramatically enhances HIV infectivity by up to 4-5 orders of magnitude. PAP(248-286) appears to enhance HIV infection by forming amyloid fibers known as SEVI, which are believed to enhance the attachment of the virus by bridging interactions between virion and host-cell membranes. We have solved the atomic-level resolution structure of the SEVI precursor PAP(248-286) using NMR spectroscopy in SDS micelles, which serve as a model membrane system. PAP(248-286), which does not disrupt membranes like most amyloid proteins, binds superficially to the surface of the micelle, in contrast to other membrane-disruptive amyloid peptides that generally penetrate into the core of the membrane. The structure of PAP(248-286) is unlike most amyloid peptides in that PAP(248-286) is mostly disordered when bound to the surface of the micelle, as opposed to the alpha-helical structures typically found of most amyloid proteins. The highly disordered nature of the SEVI peptide may explain the unique ability of SEVI amyloid fibers to enhance HIV infection as partially disordered amyloid fibers will have a greater capture radius for the virus than compact amyloid fibers. Two regions of nascent structure (an alpha-helix from V262-H270 and a dynamic alpha/3(10) helix from S279-L283) match the prediction of highly amyloidogenic sequences and may serve as nuclei for aggregation and amyloid fibril formation. The structure presented here can be used for the rational design of mutagenesis studies on SEVI amyloid formation and viral infection enhancement.

Indexed as

Membranes, ArtificialAmyloidHIV InfectionsMagnetic Resonance SpectroscopyPeptide FragmentsSemenAmyloidMembranes, ArtificialPeptide Fragments

Identifiers

PMID19995078
PMCPMC2792124
OpenAlexW2084963421

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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.