Evidence map›Paper›PMID 18391029›Full record

ArticleAntimicrobial agents and chemotherapy2008

Inhibition of herpes simplex virus type 1 infection by cationic beta-peptides.

Radeekorn Akkarawongsa, Terra B Potocky, Emily P English, Samuel H Gellman, Curtis R Brandt

Open access · greenAbstract read
In one paragraph

Article in Antimicrobial agents and chemotherapy, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
2.6field-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

9 citing papers in PubMed, 32 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Synthetic mimetics of protein secondary structure domains.Philosophical transactions. Series A, Mathematical, physical, and engineering sciences · 2010
    Review
  8. Article
  9. 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 2 countries.

Radeekorn AkkarawongsaProgram in Cell and Molecular Biology, University of Wisconsin-Madison, Madison, Wisconsin 53706, USA.
Terra B Potocky
Emily P English
Samuel H Gellman
Curtis R Brandt
Institute of Molecular and Cell Biology · RU

Funding

UW Vision Research Core - Administrative CoreP30EY016665 · NEI · UNIVERSITY OF WISCONSIN-MADISON · PI AKIHIRO IKEDA · 2005 to 2026
$12.6M
Chemistry-Biology Interface Training ProgramT32GM008505 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI BLACKWELL, HELEN E. · 1993 to 2023
$9.8M
Protein Recognition by Peptidic FoldamersR01GM056414 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI GELLMAN, SAMUEL H. · 1997 to 2023
$6.5M
PEPTIDE INHIBITORS OF PAPILLOMAVIRAL INFECTIONP01AI052049 · NIAID · UNIVERSITY OF WISCONSIN MADISON · PI BRANDT, CURTIS R · 2001 to 2004
$3.5M
VIRUS SPECIFIC FACTORS OF HSV TO CORNEAL DISEASER01EY007336 · NEI · UNIVERSITY OF WISCONSIN-MADISON · PI BRANDT, CURTIS R · 1987 to 2008
$1.8M
NEI NIH HHS EY016665NEI NIH HHS EY07336NEI NIH HHS P30 EY016665NEI NIH HHS R01 EY007336NIAID NIH HHS AI52089NIAID NIH HHS P01 AI052049NIGMS NIH HHS GM56414NIGMS NIH HHS R01 GM056414NIGMS NIH HHS T32 GM008505NIGMS NIH HHS T32GM008505
6 · The paper itself

Abstract

Previously, it was shown that cationic alpha-peptides derived from the human immunodeficiency virus TAT protein transduction domain blocked herpes simplex virus type 1 (HSV-1) entry. We now show that cationic oligomers of beta-amino acids ("beta-peptides") inhibit HSV-1 infection. Among three cationic beta-peptides tested, the most effective inhibition was observed for the one with a strong propensity to adopt a helical conformation in which cationic and hydrophobic residues are segregated from one another ("globally amphiphilic helix"). The antiviral effect was not cell type specific. Inhibition of virus infection by the beta-peptides occurred at the postattachment penetration step, with a 50% effective concentration of 3 muM for the most-effective beta-peptide. The beta-peptides did not inactivate virions in solution, nor did they induce resistance to infection when cells were pretreated with the beta-peptides. The beta-peptides showed little if any toxicity toward Vero cells. These results raise the possibility that cationic beta-peptides may be useful antiviral agents for HSV-1 and demonstrate the potential of beta-peptides as novel antiviral drugs.

Indexed as

AnimalsAntiviral AgentsCationsCells, CulturedChlorocebus aethiopsCorneaFibroblastsHerpesvirus 1, HumanHumansMicrobial Sensitivity TestsPeptidesProtein ConformationVero CellsAntiviral AgentsCationsPeptides

Identifiers

PMID18391029
PMCPMC2415802
OpenAlexW2018866826

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.