Evidence map›Paper›PMID 19104014›Full record

ArticleAntimicrobial agents and chemotherapy2009

Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection.

Radeekorn Akkarawongsa, Nina E Pocaro, Gary Case, Aaron W Kolb, Curtis R Brandt

Abstract read
In one paragraph

Article in Antimicrobial agents and chemotherapy, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
1.4field-weighted citation impact, top 18% 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

27 citing papers in PubMed, 48 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Entry of Alphaherpesviruses.Current issues in molecular biology · 2021
    Review
  5. Article
  6. Herpes Simplex Virus Cell Entry Mechanisms: An Update.Frontiers in cellular and infection microbiology · 2020
    Review
  7. Review
  8. Antiviral peptides as promising therapeutic drugs.Cellular and molecular life sciences : CMLS · 2019
    Review
  9. Infectivity inhibition by overlapping synthetic peptides derived from the gH/gL heterodimer of herpes simplex virus type 1.Journal of peptide science : an official publication of the European Peptide Society · 2017
    Article
  10. Membranotropic Cell Penetrating Peptides: The Outstanding Journey.International journal of molecular sciences · 2015
    Review
  11. Article
  12. Article
  13. Review
  14. Review
  15. Review
  16. Review
  17. Inhibition of herpes simplex virus type 1 with the modified green tea polyphenol palmitoyl-epigallocatechin gallate.Food and chemical toxicology : an international journal published for the British Industrial Biological Research Association · 2013
    Article
  18. Article
  19. Article
  20. 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 3 institutions in 3 countries.

Radeekorn AkkarawongsaDepartment of Ophthalmology and Visual Sciences, University of Wisconsin-Madison, Madison, Wisconsin 53706, USA.
Nina E Pocaro
Gary Case
Aaron W Kolb
Curtis R Brandt
Biotechnology Research Center · IRInstitute of Molecular and Cell Biology · RUUniversity of Wisconsin–Madison · US

Funding

UW Vision Research Core - Administrative CoreP30EY016665 · NEI · UNIVERSITY OF WISCONSIN-MADISON · PI Colleen Mary McDowell · 2005 to 2026
$12.6M
PEPTIDE INHIBITORS OF PAPILLOMAVIRAL INFECTIONP01AI052049 · NIAID · UNIVERSITY OF WISCONSIN MADISON · PI BRANDT, CURTIS R · 2001 to 2004
$3.5M
NEI NIH HHS P30 EY016665NIAID NIH HHS P01 AI052049NIAID NIH HHS P01-AI52049PHS HHS P30-016665
6 · The paper itself

Abstract

The 773-residue ectodomain of the herpes simplex virus type 1 (HSV-1) glycoprotein B (gB) has been resistant to the use of mutagenic strategies because the majority of the induced mutations result in defective proteins. As an alternative strategy for the identification of functionally important regions and novel inhibitors of infection, we prepared a library of overlapping peptides homologous to the ectodomain of gB and screened for the ability of the peptides to block infection. Seven of 138 15-mer peptides inhibited infection by more than 50% at a concentration of 100 microM. Three peptides (gB94, gB122, and gB131) with 50% effective concentrations (EC(50)s) below 20 microM were selected for further studies. The gB131 peptide (residues 681 to 695 in HSV-1 gB [gB-1]) was a specific entry inhibitor (EC(50), approximately 12 microM). The gB122 peptide (residues 636 to 650 in gB-1) blocked viral entry (EC(50), approximately 18 microM), protected cells from infection (EC(50), approximately 72 microM), and inactivated virions in solution (EC(50), approximately 138 microM). We were unable to discern the step or steps inhibited by the gB94 peptide, which is homologous to residues 496 to 510 in gB-1. Substitution of a tyrosine in the gB122 peptide (Y640 in full-length gB-1) reduced the antiviral activity eightfold, suggesting that this residue is critical for inhibition. This peptide-based strategy could lead to the identification of functionally important regions of gB or other membrane proteins and identify novel inhibitors of HSV-1 entry.

Indexed as

Amino Acid SequenceAmino Acid SubstitutionAnimalsBinding SitesChlorocebus aethiopsDisulfidesDose-Response Relationship, DrugHerpes SimplexHerpesvirus 1, HumanHydrophobic and Hydrophilic InteractionsInhibitory Concentration 50Molecular Sequence DataPeptidesProtein BindingProtein Structure, TertiaryTyrosineDisulfidesglycoprotein B, SimplexvirusPeptidesTyrosineViral Envelope Proteins

Identifiers

PMID19104014
PMCPMC2650530
OpenAlexW2118233228

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.