Evidence map›Paper›PMID 20138057›Full record

ArticleJournal of molecular biology2010

Antigenic characteristics of rhinovirus chimeras designed in silico for enhanced presentation of HIV-1 gp41 epitopes [corrected].

Mauro Lapelosa, Gail Ferstandig Arnold, Emilio Gallicchio, Eddy Arnold, Ronald M Levy

Erratum issuedOpen access · greenAbstract read
In one paragraph

Article in Journal of molecular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
3.2field-weighted citation impact, top 9% 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

8 citing papers in PubMed, 16 citations in OpenAlex.

  1. Article
  2. Computer-aided antibody design.Protein engineering, design & selection : PEDS · 2012
    Review
  3. Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. Article
4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

5 authors at 2 institutions in 1 country.

Mauro LapelosaBioMaPS Institute for Quantitative Biology, Rutgers University, Piscataway, NJ 08854, USA.
Gail Ferstandig Arnold
Emilio Gallicchio
Eddy Arnold
Ronald M Levy
Quantitative BioSciences · USRutgers, The State University of New Jersey · US

Funding

DYNAMICS OF PEPTIDES AND PROTEINSR01GM030580 · NIGMS · TEMPLE UNIV OF THE COMMONWEALTH · PI LEVY, RONALD · 1985 to 2018
$6.1M
Broad Neutralization of HIV-1 from Rhinoviruses Displaying gp41 MPER SequencesR01AI071874 · NIAID · RUTGERS, THE STATE UNIV OF N.J. · PI ARNOLD, GAIL F · 2006 to 2009
$1.7M
Computer Cluster for Computational and Structural BiologyS10RR022375 · NCRR · RUTGERS, THE STATE UNIV OF N.J. · PI LEVY, RONALD · 2007 to 2007
$291k
IMMUNOGENICITY &STRUCTURES OF RHINOVIRUS-HIV CHIMERASR01AI038221 · NIAID · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI ARNOLD, GAIL F · 1995 to 1999
–
NCRR NIH HHS 1 S10 RR022375NCRR NIH HHS S10 RR022375NIAID NIH HHS AI071874NIAID NIH HHS R01 AI038221NIAID NIH HHS R01 AI071874NIGMS NIH HHS GM30580NIGMS NIH HHS R01 GM030580
6 · The paper itself

Abstract

The development of an effective AIDS vaccine remains the most promising long-term strategy to combat human immunodeficiency virus (HIV)/AIDS. Here, we report favorable antigenic characteristics of vaccine candidates isolated from a combinatorial library of human rhinoviruses displaying the ELDKWA epitope of the gp41 glycoprotein of HIV-1. The design principles of this library emerged from the application of molecular modeling calculations in conjunction with our knowledge of previously obtained ELDKWA-displaying chimeras, including knowledge of a chimera with one of the best 2F5-binding characteristics obtained to date. The molecular modeling calculations identified the energetic and structural factors affecting the ability of the epitope to assume conformations capable of fitting into the complementarity determining region of the ELDKWA-binding, broadly neutralizing human mAb 2F5. Individual viruses were isolated from the library following competitive immunoselection and were tested using ELISA and fluorescence quenching experiments. Dissociation constants obtained using both techniques revealed that some of the newly isolated chimeras bind 2F5 with greater affinity than previously identified chimeric rhinoviruses. Molecular dynamics simulations of two of these same chimeras confirmed that their HIV inserts were partially preorganized for binding, which is largely responsible for their corresponding gains in binding affinity. The study illustrates the utility of combining structure-based experiments with computational modeling approaches for improving the odds of selecting vaccine component designs with preferred antigenic characteristics. The results obtained also confirm the flexibility of HRV as a presentation vehicle for HIV epitopes and the potential of this platform for the development of vaccine components against AIDS.

Indexed as

Drug DesignAIDS VaccinesAntibodies, MonoclonalAntigens, ViralEnzyme-Linked Immunosorbent AssayEpitopesHIV-1HIV AntibodiesHIV Envelope Protein gp41HumansNeutralization TestsPeptide LibraryProtein ConformationRhinovirusAIDS VaccinesAntibodies, MonoclonalAntigens, ViralEpitopesgp41 protein, Human immunodeficiency virus 1HIV AntibodiesHIV Envelope Protein gp41Peptide Library

Identifiers

PMID20138057
PMCPMC2940250
OpenAlexW2082832605

What OpenQuestion holds

Textmetadata
LicenceTDM
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.