Evidence map›Paper›PMID 9784192›Full record

ArticleAnalytical biochemistry1998

The maltose-binding protein as a scaffold for monovalent display of peptides derived from phage libraries.

M B Zwick, L L Bonnycastle, K A Noren, S Venturini, E Leong, C F Barbas, C J Noren, J K Scott

Erratum issuedAbstract read
In one paragraph

Article in Analytical biochemistry, 1998. 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 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
3.4field-weighted citation impact, top 8% 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

12 citing papers in PubMed, 46 citations in OpenAlex.

  1. Article
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  4. Article
  5. A peptide inhibitor of HIV-1 neutralizing antibody 2G12 is not a structural mimic of the natural carbohydrate epitope on gp120.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2008
    Article
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  9. Review
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4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

8 authors at 2 institutions in 2 countries.

M B ZwickBiochemistry Program, Department of Biological Sciences, Institute of Molecular Biology and Biochemistry, Simon Fraser University, 8888 University Drive, Burnaby, British Columbia, V5A 1S6, Canada.
L L Bonnycastle
K A Noren
S Venturini
E Leong
C F Barbas
C J Noren
J K Scott
Simon Fraser University · CAScripps Research Institute · US

Funding

IN VITRO EVOLUTION OF HUMAN ANTIHIV ANTIBODIESR01AI037470 · NIAID · SCRIPPS RESEARCH INSTITUTE · PI BARBAS, CARLOS F · 1995 to 2002
$1.1M
FAB LIBRARIES TO DISCOVER VACCINE LEADS AGAINST HIV-1R21AI046303 · NIAID · SIMON FRASER UNIVERSITY · PI SCOTT, JAMIE K · 1999 to 2000
$158k
PEPTIDE MIMICS OF NEUTRALIZING SITES ON HIV ENV PROTEINSR21AI044395 · NIAID · SIMON FRASER UNIVERSITY · PI SCOTT, JAMIE K · 1998 to 1999
–
NIAID NIH HHS AI 37470NIAID NIH HHS R21 AI044395NIAID NIH HHS R21 AI046303
6 · The paper itself

Abstract

Random peptide libraries are displayed on filamentous bacteriophage as fusions to either the minor coat protein, pIII, or the major coat protein, pVIII. We have devised a means of isolating the peptide displayed on a phage clone by transferring it to the N-terminus of the maltose-binding protein (MBP) of Escherichia coli encoded by malE. Transfer of a peptide sequence to monomeric MBP eliminates phage-encoded amino acids downstream of the insert peptide as well as avidity effects caused by multivalent display on phage. Peptide:MBP fusions are also easily affinity purified on amylose columns. The pMal-p2 vector was engineered to accept phage DNA encoding pIII- and pVIII-displayed peptides fused to their respective leader sequences. Both types of leader sequence were shown to target the peptide:MBP fusions to the periplasm of E. coli. A streamlined procedure for transferring peptides to MBP was applied to clones that had been isolated from a panel of pVIII-displayed peptide libraries by screening with an HIV-1-specific monoclonal antibody (Ab). By enzyme-linked immunosorbent assay, the Ab bound each of the peptide:MBP fusions and required the presence of a disulfide bridge within each peptide. Some of the peptide:MBP fusions were also analyzed using surface plasmon resonance. Thus, our study shows the value of malE fusion vectors in characterizing phage-displayed peptides.

Indexed as

ATP-Binding Cassette TransportersEscherichia coli ProteinsMonosaccharide Transport ProteinsPeptide LibraryPeriplasmic Binding ProteinsAmino Acid SequenceBacteriophagesBase SequenceCarrier ProteinsCloning, MolecularDNA, RecombinantEscherichia coliGenetic VectorsHIV-1HIV AntibodiesHumansATP-Binding Cassette TransportersCarrier ProteinsDNA, RecombinantEscherichia coli ProteinsHIV AntibodiesMalE protein, E coliMaltose-Binding Proteinsmaltose transport system, E coliMonosaccharide Transport ProteinsPeptide LibraryPeriplasmic Binding ProteinsProtein Sorting SignalsRecombinant Fusion Proteins

Identifiers

PMID9784192
PMCPMC3998728
OpenAlexW2032380264

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.