Evidence map›Paper›PMID 22948159›Full record

ArticleThe Journal of biological chemistry2012

Constant domain-regulated antibody catalysis.

Gopal Sapparapu, Stephanie Planque, Yukie Mitsuda, Gary McLean, Yasuhiro Nishiyama, Sudhir Paul

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed, 1 pooled it
2.0field-weighted citation impact, top 14% 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

11 citing papers in PubMed, 1 synthesis or guideline pooled it, 14 citations in OpenAlex.

  1. Pooled it
  2. Trial
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. 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

6 authors at 1 institution in 1 country.

Gopal SapparapuChemical Immunology Research Center, Department of Pathology and Laboratory Medicine, University of Texas Houston Medical School, Houston, Texas 77030, USA.
Stephanie Planque
Yukie Mitsuda
Gary McLean
Yasuhiro Nishiyama
Sudhir Paul
Texas Medical Center · US

Funding

U OF TEXAS HLTH SCI CTR HOUSTON CENTER FOR CLINICAL AND TRANSLATIONAL SCIENCESUL1RR024148 · NCRR · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI MCPHERSON, DAVID D · 2006 to 2010
$27.9M
Nucleophilic Antibodies: Characterization and InductionR01AI067020 · NIAID · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI PAUL, SUDHIR · 2007 to 2011
$2.2M
gp120 covalent analogs as candidate HIV vaccinesR01AI058865 · NIAID · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI PAUL, SUDHIR · 2004 to 2008
$1.7M
Covalent Vaccine for HIVR41AI093261 · NIAID · COVALENT BIOSCIENCE, INC. · PI NISHIYAMA, YASUHIRO · 2011 to 2012
$600k
Proteolytic Antibody HIVcidesR21AI071951 · NIAID · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI PAUL, SUDHIR · 2006 to 2007
$384k
Development of monoclonal catalytic antibodies for HIV immunotherapyR41AI087527 · NIAID · COVALENT IMMUNOLOGY PRODUCTS, INC. · PI PLANQUE, STEPHANIE A. · 2010 to 2010
$173k
NCRR NIH HHS UL1 RR024148NIAID NIH HHS AI058865NIAID NIH HHS AI067020NIAID NIH HHS AI071951NIAID NIH HHS AI087527NIAID NIH HHS AI093261NIAID NIH HHS R01 AI058865NIAID NIH HHS R01 AI067020NIAID NIH HHS R21 AI071951NIAID NIH HHS R41 AI087527NIAID NIH HHS R41 AI093261
6 · The paper itself

Abstract

Some antibodies contain variable (V) domain catalytic sites. We report the superior amide and peptide bond-hydrolyzing activity of the same heavy and light chain V domains expressed in the IgM constant domain scaffold compared with the IgG scaffold. The superior catalytic activity of recombinant IgM was evident using two substrates, a small model peptide that is hydrolyzed without involvement of high affinity epitope binding, and HIV gp120, which is recognized specifically by noncovalent means prior to the hydrolytic reaction. The catalytic activity was inhibited by an electrophilic phosphonate diester, consistent with a nucleophilic catalytic mechanism. All 13 monoclonal IgMs tested displayed robust hydrolytic activities varying over a 91-fold range, consistent with expression of the catalytic functions at distinct levels by different V domains. The catalytic activity of polyclonal IgM was superior to polyclonal IgG from the same sera, indicating that on average IgMs express the catalytic function at levels greater than IgGs. The findings indicate a favorable effect of the remote IgM constant domain scaffold on the integrity of the V-domain catalytic site and provide a structural basis for conceiving antibody catalysis as a first line immune function expressed at high levels prior to development of mature IgG class antibodies.

Indexed as

AdolescentAdultAgedAmino Acid SequenceAntibodies, CatalyticAntibodies, MonoclonalCatalytic DomainFemaleHumansImmunoglobulin Constant RegionsImmunoglobulin GImmunoglobulin MImmunoglobulin Variable RegionMaleMiddle AgedMolecular Sequence DataAntibodies, CatalyticAntibodies, MonoclonalImmunoglobulin Constant RegionsImmunoglobulin GImmunoglobulin MImmunoglobulin Variable Region

Identifiers

PMID22948159
PMCPMC3476277
OpenAlexW2044465411

What Socratic 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 Socratic graph.