Evidence map›Paper›PMID 27574710›Full record

ArticleScience immunology2016

Conservation and diversity in the ultralong third heavy-chain complementarity-determining region of bovine antibodies.

Robyn L Stanfield, Ian A Wilson, Vaughn V Smider

Open access · greenAbstract read
In one paragraph

Article in Science immunology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
5.4field-weighted citation impact, top 4% 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

43 citing papers in PubMed, 67 citations in OpenAlex.

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  9. The impact of exchanging the light and heavy chains on the structures of bovine ultralong antibodies.Acta crystallographica. Section F, Structural biology communications · 2024
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  12. The smallest functional antibody fragment: Ultralong CDR H3 antibody knob regions potently neutralize SARS-CoV-2.Proceedings of the National Academy of Sciences of the United States of America · 2023
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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

3 authors at 1 institution in 1 country.

Robyn L StanfieldDepartment of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, California, 92037, USA.
Ian A WilsonDepartment of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, California, 92037, USA; Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, California, 92037, USA.
Vaughn V SmiderDepartment of Cell and Molecular Biology, The Scripps Research Institute, La Jolla, California, 92037, USA; Fabrus Inc., A Division of Sevion Therapeutics, San Diego, CA 92121, USA.
Scripps Research Institute · US

Funding

ZWITTERION SURFACTANT DDMAB FOR IMPROV STABIL OF PROTEINP41RR001209 · NCRR · STANFORD UNIVERSITY · PI GONZALEZ, ANA M · 1985 to 2011
$38.9M
X-ray Absorption Spectroscopy (XAS) pp.711-759P41GM103393 · NIGMS · STANFORD UNIVERSITY · PI HODGSON, KEITH O · 2012 to 2019
$30.6M
Structural Biology of HIV-1 Neutralizing Antibody Targets for Vaccine DesignR01AI084817 · NIAID · SCRIPPS RESEARCH INSTITUTE, THE · PI WILSON, IAN A · 2009 to 2013
$3.2M
Molecular and Structural Studies of Antibody Diversity MechanismsR01GM105826 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI SMIDER, VAUGHN VASIL · 2014 to 2021
$3.1M
Exploiting sites of vulnerability on influenza virusesR56AI117675 · NIAID · SCRIPPS RESEARCH INSTITUTE, THE · PI WILSON, IAN A · 2015 to 2015
$836k
Structure and dynamics of native HIV-1 envelope trimersR56AI084817 · NIAID · SCRIPPS RESEARCH INSTITUTE, THE · PI WILSON, IAN A · 2015 to 2015
$593k
Antibody Fingerprinting of Triple Negative Breast Cancer by High Throughput FACSR21CA198595 · NCI · SCRIPPS RESEARCH INSTITUTE, THE · PI FELDING, BRUNIE H., SMIDER, VAUGHN VASIL · 2015 to 2016
$457k
NCI NIH HHS R21 CA198595NCRR NIH HHS P41 RR001209NIAID NIH HHS R01 AI084817NIAID NIH HHS R56 AI084817NIAID NIH HHS R56 AI117675NIGMS NIH HHS P41 GM103393NIGMS NIH HHS R01 GM105826
6 · The paper itself

Abstract

A subset of bovine antibodies have an exceptionally long third heavy-chain complementarity determining region (CDR H3) that is highly variable in sequence and includes multiple cysteines. These long CDR H3s (up to 69 residues) fold into a long stalk atop which sits a knob domain that is located far from the antibody surface. Three new bovine Fab crystal structures have been determined to decipher the conserved and variable features of ultralong CDR H3s that lead to diversity in antigen recognition. Despite high sequence variability, the stalks adopt a conserved β-ribbon structure, while the knob regions share a conserved β-sheet that serves as a scaffold for two connecting loops of variable length and conformation, as well as one conserved disulfide. Variation in patterns and connectivity of the remaining disulfides contribute to the knob structural diversity. The unusual architecture of these ultralong bovine CDR H3s for generating diversity is unique in adaptive immune systems.

Identifiers

PMID27574710
PMCPMC5000368
OpenAlexW2482075725

What OpenQuestion holds

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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.