Evidence map›Paper›PMID 31981247›Full record

ArticleProtein science : a publication of the Protein Society2020

Role of a noncanonical disulfide bond in the stability, affinity, and flexibility of a VHH specific for the Listeria virulence factor InlB.

Matthew N Mendoza, Mike Jian, Moeko T King, Cory L Brooks

Abstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
–field-weighted citation impact
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

25 citing papers in PubMed.

  1. Article
  2. Article
  3. Luteolin Inhibits Invasion ofMolecules (Basel, Switzerland) · 2026
    Article
  4. Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Affinity-stability trade-off mechanism of residue 35 in framework region 2 of VProtein science : a publication of the Protein Society · 2025
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Conformational features and interaction mechanisms of VProtein science : a publication of the Protein Society · 2023
    Article
  16. Therapeutic Antibodies in Medicine.Molecules (Basel, Switzerland) · 2023
    Review
  17. Article
  18. Article
  19. Article
  20. Dromedary camel nanobodies broadly neutralize SARS-CoV-2 variants.Proceedings of the National Academy of Sciences of the United States of America · 2022
    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

4 authors.

Matthew N MendozaDepartment of Chemistry, California State University Fresno, Fresno, California.
Mike JianDepartment of Chemistry, California State University Fresno, Fresno, California.
Moeko T KingDepartment of Chemistry, California State University Fresno, Fresno, California.
Cory L BrooksDepartment of Chemistry, California State University Fresno, Fresno, California.ORCID 0000-0002-6745-6526

Funding

Nanobodies for the Detection and Neutralization of Listeria monocytogenesSC3GM112532 · NIGMS · CALIFORNIA STATE UNIVERSITY FRESNO · PI BROOKS, CORY · 2015 to 2018
$420k
CIHRNIGMS NIH HHS SC3 GM112532NIGMS NIH HHS SC3GM112532
6 · The paper itself

Abstract

A distinguishing feature of camel (Camelus dromedarius) VHH domains are noncanonical disulfide bonds between CDR1 and CDR3. The disulfide bond may provide an evolutionary advantage, as one of the cysteines in the bond is germline encoded. It has been hypothesized that this additional disulfide bond may play a role in binding affinity by reducing the entropic penalty associated with immobilization of a long CDR3 loop upon antigen binding. To examine the role of a noncanonical disulfide bond on antigen binding and the biophysical properties of a VHH domain, we have used the VHH R303, which binds the Listeria virulence factor InlB as a model. Using site directed mutagenesis, we produced a double mutant of R303 (C33A/C102A) to remove the extra disulfide bond of the VHH R303. Antigen binding was not affected by loss of the disulfide bond, however the mutant VHH displayed reduced thermal stability (T

Indexed as

AnimalsAntigen-Antibody ReactionsBinding SitesCamelusDisulfidesListeriaModels, MolecularSingle-Domain AntibodiesVirulence FactorsDisulfidesSingle-Domain AntibodiesVirulence Factorsantigendisulfide bonddynamicsflexibilityNanobodyprotein aggregationVHH

Identifiers

PMID31981247
PMCPMC7096713

What OpenQuestion holds

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Registered trials

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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.