Evidence map›Paper›PMID 31754129›Full record

ArticleScientific reports2019

Specific metallo-protein interactions and antimicrobial activity in Histatin-5, an intrinsically disordered salivary peptide.

Tyler G McCaslin, Cynthia V Pagba, Jiby Yohannan, Bridgette A Barry

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.9field-weighted citation impact, top 16% 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

18 citing papers in PubMed, 27 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Review
  8. Article
  9. Antimicrobial Peptides with Anti-International journal of molecular sciences · 2022
    Review
  10. Review
  11. Article
  12. Review
  13. Review
  14. Membrane-Interacting Antifungal Peptides.Frontiers in cell and developmental biology · 2021
    Review
  15. Review
  16. Article
  17. Histidine-Rich Defensins from theJournal of fungi (Basel, Switzerland) · 2020
    Article
  18. 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 at 1 institution in 1 country.

Tyler G McCaslinSchool of Chemistry and Biochemistry, Georgia Institute of Technology, Atlanta, GA, 30332, USA.
Cynthia V PagbaSchool of Chemistry and Biochemistry, Georgia Institute of Technology, Atlanta, GA, 30332, USA.
Jiby YohannanSchool of Chemistry and Biochemistry, Georgia Institute of Technology, Atlanta, GA, 30332, USA.
Bridgette A BarrySchool of Chemistry and Biochemistry, Georgia Institute of Technology, Atlanta, GA, 30332, USA. bridgette.barry@chemistry.gatech.edu.ORCID http://orcid.org/0000-0003-3421-1407
Georgia Institute of Technology · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Histatin-5 (Hst-5) is an antimicrobial, salivary protein that is involved in the host defense system. Hst-5 has been proposed to bind functionally relevant zinc and copper but presents challenges in structural studies due to its disordered conformation in aqueous solution. Here, we used circular dichroism (CD) and UV resonance Raman (UVRR) spectroscopy to define metallo-Hst-5 interactions in aqueous solution. A zinc-containing Hst-5 sample exhibits shifted Raman bands, relative to bands observed in the absence of zinc. Based on comparison to model compounds and to a family of designed, zinc-binding beta hairpins, the alterations in the Hst-5 UVRR spectrum are attributed to zinc coordination by imidazole side chains. Zinc addition also shifted a tyrosine aromatic ring UVRR band through an electrostatic interaction. Copper addition did not have these effects. A sequence variant, H18A/H19A, was employed; this mutant has less potent antifungal activity, when compared to Hst-5. Zinc addition had only a small effect on the thermal stability of this mutant. Interestingly, both zinc and copper addition shifted histidine UVRR bands in a manner diagnostic for metal coordination. Results obtained with a K13E/R22G mutant were similar to those obtained with wildtype. These experiments show that H18 and H19 contribute to a zinc binding site. In the H18A/H19A mutant the specificity of the copper/zinc binding sites is lost. The experiments implicate specific zinc binding to be important in the antimicrobial activity of Hst-5.

Indexed as

Anti-Infective AgentsBinding SitesCircular DichroismCopperHistatinsIntrinsically Disordered ProteinsMutationProtein BindingSpectrum Analysis, RamanZincAnti-Infective AgentsCopperHistatinsHTN3 protein, humanIntrinsically Disordered ProteinsZinc

Identifiers

PMID31754129
PMCPMC6872563
OpenAlexW2991218382

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.