Evidence map›Paper›PMID 9333052›Full record

ArticleAntimicrobial agents and chemotherapy1997

Studies of the mechanism of human salivary histatin-5 candidacidal activity with histatin-5 variants and azole-sensitive and -resistant Candida species.

H Tsai, L A Bobek

Open access · bronzeAbstract read
In one paragraph

Article in Antimicrobial agents and chemotherapy, 1997. 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
3.3field-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

25 citing papers in PubMed, 73 citations in OpenAlex.

  1. Article
  2. Article
  3. Exploring the Healing Powers of Histatins: From Oral Health to Therapeutics.International journal of molecular sciences · 2025
    Review
  4. Effects of histatin 5 modifications on antifungal activity and kinetics of proteolysis.Protein science : a publication of the Protein Society · 2020
    Article
  5. Article
  6. Article
  7. Article
  8. Histatin peptides: Pharmacological functions and their applications in dentistry.Saudi pharmaceutical journal : SPJ : the official publication of the Saudi Pharmaceutical Society · 2017
    Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Susceptibility of Candida dubliniensis to salivary histatin 3.Antimicrobial agents and chemotherapy · 2003
    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

2 authors at 1 institution in 1 country.

H TsaiDepartment of Oral Biology, School of Dental Medicine, State University of New York at Buffalo, 14214, USA.
L A Bobek
University at Buffalo, State University of New York · US

Funding

SALIVARY PROTEINS--MOLECULAR STUDY OF STRUCTURE/FUNCTIONR01DE009820 · NIDCR · STATE UNIVERSITY OF NEW YORK AT BUFFALO · PI BOBEK, LIBUSE ANNA · 1992 to 2007
$1.7M
NIDCR NIH HHS DE09820
6 · The paper itself

Abstract

Histatins are a group of small, cationic, antifungal peptides present in human saliva. A previous molecular modeling analysis suggested structural similarity between the Phe14-His15 and His18-His19 dipeptide sequences in histatin-5 (Hsn-5; a 24-amino-acid polypeptide) and the sequence of miconazole (one of the azole-based antifungal therapeutic agents), implying that the mechanisms of killing of Candida albicans by these two molecules may be similar. To further elaborate on this observation, we have produced two variants of Hsn-5 in which Phe14-His15 or His18-His19 dipeptide sequences were replaced by Ala-Ala (F14A/H15A and H18A/H19A) to eliminate the phenyl and imidazole rings of the side chains and assessed their candidacidal activities against C. albicans. In addition, we tested azole-resistant C. albicans and Candida glabrata strains for their susceptibilities to Hsn-5. Analysis of the purified recombinant proteins for their candidacidal activities indicated that both variants were significantly less effective (the molar concentrations required to kill half of the maximum number of cells [ED50s], approximately 67 and approximately 149 microM for F14A/H15A and H18A/H19A, respectively) than the unaltered Hsn-5 (ED50, approximately 8 microM) at killing C. albicans, suggesting that the two dipeptide sequences are important for the candidacidal activity of Hsn-5. Assessment of the candidacidal activity of Hsn-5 with the well-characterized azole-resistant strains of C. albicans and C. glabrata, however, suggested that the mode of action of histatins against Candida is distinct from that of azole-based antifungal agents because Hsn-5 kills both azole-sensitive and azole-resistant strains equally well.

Indexed as

Amino AcidsAntifungal AgentsAzolesCandidaCandida albicansCircular DichroismCloning, MolecularDrug Resistance, MicrobialElectrophoresis, Polyacrylamide GelHistatinsHumansMicrobial Sensitivity TestsMutagenesis, Site-DirectedPlasmidsRecombinant ProteinsSalivary Proteins and PeptidesAmino AcidsAntifungal AgentsAzolesHistatinsHTN3 protein, humanRecombinant ProteinsSalivary Proteins and Peptides

Identifiers

PMID9333052
PMCPMC164097
OpenAlexW1946868005

What OpenQuestion holds

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Read underepoch 390

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.