Evidence map›Paper›PMID 19006817›Full record

ArticleMolecular microbiology2008

Uptake of the antifungal cationic peptide Histatin 5 by Candida albicans Ssa2p requires binding to non-conventional sites within the ATPase domain.

Jianing N Sun, Wansheng Li, Woong Sik Jang, Namrata Nayyar, Mark D Sutton, Mira Edgerton

Open access · greenAbstract read
In one paragraph

Article in Molecular microbiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.0field-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

23 citing papers in PubMed, 51 citations in OpenAlex.

  1. Article
  2. Exploring the Healing Powers of Histatins: From Oral Health to Therapeutics.International journal of molecular sciences · 2025
    Review
  3. Microorganisms · 2025
    Review
  4. Article
  5. Review
  6. Article
  7. Bioactive Peptides Against Fungal Biofilms.Frontiers in microbiology · 2019
    Review
  8. Review
  9. Review
  10. Antibiofilm peptides against oral biofilms.Journal of oral microbiology · 2017
    Article
  11. Review
  12. Review
  13. Review
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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 2 institutions in 1 country.

Jianing N SunDepartment of Oral Biology, School of Dental Medicine, Public Health and Health Professions and Biomedical Sciences, University at Buffalo, Buffalo, NY 14214, USA.
Wansheng Li
Woong Sik Jang
Namrata Nayyar
Mark D Sutton
Mira Edgerton
University at Buffalo, State University of New York · USCancer Research And Biostatistics · US

Funding

Supplements to Support Candida DNA Microarray FacilitiesR01DE010641 · NIDCR · STATE UNIVERSITY OF NEW YORK AT BUFFALO · PI EDGERTON, MIRA · 2000 to 2019
$6.7M
CANDIDACIDAL MECHANISMS OF SALIVARY HISTATINSR29DE010641 · NIDCR · STATE UNIVERSITY OF NEW YORK AT BUFFALO · PI EDGERTON, MIRA · 1994 to 1998
–
NIDCR NIH HHS DE10641NIDCR NIH HHS R01 DE010641
6 · The paper itself

Abstract

Candida albicans Hsp70 Ssa1/2 proteins have been identified as cell wall binding partners for the antifungal cationic peptide Histatin 5 (Hst 5) in vivo. C. albicans Ssa2p plays a major role in binding and translocation of Hst 5 into fungal cells, as demonstrated by defective peptide uptake and killing in C. albicans SSA2 null mutants. Candidal Hsp70 proteins are classical chaperone proteins with two discrete functional domains consisting of peptide binding and ATP binding regions. Pull-down assays with full-length and truncated Ssa2 proteins found that the ATPase domain was required for Hst 5 binding. Further mapping of Ssa2p by limited digestion and peptide array analyses identified two discrete Hst 5-binding epitopes within the ATPase region. Expression of Ssa2p in C. albicans cells carrying mutations in the first epitope identified by thermolysin digestion (Ssa2128-132A3) significantly reduced intracellular transport and fungicidal activity of Hst 5, confirming its importance as a binding site for Hst 5 function in vivo. Since this Hst 5 binding site lies within the Ssa2p ATPase domain near the ATP-binding cleft, it is possible that ATP modulates Hst 5 binding to Ssa2p. Indeed, gel filtration assays demonstrated that although nucleotides are not required for Hst 5 binding, their presence improved binding affinity by 10-fold. Thus, C. albicans Ssa2p binds Hst 5 at a surface-localized epitope in a subunit of the ATPase domain; and this region is required for intracellular translocation and killing functions of Hst 5.

Indexed as

Adenosine TriphosphatasesAmino Acid SequenceBinding SitesCandida albicansDNA, FungalEpitope MappingFungal ProteinsHistatinsHSP70 Heat-Shock ProteinsHumansMolecular Sequence DataMutagenesis, Site-DirectedMutationProtein BindingProtein Structure, SecondaryProtein Structure, TertiaryAdenosine TriphosphatasesDNA, FungalFungal ProteinsHistatinsHSP70 Heat-Shock ProteinsHTN3 protein, humanRecombinant Proteins

Identifiers

PMID19006817
PMCPMC2643122
OpenAlexW2063656851

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.