Evidence map›Paper›PMID 35377230›Full record

ArticleMicrobiology spectrum2022

Development of Antifungal Peptides against Cryptococcus neoformans; Leveraging Knowledge about the

Robert J Tancer, Yina Wang, Siddhi Pawar, Chaoyang Xue, Gregory R Wiedman

Open access · goldAbstract read
In one paragraph

Article in Microbiology spectrum, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

9 citing papers in PubMed, 12 citations in OpenAlex.

  1. Article
  2. Review
  3. Repositioning Antimicrobial Peptides Against WHO-Priority Fungi.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Functional Analysis of the P-Type ATPases Apt2-4 fromJournal of fungi (Basel, Switzerland) · 2023
    Article
  9. 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

5 authors at 2 institutions in 1 country.

Robert J TancerDepartment of Chemistry and Biochemistry, Seton Hall University, South Orange, New Jersey, USA.
Yina WangPublic Health Research Institute, Department of Microbiology, Biochemistry and Molecular Genetics, New Jersey Medical School, Rutgers University, Newark, New Jersey, USA.
Siddhi PawarPublic Health Research Institute, Department of Microbiology, Biochemistry and Molecular Genetics, New Jersey Medical School, Rutgers University, Newark, New Jersey, USA.
Chaoyang XuePublic Health Research Institute, Department of Microbiology, Biochemistry and Molecular Genetics, New Jersey Medical School, Rutgers University, Newark, New Jersey, USA.
Gregory R WiedmanDepartment of Chemistry and Biochemistry, Seton Hall University, South Orange, New Jersey, USA.ORCID 0000-0002-6720-699X
Rutgers, The State University of New Jersey · USSeton Hall University · US

Funding

The role of inositol in Cryptococcus biology and pathogenesisR01AI123315 · NIAID · RUTGERS BIOMEDICAL AND HEALTH SCIENCES · PI Chaoyang Xue · 2017 to 2026
$5.0M
Role of phospholipids in antifungal drug resistance in Cryptococcus neoformansR01AI155647 · NIAID · RUTGERS BIOMEDICAL AND HEALTH SCIENCES · PI Chaoyang Xue · 2022 to 2026
$2.8M
Lipid flippase in echinocandin drug resistance in Cryptococcus neoformansR21AI154318 · NIAID · RBHS-NEW JERSEY MEDICAL SCHOOL · PI XUE, CHAOYANG · 2020 to 2021
$430k
NIAID NIH HHS R01 AI123315NIAID NIH HHS R01 AI155647NIAID NIH HHS R21 AI154318
6 · The paper itself

Abstract

Cryptococcus neoformans is a major fungal pathogen that often causes life-threatening meningitis in immunocompromised populations. This yeast pathogen is highly resistant to the echinocandin drug caspofungin. Previous studies showed that Cryptococcus lipid translocase (flippase) is required for the caspofungin resistance of that fungus. Mutants with a deleted subunit of lipid flippase, Cdc50, showed increased sensitivity to caspofungin. Here we designed an antifungal peptide targeting the P4-ATPase function. We synthesized stable peptides based on the Cdc50 loop region to identify peptides that can sensitize caspofungin by blocking flippase function and found that myristylated peptides based on the "AS15 sequence" was effective at high concentrations. A modified peptide, "AW9-Ma" showed a MIC of 64 μg/mL against H99 wild type and a fractional inhibitory concentration (FIC) index value of 0.5 when used in combination with caspofungin. Most notably, in the presence of the AW9-Ma peptide, C. neoformans wild type was highly sensitive to caspofungin with a MIC of 4 μg/mL, the same as the

Indexed as

CryptococcosisCryptococcus neoformansAdenosine TriphosphatasesAntifungal AgentsCaspofunginEchinocandinsLeadMicrobial Sensitivity TestsPeptidesAdenosine TriphosphatasesAntifungal AgentsCaspofunginEchinocandinsLeadPeptidesantimicrobial agentsantimicrobial peptidesCryptococcus neoformansdrug synergyfungal meningitisfungiimmunocompromised hostslead compoundsmutantsresistance

Identifiers

PMID35377230
PMCPMC9045296
OpenAlexW4225089644

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.