Evidence map›Paper›PMID 15320865›Full record

ArticleThe Biochemical journal2004

Cryptococcal phospholipases: a novel lysophospholipase discovered in the pathogenic fungus Cryptococcus gattii.

Lesley C Wright, Jackie Payne, Rosemary T Santangelo, Mukoma F Simpanya, Sharon C A Chen, Fred Widmer, Tania C Sorrell

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in The Biochemical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.6field-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

19 citing papers in PubMed, 47 citations in OpenAlex.

  1. Influence of the agrochemical benomyl on Cryptococcus gattii-plant interaction in vitro and in vivo.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2024
    Article
  2. The Pathogenic YeastJournal of fungi (Basel, Switzerland) · 2023
    Review
  3. Article
  4. What's New inJournal of fungi (Basel, Switzerland) · 2022
    Review
  5. Gene, virulence and related regulatory mechanisms inActa biochimica et biophysica Sinica · 2022
    Review
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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

7 authors at 2 institutions in 1 country.

Lesley C WrightCentre for Infectious Diseases and Microbiology, University of Sydney at Westmead, Westmead, NSW 2145, Australia. lesleyw@icpmr.wsahs.nsw.gov.au
Jackie Payne
Rosemary T Santangelo
Mukoma F Simpanya
Sharon C A Chen
Fred Widmer
Tania C Sorrell
The University of Sydney · AUWestmead Hospital · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The pathogenic fungus Cryptococcus neoformans produces an extracellular PLB1 (phospholipase B1), shown previously to be a virulence factor. A novel phospholipase (LPL1) with only LPL (lysophospholipase) and LPTA (transacylase) activities has now been characterized in C. gattii, and found to be a 66-kDa glycoprotein (by SDS/PAGE), with a native molecular mass of 670 kDa. The pI was 6.3, and it was active at high temperatures (to 70 degrees C), as well as at both acidic and neutral pH values. It was stimulated by calcium and palmitoyl carnitine at pH 7.0, but not at pH 5.0, and palmitoyl lysophosphatidylcholine was the preferred substrate. Sequencing indicated that LPL1 is a novel cryptococcal lysophospholipase, and not the gene product of CnLYSO1 or PLB1. A protein with only LPL and LPTA activities was subsequently isolated from two strains of C. neoformans var. grubii. A PLB1 enzyme was isolated from both C. gattii and a highly virulent strain of C. neoformans var. grubii (H99). In both cases, all three enzyme activities (PLB, LPL and LPTA) were present in one 95-120 kDa glycoprotein (by SDS/PAGE) with pI 3.9-4.3. Characterization of PLB1 from C. gattii showed that it differed from that of C. neoformans in its larger native mass (275 kDa), high PLB activity relative to LPL and LPTA, and preference for saturated lipid substrates. Differences in the properties between the secreted phospholipases of the two cryptococcal species could contribute to phenotypic differences that determine their respective environmental niches and different clinical manifestations.

Indexed as

Amino Acid SequenceCryptococcusCryptococcus neoformansDatabases, ProteinFungal ProteinsLysophospholipaseMolecular Sequence DataMolecular WeightSpecies SpecificitySubstrate SpecificityVirulenceFungal ProteinsLysophospholipase

Identifiers

PMID15320865
PMCPMC1134121
OpenAlexW2059599738

What OpenQuestion holds

Textmetadata
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.