Evidence map›Paper›PMID 9488383›Full record

ArticleInfection and immunity1998

MP1 encodes an abundant and highly antigenic cell wall mannoprotein in the pathogenic fungus Penicillium marneffei.

L Cao, C M Chan, C Lee, S S Wong, K Y Yuen

Open access · bronzeAbstract read
In one paragraph

Article in Infection and immunity, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed
3.5field-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

58 citing papers in PubMed, 106 citations in OpenAlex.

  1. Development and Clinical Evaluation of a Novel Talaromyces marneffei Mp1p Lateral Flow Assay for Rapid Diagnosis of Talaromycosis.Clinical infectious diseases : an official publication of the Infectious Diseases Society of America · 2026
    Article
  2. Review
  3. Clinical Performance of a Mp1p Antibody Detection Immunoassay For Talaromycosis.medRxiv : the preprint server for health sciences · 2026
    Article
  4. Article
  5. Review
  6. Article
  7. Review
  8. The Contribution of Human Antimicrobial Peptides to Fungi.International journal of molecular sciences · 2025
    Review
  9. Article
  10. Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. Review
  16. Evaluation of the yeast phase-specific monoclonal antibody 4D1 andFrontiers in cellular and infection microbiology · 2023
    Article
  17. Article
  18. Review
  19. Superiority of a Novel Mp1p Antigen Detection Enzyme Immunoassay Compared to Standard BACTEC Blood Culture in the Diagnosis of Talaromycosis.Clinical infectious diseases : an official publication of the Infectious Diseases Society of America · 2021
    Article
  20. Diagnosis of Pulmonary Infections Due to Endemic Fungi.Diagnostics (Basel, Switzerland) · 2021
    Review
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 2 countries.

L CaoDepartment of Microbiology, The University of Hong Kong. lcao@hkucc.hku.hk
C M Chan
C Lee
S S Wong
K Y Yuen
Chinese University of Hong Kong · CNUniversity of Hong Kong · HK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We cloned the MP1 gene, which encodes an abundant antigenic cell wall mannoprotein from the dimorphic pathogenic fungus Penicillium marneffei. MP1 is a unique gene without homologs in sequence databases. It codes for a protein, Mp1p, of 462 amino acid residues, with a few sequence features that are present in several cell wall proteins of Saccharomyces cerevisiae and Candida albicans. It contains two putative N glycosylation sites, a serine- and threonine-rich region for O glycosylation, a signal peptide, and a putative glycosylphosphatidylinositol attachment signal sequence. Specific anti-Mp1p antibody was generated with recombinant Mp1p protein purified from Escherichia coli to allow further characterization of Mp1p. Western blot analysis with anti-Mp1p antibody revealed that Mp1p has predominant bands with molecular masses of 58 and 90 kDa and that it belongs to a group of cell wall proteins that can be readily removed from yeast cell surfaces by glucanase digestion. In addition, Mp1p is an abundant yeast glycoprotein and has high affinity for concanavalin A, a characteristic indicative of a mannoprotein. Furthermore, ultrastructural analysis with immunogold staining indicated that Mp1p is present in the cell walls of the yeast, hyphae, and conidia of P. marneffei. Finally, it was observed that infected patients develop a specific antibody response against Mp1p, suggesting that this protein represents a good cell surface target for host humoral immunity.

Indexed as

Genes, FungalAmino Acid SequenceAnimalsAntibodies, FungalAntigens, FungalBase SequenceCloning, MolecularDNA, FungalFungal ProteinsGuinea PigsHumansMembrane GlycoproteinsMolecular Sequence DataPenicilliumRabbitsAntibodies, FungalAntigens, FungalDNA, FungalFungal ProteinsmannoproteinsMembrane Glycoproteins

Identifiers

PMID9488383
PMCPMC108003
OpenAlexW1963198502

What OpenQuestion holds

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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.