Evidence map›Paper›PMID 11705911›Full record

ArticleInfection and immunity2001

Nippocystatin, a cysteine protease inhibitor from Nippostrongylus brasiliensis, inhibits antigen processing and modulates antigen-specific immune response.

T Dainichi, Y Maekawa, K Ishii, T Zhang, B F Nashed, T Sakai, M Takashima, K Himeno

Abstract read
In one paragraph

Article in Infection and immunity, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed
6.2field-weighted citation impact, top 3% 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

55 citing papers in PubMed, 127 citations in OpenAlex.

  1. Modulation of the Immune Response by Nematode Derived Molecules.International journal of molecular sciences · 2025
    Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. Cystatin from the helminthFrontiers in immunology · 2024
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. The yin and yang of human soil-transmitted helminth infections.International journal for parasitology · 2021
    Review
  13. Rodent Models for the Study of Soil-Transmitted Helminths: A Proteomics Approach.Frontiers in cellular and infection microbiology · 2021
    Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. Review
  19. Review
  20. 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

8 authors at 1 institution in 1 country.

T DainichiDepartment of Parasitology and Immunology, The University of Tokushima School of Medicine, Tokushima, Japan. dainichi@dermatol.med.kyushu-u.ac.jp
Y Maekawa
K Ishii
T Zhang
B F Nashed
T Sakai
M Takashima
K Himeno
Tokushima University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

During infection, parasites evade the host immune system by modulating or exploiting the immune system; e.g., they suppress expression of major histocompatibility complex class II molecules or secrete cytokine-like molecules. However, it is not clear whether helminths disturb the immune responses of their hosts by controlling the antigen-processing pathways of the hosts. In this study, we identified a new cysteine protease inhibitor, nippocystatin, derived from excretory-secretory (ES) products of an intestinal nematode, Nippostrongylus brasiliensis. Nippocystatin, which belongs to cystatin family 2, consists of 144 amino acids and is secreted as a 14-kDa mature form. In vivo treatment of ovalbumin (OVA)-immunized mice with recombinant nippocystatin (rNbCys) profoundly suppressed OVA-specific proliferation of splenocytes but not non-antigen-specific proliferation of splenocytes. OVA-specific cytokine production was also greatly suppressed in rNbCys-treated mice. Although the serum levels of both OVA-specific immunoglobulin G1 (IgG1) and IgG2a were not affected by rNbCys treatment, OVA-specific IgE was preferentially downregulated in rNbCys-treated mice. In vitro rNbCys inhibited processing of OVA by lysosomal cysteine proteases from the spleens of mice. Mice with anti-nippocystatin antibodies became partially resistant to infection with N. brasiliensis. Based on these findings, N. brasiliensis appears to skillfully evade host immune systems by secreting nippocystatin, which modulates antigen processing in antigen-presenting cells of hosts.

Indexed as

Amino Acid SequenceAnimalsAntibody SpecificityAntigen PresentationAntigens, HelminthCystatinsCysteine Proteinase InhibitorsMiceMice, Inbred BALB CModels, MolecularMolecular Sequence DataNippostrongylusOvalbuminSequence Homology, Amino AcidSpleenStrongylida InfectionsAntigens, HelminthCystatinsCysteine Proteinase Inhibitorsnbcys protein, Nippostrongylus brasiliensisOvalbumin

Identifiers

PMID11705911
PMCPMC98825
OpenAlexW2135449563

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.