Evidence map›Paper›PMID 37074531›Full record

ArticleCell stress & chaperones2023

Human granzyme B binds Plasmodium falciparum Hsp70-x and mediates antiplasmodial activity in vitro.

Lebogang Ramatsui, Tendamudzimu Harmfree Dongola, Tawanda Zininga, Gabriele Multhoff, Addmore Shonhai

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Cell stress & chaperones, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.3field-weighted citation impact, top 38% 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

2 citing papers in PubMed, 2 citations in OpenAlex.

  1. Article
  2. 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 3 institutions in 2 countries.

Lebogang RamatsuiDepartment of Biochemistry and Microbiology, Faculty of Science, University of Venda, Engineering & Agriculture, Thohoyandou, 0950, Limpopo, South Africa.
Tendamudzimu Harmfree DongolaDepartment of Biochemistry and Microbiology, Faculty of Science, University of Venda, Engineering & Agriculture, Thohoyandou, 0950, Limpopo, South Africa.
Tawanda ZiningaDepartment of Biochemistry and Microbiology, Faculty of Science, University of Venda, Engineering & Agriculture, Thohoyandou, 0950, Limpopo, South Africa.
Gabriele MulthoffKlinik Und Poliklinik Für Strahlentherapie Und Radiologische Onkologie, Klinikum Rechts Der Isar and Central Institute for Translational Cancer Research TU München, TranslaTUM) Einsteinstr. 25, 81675, Munich, Germany.
Addmore ShonhaiDepartment of Biochemistry and Microbiology, Faculty of Science, University of Venda, Engineering & Agriculture, Thohoyandou, 0950, Limpopo, South Africa. addmore.shonhai@univen.ac.za.ORCID 0000-0003-3203-0602
University of Venda · ZAKlinik und Poliklinik für Strahlentherapie und Radioonkologie · DEStellenbosch University · ZA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cell surface-bound human Hsp70 (hHsp70) sensitises tumour cells to the cytolytic attack of natural killer (NK) cells through the mediation of apoptosis-inducing serine protease, granzyme B (GrB). hHsp70 is thought to recruit NK cells to the immunological synapse via the extracellularly exposed 14 amino acid sequence, TKDNNLLGRFELSG, known as the TKD motif of Hsp70. Plasmodium falciparum-infected red blood cells (RBCs) habour both hHsp70 and an exported parasite Hsp70 termed PfHsp70-x. Both PfHsp70-x and hHsp70 share conserved TKD motifs. The role of PfHsp70-x in facilitating GrB uptake in malaria parasite-infected RBCs remains unknown, but hHsp70 enables a perforin-independent uptake of GrB into tumour cells. In the current study, we comparatively investigated the direct binding of GrB to either PfHsp70-x or hHsp70 in vitro. Using ELISA, slot blot assay and surface plasmon resonance (SPR) analysis, we demonstrated a direct interaction of GrB with hHsp70 and PfHsp70-x. SPR analysis revealed a higher affinity of GrB for PfHsp70-x than hHsp70. In addition, we established that the TKD motif of PfHsp70-x directly interacts with GrB. The data further suggest that the C-terminal EEVN motif of PfHsp70-x augments the affinity of PfHsp70-x for GrB but is not a prerequisite for the binding. A potent antiplasmodial activity (IC

Indexed as

AntimalarialsNeoplasmsGranzymesHSP70 Heat-Shock ProteinsHumansPlasmodium falciparumProtein BindingAntimalarialsGranzymesHSP70 Heat-Shock ProteinsGranzyme BHeat shock proteinsMalariaPfHsp70-xPlasmodium falciparum

Identifiers

PMID37074531
PMCPMC10167072
OpenAlexW4366351955

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.