Evidence map›Paper›PMID 33789282›Full record

ArticleJournal of innate immunity2021

A Thermally Stable Protein EPP1 of Corn Borer Ostrinia furnacalis Regulates Hemocytic Encapsulation.

Jian Hu, Xiangping Feng, Li Yao, Meng Meng, Yan Du, Yipei Dong, Zhenkun Song, Mengli Tian, Yu Chen

Open access · goldAbstract read
In one paragraph

Article in Journal of innate immunity, 2021. 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
0.4field-weighted citation impact, top 43% 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, 7 citations in OpenAlex.

  1. Article
  2. Functional Analysis ofInsects · 2026
    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

9 authors at 1 institution in 1 country.

Jian HuSchool of Agriculture, Sun Yat-Sen University, Guangzhou, China.
Xiangping FengState key Laboratory of Biocontrol, School of life sciences, Sun Yat-Sen University, Guangzhou, China.
Li YaoState key Laboratory of Biocontrol, School of life sciences, Sun Yat-Sen University, Guangzhou, China.
Meng MengState key Laboratory of Biocontrol, School of life sciences, Sun Yat-Sen University, Guangzhou, China.
Yan DuState key Laboratory of Biocontrol, School of life sciences, Sun Yat-Sen University, Guangzhou, China.
Yipei DongState key Laboratory of Biocontrol, School of life sciences, Sun Yat-Sen University, Guangzhou, China.
Zhenkun SongState key Laboratory of Biocontrol, School of life sciences, Sun Yat-Sen University, Guangzhou, China.
Mengli TianState key Laboratory of Biocontrol, School of life sciences, Sun Yat-Sen University, Guangzhou, China.
Yu ChenState key Laboratory of Biocontrol, School of life sciences, Sun Yat-Sen University, Guangzhou, China.
Sun Yat-sen University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Encapsulation is a vital cellular immune reaction of host insects against endoparasitoids; however, how encapsulation is regulated is still unclear. Utilizing a cell line, SYSU-OfHem C, derived from larval hemocytes of the Asian corn borer Ostrinia furnacalis to assay for encapsulation response, an encapsulation-promoting protein (OfEPP1) was isolated from the plasma of O. furnacalis larvae. OfEPP1 is a novel secretory protein, which exists only in O. furnacalis to date. The OfEpp1 gene is intronless and encodes a protein containing several groups of short repetitive sequences and a high proportion of proline residues (18.3%). OfEPP1 is a thermally stable protein that is mainly expressed in fat bodies, and its accumulation could be induced by the injection of foreign objects (Sephadex beads). Eukaryotically expressed recombinant OfEPP1 promoted hemocytes to encapsulate Sephadex beads, while prokaryotically expressed protein did not, indicating that posttranscriptional modification affects the function of OfEPP1. The encapsulation-promoting function of OfEPP1 could be neutralized by the addition of polyclonal antibodies against OfEPP1 or disrupted by the injection of dsRNA targeting OfEpp1. Eukaryotically expressed OfEPP1 promoted the aggregation, but not spreading, of both granulocytes and plasmatocytes. Immunocytochemistry analysis showed that eukaryotically expressed OfEPP1 could bind to the surface of hemocytes. Therefore, we speculate that OfEPP1 possibly promotes hemocytic encapsulation by binding to the surface of hemocytes as a ligand to induce their aggregation. This study provides evidence clarifying the mechanism of encapsulation in insects.

Indexed as

HemocytesMothsAnimalsInsect ProteinsLarvaZea maysInsect ProteinsAggregationEncapsulation-promoting proteinHemocytesInsect cellular immunityPlasma

Identifiers

PMID33789282
PMCPMC8460984
OpenAlexW3147209700

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.