Evidence map›Paper›PMID 42829974›Full record

ArticleArchives of insect biochemistry and physiology2026

Integrated Transcriptomic and Physiological Analyses Reveal Disruption of Digestive Homeostasis Induced by Protease Inhibitors in Anticarsia gemmatalis Caterpillars.

Neilier Rodrigues da Silva Júnior, Eulálio Gutemberg Dias Dos Santos, Daniel Guimarães Silva Paulo, Yaremis Meriño-Cabrera, Ian de Paula Alves Pinto, Maria Julia Summy, Ian Lucas Batista Santos, Milena Godoi Lima, Maria Clara Neves Gomes Rodrigues, Rafael Junior de Andrade and 4 more

Abstract read
In one paragraph

Article in Archives of insect biochemistry and physiology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
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

1 citing paper in PubMed.

  1. 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

14 authors.

Neilier Rodrigues da Silva JúniorDepartment of Biochemistry and Molecular Biology, Laboratory of Enzymology and Biochemistry of Proteins and Peptides, Universidade Federal de Viçosa, UFV, BIOAGRO/INCT-IPP, Viçosa, Brazil.ORCID https://orcid.org/0000-0002-4683-249X
Eulálio Gutemberg Dias Dos SantosDepartment of Biochemistry and Molecular Biology, Laboratory of Enzymology and Biochemistry of Proteins and Peptides, Universidade Federal de Viçosa, UFV, BIOAGRO/INCT-IPP, Viçosa, Brazil.ORCID https://orcid.org/0009-0006-1585-8108
Daniel Guimarães Silva PauloDepartment of Biochemistry and Molecular Biology, Laboratory of Enzymology and Biochemistry of Proteins and Peptides, Universidade Federal de Viçosa, UFV, BIOAGRO/INCT-IPP, Viçosa, Brazil.ORCID https://orcid.org/0009-0007-5790-187X
Yaremis Meriño-CabreraDepartment of Biochemistry and Molecular Biology, Laboratory of Enzymology and Biochemistry of Proteins and Peptides, Universidade Federal de Viçosa, UFV, BIOAGRO/INCT-IPP, Viçosa, Brazil.ORCID https://orcid.org/0000-0002-5712-9759
Ian de Paula Alves PintoDepartment of Biochemistry and Molecular Biology, Laboratory of Enzymology and Biochemistry of Proteins and Peptides, Universidade Federal de Viçosa, UFV, BIOAGRO/INCT-IPP, Viçosa, Brazil.ORCID https://orcid.org/0009-0000-1848-2966
Maria Julia SummyDepartment of Biochemistry and Molecular Biology, Laboratory of Enzymology and Biochemistry of Proteins and Peptides, Universidade Federal de Viçosa, UFV, BIOAGRO/INCT-IPP, Viçosa, Brazil.
Ian Lucas Batista SantosDepartment of Biochemistry and Molecular Biology, Laboratory of Enzymology and Biochemistry of Proteins and Peptides, Universidade Federal de Viçosa, UFV, BIOAGRO/INCT-IPP, Viçosa, Brazil.ORCID https://orcid.org/0009-0001-2761-7022
Milena Godoi LimaDepartment of Biochemistry and Molecular Biology, Laboratory of Enzymology and Biochemistry of Proteins and Peptides, Universidade Federal de Viçosa, UFV, BIOAGRO/INCT-IPP, Viçosa, Brazil.ORCID https://orcid.org/0009-0002-1620-211X
Maria Clara Neves Gomes RodriguesDepartment of Biochemistry and Molecular Biology, Laboratory of Enzymology and Biochemistry of Proteins and Peptides, Universidade Federal de Viçosa, UFV, BIOAGRO/INCT-IPP, Viçosa, Brazil.ORCID https://orcid.org/0009-0006-5409-2379
Rafael Junior de AndradeDepartment of Biochemistry and Molecular Biology, Laboratory of Enzymology and Biochemistry of Proteins and Peptides, Universidade Federal de Viçosa, UFV, BIOAGRO/INCT-IPP, Viçosa, Brazil.ORCID https://orcid.org/0000-0003-3162-7888
José Eduardo SerrãoDepartment of General Biology, Universidade Federal de Viçosa, Viçosa, Brazil.ORCID https://orcid.org/0000-0002-0477-4252
Elizabeth Pacheco Batista FontesDepartment of Biochemistry and Molecular Biology, Laboratory of Plant Molecular Biology, Universidade Federal de Viçosa, UFV, BIOAGRO/INCT-IPP, Viçosa, Brazil.ORCID https://orcid.org/0000-0002-7986-1369
Humberto Josué Oliveira RamosDepartment of Biochemistry and Molecular Biology, Laboratory of Enzymology and Biochemistry of Proteins and Peptides, Universidade Federal de Viçosa, UFV, BIOAGRO/INCT-IPP, Viçosa, Brazil.ORCID https://orcid.org/0000-0001-6447-8108
Maria Goreti de Almeida OliveiraDepartment of Biochemistry and Molecular Biology, Laboratory of Enzymology and Biochemistry of Proteins and Peptides, Universidade Federal de Viçosa, UFV, BIOAGRO/INCT-IPP, Viçosa, Brazil.ORCID https://orcid.org/0000-0003-4862-7657

Funding

Conselho Nacional de Desenvolvimento CientÍfico e TecnolÓgicoCoordenaÇÃo de AperfeiÇoamento de Pessoal de NÍvel Superior 001FundaÇÃo de Amparo À Pesquisa do Estado de Minas Gerais
6 · The paper itself

Abstract

Protease inhibitors (PIs) are promising bioactive compounds for sustainable pest management because they interfere with the digestive processes of herbivorous insects. However, the physiological mechanisms underlying insect adaptation to natural and synthetic PIs remain poorly understood. Here, we investigated the midgut responses of Anticarsia gemmatalis Hübner (Lepidoptera: Erebidae) to the soybean Kunitz trypsin inhibitor (SKTI) and the synthetic tripeptide GORE-2 using integrated transcriptomic, biochemical, and histological approaches, complemented by an exploratory metatranscriptomic analysis of putative gut-associated microbial transcripts. RNA-seq analysis identified 2542 unique differentially expressed genes (FDR-adjusted p < 0.05, |log2FC | ≥ 1), including extensive modulation of digestive proteases and redox-related pathways. SKTI induced a compensatory response characterized by the up-regulation of serine proteases, antioxidant enzymes, and detoxification-associated pathways. In contrast, GORE-2 promoted broader repression of digestive proteases, including chymotrypsin- and trypsin-related transcripts and matrix metalloproteinases, together with a distinct antioxidant response. Biochemical assays demonstrated increased CAT, GST, POX, and SOD activities under both treatments. Compared with SKTI, GORE-2 induced lower POX, GST, and SOD activities, whereas CAT activity did not differ significantly between the two treatments. Histological analyses demonstrated notable epithelial disruption, vacuolization, and disorganization of the striated border in the larval midgut, with lesion scores being significantly elevated following GORE-2 exposure. Exploratory analysis of putative gut-associated microbial transcripts recovered from whole-midgut RNA-seq revealed taxonomically diverse microbial signals associated with carbon metabolism, proteolysis, and detoxification. However, no treatment-associated differential expression was detected among the putative bacterial transcripts. These findings indicate that GORE-2 induced broader disruption of digestive and protective midgut functions than SKTI, with weaker antioxidant enzyme induction and more pronounced histological injury, consistent with reduced physiological compensation in A. gemmatalis larvae. These results underscore the potential of synthetic peptide-based protease inhibitors to interfere with adaptive digestive processes in pest insects of agricultural importance.

Indexed as

MothsOligopeptidesProtease InhibitorsTrypsin Inhibitor, Kunitz SoybeanAnimalsGastrointestinal MicrobiomeGastrointestinal TractHomeostasisInsect ProteinsLarvaTranscriptomeInsect ProteinsOligopeptidesProtease InhibitorsTrypsin Inhibitor, Kunitz Soybeandigestive proteasesmidgut transcriptomeoxidative stressprotease inhibitors

Identifiers

PMID42829974
PMCPMC13634601

What Socratic 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 Socratic graph.