Evidence map›Paper›PMID 41700843›Full record

ArticleArchives of insect biochemistry and physiology2026

Molecular and Structural Characterization of Foam Proteins from Mahanarva spectabilis (Distant, 1909) (Hemiptera: Cercopidae) Nymphs Reveals Adaptive Features and Potential Targets for Pest Control.

Angelo José Rinaldi, Monique da Silva Bonjour, Ian de Paula Alves Pinto, Gabriely Teixeira Bhering Faria, Lucas Leal Lima, Marcela Chellini Pereira, Alexander Machado Auad, Jorge Fernando Pereira, Maria Goreti Almeida Oliveira, Humberto Josué de Oliveira Ramos

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

10 authors.

Angelo José RinaldiLaboratory of Enzymology and Biochemistry of Proteins and Peptides, Department of Biochemistry and Molecular Biology, Universidade Federal de Viçosa, UFV, BIOAGRO/INCT-IPP, Viçosa-MG, Brazil.ORCID https://orcid.org/0000-0001-6392-6976
Monique da Silva BonjourLaboratory of Enzymology and Biochemistry of Proteins and Peptides, Department of Biochemistry and Molecular Biology, Universidade Federal de Viçosa, UFV, BIOAGRO/INCT-IPP, Viçosa-MG, Brazil.ORCID https://orcid.org/0009-0000-8830-9704
Ian de Paula Alves PintoLaboratory of Enzymology and Biochemistry of Proteins and Peptides, Department of Biochemistry and Molecular Biology, Universidade Federal de Viçosa, UFV, BIOAGRO/INCT-IPP, Viçosa-MG, Brazil.ORCID https://orcid.org/0009-0000-1848-2966
Gabriely Teixeira Bhering FariaLaboratory of Enzymology and Biochemistry of Proteins and Peptides, Department of Biochemistry and Molecular Biology, Universidade Federal de Viçosa, UFV, BIOAGRO/INCT-IPP, Viçosa-MG, Brazil.ORCID https://orcid.org/0009-0002-6473-9990
Lucas Leal LimaLaboratory of Enzymology and Biochemistry of Proteins and Peptides, Department of Biochemistry and Molecular Biology, Universidade Federal de Viçosa, UFV, BIOAGRO/INCT-IPP, Viçosa-MG, Brazil.ORCID https://orcid.org/0009-0000-8064-4284
Marcela Chellini PereiraLaboratory of Enzymology and Biochemistry of Proteins and Peptides, Department of Biochemistry and Molecular Biology, Universidade Federal de Viçosa, UFV, BIOAGRO/INCT-IPP, Viçosa-MG, Brazil.ORCID https://orcid.org/0009-0004-0124-0126
Alexander Machado AuadEmbrapa Dairy Cattle, Juiz de Fora, Brazil.ORCID https://orcid.org/0000-0002-3420-201X
Jorge Fernando PereiraEmbrapa Dairy Cattle, Juiz de Fora, Brazil.ORCID https://orcid.org/0000-0001-9340-065X
Maria Goreti Almeida OliveiraLaboratory of Enzymology and Biochemistry of Proteins and Peptides, Department of Biochemistry and Molecular Biology, Universidade Federal de Viçosa, UFV, BIOAGRO/INCT-IPP, Viçosa-MG, Brazil.ORCID https://orcid.org/0000-0003-4862-7657
Humberto Josué de Oliveira RamosLaboratory of Enzymology and Biochemistry of Proteins and Peptides, Department of Biochemistry and Molecular Biology, Universidade Federal de Viçosa, UFV, BIOAGRO/INCT-IPP, Viçosa-MG, Brazil.ORCID https://orcid.org/0000-0001-6447-8108

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

During its nymphal development, the spittlebug Mahanarva spectabilis (Distant, 1909) (Hemiptera: Cercopidae) secretes a persistent extracellular foam that functions as a multifunctional barrier against environmental stressors. In this study, we present a molecular and structural characterization of the foam proteins using LC-MS/MS and AlphaFold-based structural modeling. Although no significant differences were observed in total protein concentration across different host plant genotypes, proteomic analyses revealed the down-regulation of specific high-abundance proteins in nymphs feeding on resistant/moderately resistant grasses. This suggests a potential impairment of foam functionality and reduced nymphal fitness under field conditions. Peptides from individual SDS-PAGE bands mapped to multiple distinct unigenes, indicating that proteins encoded by different transcripts share highly conserved sequence motifs, domain architectures, and structural folds. This was particularly evident for the most abundant protein, likely reflecting post-translational modifications such as signal peptide cleavage, proteolytic processing, or alternative splicing. AlphaFold structural predictions revealed the presence of adhesive and matrix-related domains, such as WSC, S-layer, ankyrin repeats, and apolipophorin folds, across several foam proteins. The dominance of extended α-helices and the predicted dimerization interfaces reinforce the hypothesis that these proteins participate in the formation of supramolecular scaffolds essential for the mechanical stability and adhesion of the foam. Collectively, these findings suggest that M. spectabilis foam proteins have undergone evolutionary specialization to assemble a multifunctional extracellular matrix that ensures nymphal protection. These insights highlight potential molecular targets for novel pest control strategies and contribute to the broader understanding of insect-derived extracellular secretions with biomimetic relevance.

Indexed as

HemipteraInsect ProteinsAmino Acid SequenceAnimalsNymphInsect ProteinsAlphaFold structural modelingbiocontrol targetsinsect extracellular matrixplant defense

Identifiers

PMID41700843
PMCPMC12911473

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Registered trials

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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.