Evidence map›Paper›PMID 39060200›Full record

ArticleVaccine2024

In vitro identification of neutralizing epitopes of Rhipicephalus microplus serpin 17 (RmS-17).

Pedro Machado Medeiros de Albuquerque, Jan Kotál, Maria Aparecida Juliano, Lucas Tirloni, Itabajara da Silva Vaz

Abstract read
In one paragraph

Article in Vaccine, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Article
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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.

Pedro Machado Medeiros de AlbuquerqueCentro de Biotecnologia, Universidade Federal do Rio Grande do Sul (UFRGS), RS, Brazil; Tick-Pathogen Transmission Unit, Laboratory of Bacteriology, National Institute of Allergy and Infectious Diseases, Hamilton, MT, USA.
Jan KotálTick-Pathogen Transmission Unit, Laboratory of Bacteriology, National Institute of Allergy and Infectious Diseases, Hamilton, MT, USA.
Maria Aparecida JulianoDepartamento de Biofísica, Universidade Federal de São Paulo, SP, Brazil.
Lucas TirloniTick-Pathogen Transmission Unit, Laboratory of Bacteriology, National Institute of Allergy and Infectious Diseases, Hamilton, MT, USA.
Itabajara da Silva VazCentro de Biotecnologia, Universidade Federal do Rio Grande do Sul (UFRGS), RS, Brazil; Faculdade de Veterinária, Universidade Federal do Rio Grande do Sul (UFRGS), RS, Brazil; Instituto Nacional de Ciência e Tecnologia - Entomologia Molecular, Rio de Janeiro, RJ, Brazil. Electronic address: itabajara.vaz@ufrgs.br.

Funding

Tick saliva and its importance for tick feeding and pathogen transmissionZIAAI001337 · NIAID · NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES · PI TIRLONI, LUCAS · 2021 to 2025
$8.5M
Intramural NIH HHS Z99 AI999999Intramural NIH HHS ZIA AI001337
6 · The paper itself

Abstract

backgroundRhipicephalus microplus poses a significant problem for livestock worldwide and is primarily controlled with synthetic acaricides. The continuous use of acaricides results in the selection of resistance and causes environmental harm. Vaccination presents an alternative solution to this problem, although searching for the suitable antigen is still a work in progress. Salivary proteins hold promise for inclusion in vaccine formulation due to their roles in modulating host responses, assisting blood feeding and pathogen transmission. Serpins are a class of proteinase inhibitors and are among the molecules found in tick saliva that modulate host blood coagulation, inflammation, and adaptive immune responses. Previous studies have demonstrated the potential of R. microplus serpin 17 (RmS-17) to interfere with the host's defenses, and antibodies have been shown to neutralize its effects. This makes RmS-17 an putative target for vaccine development.

methodsEpitope mapping of RmS-17 was achieved using in silico approach combining linear B-cell epitope and antigenicity predictor. In addition, epitope mapping using overlapping peptides in an ELISA screening was used. The serpin tridimensional structure and the epitopes spatial location within the molecule were determined. Peptides were synthetized based on the predictions and used for the production of rabbit anti-sera. Purified IgG's were used to assess the antibodies capacity to neutralize RmS-17.

resultsThrough in silico mapping, nine potential B cell epitope regions were screened, with p1RmS-17 and p2RmS-17 selected for the experiment based on antigen prediction. In the ELISA screening using overlapping peptides, eight antibody-binding regions were identified, and p3RmS-17 and p4RmS-17 were chosen. Antibodies raised against p3RmS-17 and p4RmS-17 partially neutralized RmS-17 activity.

conclusionIt was found that antibodies against a single epitope are sufficient to partially neutralize RmS-17 activity. These findings support the possibility of using an epitope-based vaccine for immunization against R. microplus.

Indexed as

Epitope MappingRhipicephalusSerpinsAnimalsAntibodies, NeutralizingArthropod ProteinsEnzyme-Linked Immunosorbent AssayEpitopes, B-LymphocyteImmunoglobulin GRabbitsAntibodies, NeutralizingArthropod ProteinsEpitopes, B-LymphocyteImmunoglobulin GSerpinsEpitope-based vaccineSerpinTick saliva

Identifiers

PMID39060200
PMCPMC11456362

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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.