Host-specific targets of Histomonas meleagridis antigens revealed by immunoprecipitation

Abstract Histomonas meleagridis, a protozoan parasite responsible for histomonosis (syn. Blackhead disease, histomoniasis), presents an increasing challenge for poultry health, particularly with the ban of licensed prophylactic and treatment options. Recent studies have explored H. meleagridis prote...

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Main Authors: Marcelo de Jesus Ramires, Karin Hummel, Tamas Hatfaludi, Michael Hess, Ivana Bilic
Format: Article
Language:English
Published: Nature Portfolio 2025-02-01
Series:Scientific Reports
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Online Access:https://doi.org/10.1038/s41598-025-88855-y
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author Marcelo de Jesus Ramires
Karin Hummel
Tamas Hatfaludi
Michael Hess
Ivana Bilic
author_facet Marcelo de Jesus Ramires
Karin Hummel
Tamas Hatfaludi
Michael Hess
Ivana Bilic
author_sort Marcelo de Jesus Ramires
collection DOAJ
description Abstract Histomonas meleagridis, a protozoan parasite responsible for histomonosis (syn. Blackhead disease, histomoniasis), presents an increasing challenge for poultry health, particularly with the ban of licensed prophylactic and treatment options. Recent studies have explored H. meleagridis proteome, exoproteome, and surfaceome, linking molecular data to virulence and in vitro attenuation. Nevertheless, proteins involved in interactions with hosts remain largely unknown. In this study, we conducted immunoproteome analyses to identify key antigens involved in the humoral immune response of the parasite’s main hosts, turkeys and chickens. Immunogenic proteins were isolated via immunoprecipitation using sera from chickens and turkeys that were vaccinated with a single attenuated strain and challenged with virulent strains of the protozoan, respectively. Mass spectrometry identified 155 putative H. meleagridis immunogenic proteins, of which 43 were recognized by sera from both hosts. In silico antigenicity screening (VaxElan) identified 33 pan-reactive antigens, with VaxiDL further highlighting 10 as potential vaccine candidates. Comparative analysis revealed host-specific immune responses, with 16 differential immunogenic proteins in chickens (6 specific to virulent and 10 to attenuated preparations) and 19 unique proteins in turkeys, all associated with virulent strains. These results enhance our understanding of H. meleagridis immunogenic protein dynamics and host-pathogen specificities, supporting the development of improved diagnostic tools and potential protective measures against the infection.
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spelling doaj-art-61d3f19a666b468aa47512d93872002f2025-08-20T02:14:59ZengNature PortfolioScientific Reports2045-23222025-02-0115111810.1038/s41598-025-88855-yHost-specific targets of Histomonas meleagridis antigens revealed by immunoprecipitationMarcelo de Jesus Ramires0Karin Hummel1Tamas Hatfaludi2Michael Hess3Ivana Bilic4Clinic for Poultry and Fish Medicine, Department for Farm Animals and Food System Science, University of Veterinary Medicine ViennaVetCore Facility for Research, University of Veterinary Medicine ViennaClinic for Poultry and Fish Medicine, Department for Farm Animals and Food System Science, University of Veterinary Medicine ViennaClinic for Poultry and Fish Medicine, Department for Farm Animals and Food System Science, University of Veterinary Medicine ViennaClinic for Poultry and Fish Medicine, Department for Farm Animals and Food System Science, University of Veterinary Medicine ViennaAbstract Histomonas meleagridis, a protozoan parasite responsible for histomonosis (syn. Blackhead disease, histomoniasis), presents an increasing challenge for poultry health, particularly with the ban of licensed prophylactic and treatment options. Recent studies have explored H. meleagridis proteome, exoproteome, and surfaceome, linking molecular data to virulence and in vitro attenuation. Nevertheless, proteins involved in interactions with hosts remain largely unknown. In this study, we conducted immunoproteome analyses to identify key antigens involved in the humoral immune response of the parasite’s main hosts, turkeys and chickens. Immunogenic proteins were isolated via immunoprecipitation using sera from chickens and turkeys that were vaccinated with a single attenuated strain and challenged with virulent strains of the protozoan, respectively. Mass spectrometry identified 155 putative H. meleagridis immunogenic proteins, of which 43 were recognized by sera from both hosts. In silico antigenicity screening (VaxElan) identified 33 pan-reactive antigens, with VaxiDL further highlighting 10 as potential vaccine candidates. Comparative analysis revealed host-specific immune responses, with 16 differential immunogenic proteins in chickens (6 specific to virulent and 10 to attenuated preparations) and 19 unique proteins in turkeys, all associated with virulent strains. These results enhance our understanding of H. meleagridis immunogenic protein dynamics and host-pathogen specificities, supporting the development of improved diagnostic tools and potential protective measures against the infection.https://doi.org/10.1038/s41598-025-88855-yHistomonas meleagridisImmunoprecipitationLCMSVirulenceHistomonosis
spellingShingle Marcelo de Jesus Ramires
Karin Hummel
Tamas Hatfaludi
Michael Hess
Ivana Bilic
Host-specific targets of Histomonas meleagridis antigens revealed by immunoprecipitation
Scientific Reports
Histomonas meleagridis
Immunoprecipitation
LCMS
Virulence
Histomonosis
title Host-specific targets of Histomonas meleagridis antigens revealed by immunoprecipitation
title_full Host-specific targets of Histomonas meleagridis antigens revealed by immunoprecipitation
title_fullStr Host-specific targets of Histomonas meleagridis antigens revealed by immunoprecipitation
title_full_unstemmed Host-specific targets of Histomonas meleagridis antigens revealed by immunoprecipitation
title_short Host-specific targets of Histomonas meleagridis antigens revealed by immunoprecipitation
title_sort host specific targets of histomonas meleagridis antigens revealed by immunoprecipitation
topic Histomonas meleagridis
Immunoprecipitation
LCMS
Virulence
Histomonosis
url https://doi.org/10.1038/s41598-025-88855-y
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