Using Proteomic Approaches to Unravel the Response of Ctenocephalides felis felis to Blood Feeding and Infection With Bartonella henselae

Detalhes bibliográficos
Autor(a) principal: André, Marcos Rogério [UNESP]
Data de Publicação: 2022
Outros Autores: Neupane, Pradeep, Lappin, Michael, Herrin, Brian, Smith, Vicki, Williams, Taufika Islam, Collins, Leonard, Bai, Hongxia, Jorge, Gabriel Lemes [UNESP], Balbuena, Tiago Santana [UNESP], Bradley, Julie, Maggi, Ricardo G., Breitschwerdt, Edward B.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da UNESP
Texto Completo: http://dx.doi.org/10.3389/fcimb.2022.828082
http://hdl.handle.net/11449/230383
Resumo: Among the Ctenocephalides felis felis-borne pathogens, Bartonella henselae, the main aetiological agent of cat scratch disease (CSD), is of increasing comparative biomedical importance. Despite the importance of B. henselae as an emergent pathogen, prevention of the diseases caused by this agent in cats, dogs and humans mostly relies on the use of ectoparasiticides. A vaccine targeting both flea fitness and pathogen competence is an attractive choice requiring the identification of flea proteins/metabolites with a dual effect. Even though recent developments in vector and pathogen -omics have advanced the understanding of the genetic factors and molecular pathways involved at the tick-pathogen interface, leading to discovery of candidate protective antigens, only a few studies have focused on the interaction between fleas and flea-borne pathogens. Taking into account the period of time needed for B. henselae replication in flea digestive tract, the present study investigated flea-differentially abundant proteins (FDAP) in unfed fleas, fleas fed on uninfected cats, and fleas fed on B. henselae-infected cats at 24 hours and 9 days after the beginning of blood feeding. Proteomics approaches were designed and implemented to interrogate differentially expressed proteins, so as to gain a better understanding of proteomic changes associated with the initial B. henselae transmission period (24 hour timepoint) and a subsequent time point 9 days after blood ingestion and flea infection. As a result, serine proteases, ribosomal proteins, proteasome subunit α-type, juvenile hormone epoxide hydrolase 1, vitellogenin C, allantoinase, phosphoenolpyruvate carboxykinase, succinic semialdehyde dehydrogenase, glycinamide ribotide transformylase, secreted salivary acid phosphatase had high abundance in response of C. felis blood feeding and/or infection by B. henselae. In contrast, high abundance of serpin-1, arginine kinase, ribosomal proteins, peritrophin-like protein, and FS-H/FSI antigen family member 3 was strongly associated with unfed cat fleas. Findings from this study provide insights into proteomic response of cat fleas to B. henselae infected and uninfected blood meal, as well as C. felis response to invading B. henselae over an infection time course, thus helping understand the complex interactions between cat fleas and B. henselae at protein levels.
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spelling Using Proteomic Approaches to Unravel the Response of Ctenocephalides felis felis to Blood Feeding and Infection With Bartonella henselaebartonellosiscat fleacat scratch diseaseflea-pathogen interfaceproteomeAmong the Ctenocephalides felis felis-borne pathogens, Bartonella henselae, the main aetiological agent of cat scratch disease (CSD), is of increasing comparative biomedical importance. Despite the importance of B. henselae as an emergent pathogen, prevention of the diseases caused by this agent in cats, dogs and humans mostly relies on the use of ectoparasiticides. A vaccine targeting both flea fitness and pathogen competence is an attractive choice requiring the identification of flea proteins/metabolites with a dual effect. Even though recent developments in vector and pathogen -omics have advanced the understanding of the genetic factors and molecular pathways involved at the tick-pathogen interface, leading to discovery of candidate protective antigens, only a few studies have focused on the interaction between fleas and flea-borne pathogens. Taking into account the period of time needed for B. henselae replication in flea digestive tract, the present study investigated flea-differentially abundant proteins (FDAP) in unfed fleas, fleas fed on uninfected cats, and fleas fed on B. henselae-infected cats at 24 hours and 9 days after the beginning of blood feeding. Proteomics approaches were designed and implemented to interrogate differentially expressed proteins, so as to gain a better understanding of proteomic changes associated with the initial B. henselae transmission period (24 hour timepoint) and a subsequent time point 9 days after blood ingestion and flea infection. As a result, serine proteases, ribosomal proteins, proteasome subunit α-type, juvenile hormone epoxide hydrolase 1, vitellogenin C, allantoinase, phosphoenolpyruvate carboxykinase, succinic semialdehyde dehydrogenase, glycinamide ribotide transformylase, secreted salivary acid phosphatase had high abundance in response of C. felis blood feeding and/or infection by B. henselae. In contrast, high abundance of serpin-1, arginine kinase, ribosomal proteins, peritrophin-like protein, and FS-H/FSI antigen family member 3 was strongly associated with unfed cat fleas. Findings from this study provide insights into proteomic response of cat fleas to B. henselae infected and uninfected blood meal, as well as C. felis response to invading B. henselae over an infection time course, thus helping understand the complex interactions between cat fleas and B. henselae at protein levels.Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)Laboratory of Immunoparasitology Department of Pathology Reproduction and One Health Faculdade de Ciências Agrárias e Veterinárias Universidade Estadual Paulista FCAV/UNESPIntracellular Pathogens Research Laboratory Department of Clinical Sciences The Comparative Medicine Institute College of Veterinary Medicine North Carolina State UniversityDepartment of Clinical Sciences Center for Companion Animal Studies Colorado State UniversityDepartment of Diagnostic Medicine/Pathobiology College of Veterinary Medicine Kansas State UniversityDepartment of Chemistry North Carolina State UniversityMolecular Education Technology and Research Innovation Center (METRIC) North Carolina State UniversityDepartmento de Biotecnologia Agropecuária e Ambiental Faculdade de Ciências Agrárias e Veterinárias Universidade Estadual Paulista FCAV/UNESPLaboratory of Immunoparasitology Department of Pathology Reproduction and One Health Faculdade de Ciências Agrárias e Veterinárias Universidade Estadual Paulista FCAV/UNESPDepartmento de Biotecnologia Agropecuária e Ambiental Faculdade de Ciências Agrárias e Veterinárias Universidade Estadual Paulista FCAV/UNESPUniversidade Estadual Paulista (UNESP)North Carolina State UniversityColorado State UniversityKansas State UniversityAndré, Marcos Rogério [UNESP]Neupane, PradeepLappin, MichaelHerrin, BrianSmith, VickiWilliams, Taufika IslamCollins, LeonardBai, HongxiaJorge, Gabriel Lemes [UNESP]Balbuena, Tiago Santana [UNESP]Bradley, JulieMaggi, Ricardo G.Breitschwerdt, Edward B.2022-04-29T08:39:33Z2022-04-29T08:39:33Z2022-01-28info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articlehttp://dx.doi.org/10.3389/fcimb.2022.828082Frontiers in Cellular and Infection Microbiology, v. 12.2235-2988http://hdl.handle.net/11449/23038310.3389/fcimb.2022.8280822-s2.0-85124573002Scopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengFrontiers in Cellular and Infection Microbiologyinfo:eu-repo/semantics/openAccess2022-04-29T08:39:33Zoai:repositorio.unesp.br:11449/230383Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462022-04-29T08:39:33Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false
dc.title.none.fl_str_mv Using Proteomic Approaches to Unravel the Response of Ctenocephalides felis felis to Blood Feeding and Infection With Bartonella henselae
title Using Proteomic Approaches to Unravel the Response of Ctenocephalides felis felis to Blood Feeding and Infection With Bartonella henselae
spellingShingle Using Proteomic Approaches to Unravel the Response of Ctenocephalides felis felis to Blood Feeding and Infection With Bartonella henselae
André, Marcos Rogério [UNESP]
bartonellosis
cat flea
cat scratch disease
flea-pathogen interface
proteome
title_short Using Proteomic Approaches to Unravel the Response of Ctenocephalides felis felis to Blood Feeding and Infection With Bartonella henselae
title_full Using Proteomic Approaches to Unravel the Response of Ctenocephalides felis felis to Blood Feeding and Infection With Bartonella henselae
title_fullStr Using Proteomic Approaches to Unravel the Response of Ctenocephalides felis felis to Blood Feeding and Infection With Bartonella henselae
title_full_unstemmed Using Proteomic Approaches to Unravel the Response of Ctenocephalides felis felis to Blood Feeding and Infection With Bartonella henselae
title_sort Using Proteomic Approaches to Unravel the Response of Ctenocephalides felis felis to Blood Feeding and Infection With Bartonella henselae
author André, Marcos Rogério [UNESP]
author_facet André, Marcos Rogério [UNESP]
Neupane, Pradeep
Lappin, Michael
Herrin, Brian
Smith, Vicki
Williams, Taufika Islam
Collins, Leonard
Bai, Hongxia
Jorge, Gabriel Lemes [UNESP]
Balbuena, Tiago Santana [UNESP]
Bradley, Julie
Maggi, Ricardo G.
Breitschwerdt, Edward B.
author_role author
author2 Neupane, Pradeep
Lappin, Michael
Herrin, Brian
Smith, Vicki
Williams, Taufika Islam
Collins, Leonard
Bai, Hongxia
Jorge, Gabriel Lemes [UNESP]
Balbuena, Tiago Santana [UNESP]
Bradley, Julie
Maggi, Ricardo G.
Breitschwerdt, Edward B.
author2_role author
author
author
author
author
author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv Universidade Estadual Paulista (UNESP)
North Carolina State University
Colorado State University
Kansas State University
dc.contributor.author.fl_str_mv André, Marcos Rogério [UNESP]
Neupane, Pradeep
Lappin, Michael
Herrin, Brian
Smith, Vicki
Williams, Taufika Islam
Collins, Leonard
Bai, Hongxia
Jorge, Gabriel Lemes [UNESP]
Balbuena, Tiago Santana [UNESP]
Bradley, Julie
Maggi, Ricardo G.
Breitschwerdt, Edward B.
dc.subject.por.fl_str_mv bartonellosis
cat flea
cat scratch disease
flea-pathogen interface
proteome
topic bartonellosis
cat flea
cat scratch disease
flea-pathogen interface
proteome
description Among the Ctenocephalides felis felis-borne pathogens, Bartonella henselae, the main aetiological agent of cat scratch disease (CSD), is of increasing comparative biomedical importance. Despite the importance of B. henselae as an emergent pathogen, prevention of the diseases caused by this agent in cats, dogs and humans mostly relies on the use of ectoparasiticides. A vaccine targeting both flea fitness and pathogen competence is an attractive choice requiring the identification of flea proteins/metabolites with a dual effect. Even though recent developments in vector and pathogen -omics have advanced the understanding of the genetic factors and molecular pathways involved at the tick-pathogen interface, leading to discovery of candidate protective antigens, only a few studies have focused on the interaction between fleas and flea-borne pathogens. Taking into account the period of time needed for B. henselae replication in flea digestive tract, the present study investigated flea-differentially abundant proteins (FDAP) in unfed fleas, fleas fed on uninfected cats, and fleas fed on B. henselae-infected cats at 24 hours and 9 days after the beginning of blood feeding. Proteomics approaches were designed and implemented to interrogate differentially expressed proteins, so as to gain a better understanding of proteomic changes associated with the initial B. henselae transmission period (24 hour timepoint) and a subsequent time point 9 days after blood ingestion and flea infection. As a result, serine proteases, ribosomal proteins, proteasome subunit α-type, juvenile hormone epoxide hydrolase 1, vitellogenin C, allantoinase, phosphoenolpyruvate carboxykinase, succinic semialdehyde dehydrogenase, glycinamide ribotide transformylase, secreted salivary acid phosphatase had high abundance in response of C. felis blood feeding and/or infection by B. henselae. In contrast, high abundance of serpin-1, arginine kinase, ribosomal proteins, peritrophin-like protein, and FS-H/FSI antigen family member 3 was strongly associated with unfed cat fleas. Findings from this study provide insights into proteomic response of cat fleas to B. henselae infected and uninfected blood meal, as well as C. felis response to invading B. henselae over an infection time course, thus helping understand the complex interactions between cat fleas and B. henselae at protein levels.
publishDate 2022
dc.date.none.fl_str_mv 2022-04-29T08:39:33Z
2022-04-29T08:39:33Z
2022-01-28
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://dx.doi.org/10.3389/fcimb.2022.828082
Frontiers in Cellular and Infection Microbiology, v. 12.
2235-2988
http://hdl.handle.net/11449/230383
10.3389/fcimb.2022.828082
2-s2.0-85124573002
url http://dx.doi.org/10.3389/fcimb.2022.828082
http://hdl.handle.net/11449/230383
identifier_str_mv Frontiers in Cellular and Infection Microbiology, v. 12.
2235-2988
10.3389/fcimb.2022.828082
2-s2.0-85124573002
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Frontiers in Cellular and Infection Microbiology
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.source.none.fl_str_mv Scopus
reponame:Repositório Institucional da UNESP
instname:Universidade Estadual Paulista (UNESP)
instacron:UNESP
instname_str Universidade Estadual Paulista (UNESP)
instacron_str UNESP
institution UNESP
reponame_str Repositório Institucional da UNESP
collection Repositório Institucional da UNESP
repository.name.fl_str_mv Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)
repository.mail.fl_str_mv
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