Anaplasma phagocytophilum MSP4 and HSP70 Proteins Are Involved in Interactions with Host Cells during Pathogen Infection
Jazyk angličtina Země Švýcarsko Médium electronic-ecollection
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
28725639
PubMed Central
PMC5496961
DOI
10.3389/fcimb.2017.00307
Knihovny.cz E-zdroje
- Klíčová slova
- Anaplasma phagocytophilum, HL60, anaplasmosis, immunology, sheep, tick, vaccine,
- MeSH
- Anaplasma phagocytophilum genetika metabolismus MeSH
- bakteriální proteiny genetika metabolismus MeSH
- ehrlichióza mikrobiologie veterinární MeSH
- interakce hostitele a patogenu MeSH
- membránové proteiny genetika metabolismus MeSH
- nemoci ovcí mikrobiologie MeSH
- ovce MeSH
- proteiny tepelného šoku HSP70 genetika metabolismus MeSH
- zvířata MeSH
- Check Tag
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- bakteriální proteiny MeSH
- membránové proteiny MeSH
- proteiny tepelného šoku HSP70 MeSH
Anaplasma phagocytophilum transmembrane and surface proteins play a role during infection and multiplication in host neutrophils and tick vector cells. Recently, A. phagocytophilum Major surface protein 4 (MSP4) and Heat shock protein 70 (HSP70) were shown to be localized on the bacterial membrane, with a possible role during pathogen infection in ticks. In this study, we hypothesized that A. phagocytophilum MSP4 and HSP70 have similar functions in tick-pathogen and host-pathogen interactions. To address this hypothesis, herein we characterized the role of these bacterial proteins in interaction and infection of vertebrate host cells. The results showed that A. phagocytophilum MSP4 and HSP70 are involved in host-pathogen interactions, with a role for HSP70 during pathogen infection. The analysis of the potential protective capacity of MSP4 and MSP4-HSP70 antigens in immunized sheep showed that MSP4-HSP70 was only partially protective against pathogen infection. This limited protection may be associated with several factors, including the recognition of non-protective epitopes by IgG in immunized lambs. Nevertheless, these antigens may be combined with other candidate protective antigens for the development of vaccines for the control of human and animal granulocytic anaplasmosis. Focusing on the characterization of host protective immune mechanisms and protein-protein interactions at the host-pathogen interface may lead to the discovery and design of new effective protective antigens.
Biology Centre Czech Academy of Sciences Institute of ParasitologyČeské Budějovice Czechia
Departamento de Sanidad Animal Instituto Vasco de Investigación y Desarrollo Agrario Derio Spain
Department of Virology Veterinary Research InstituteBrno Czechia
Faculty of Science University of South BohemiaČeské Budějovice Czechia
UMR BIPAR Animal Health Laboratory INRA ANSES ENVAMaisons Alfort France
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A bite so sweet: the glycobiology interface of tick-host-pathogen interactions