ArticlePloS one2013
Functional insights into recombinant TROSPA protein from Ixodes ricinus.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 18 citations in OpenAlex.
- Rickettsial Diseases and Vaccines: Is There an Opportunity for Plant-Made Vaccine Technology?Biotechnology and bioengineering · 2026Review
- Overview of Recombinant Tick Vaccines and Perspectives on the Use of Plant-Made Vaccines to Control Ticks of Veterinary Importance.Vaccines · 2024Review
- Similarities betweenCurrent research in parasitology & vector-borne diseases · 2024Article
- Interactions Between Ticks and Lyme Disease Spirochetes.Current issues in molecular biology · 2021Article
- Article
- Molecular Detection and Characterization ofPathogens (Basel, Switzerland) · 2019Article
- The genetic diversity of Borrelia afzelii is not maintained by the diversity of the rodent hosts.Parasites & vectors · 2018Article
- Tick receptor for outer surface protein A from Ixodes ricinus - the first intrinsically disordered protein involved in vector-microbe recognition.Scientific reports · 2016Article
- Transmission-Blocking Vaccines: Focus on Anti-Vector Vaccines against Tick-Borne Diseases.Archivum immunologiae et therapiae experimentalis · 2015Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lyme disease (also called borreliosis) is a prevalent chronic disease transmitted by ticks and caused by Borrelia burgdorferi s. l. spirochete. At least one tick protein, namely TROSPA from I. scapularis, commonly occurring in the USA, was shown to be required for colonization of the vector by bacteria. Located in the tick gut, TROSPA interacts with the spirochete outer surface protein A (OspA) and initiates the tick colonization. Ixodes ricinus is a primary vector involved in B. burgdorferi s. l. transmission in most European countries. In this study, we characterized the capacities of recombinant TROSPA protein from I. ricinus to interact with OspA from different Borrelia species and to induce an immune response in animals. We also showed that the N-terminal part of TROSPA (a putative transmembrane domain) is not involved in the interaction with OspA and that reduction of the total negative charge on the TROSPA protein impaired TROSPA-OspA binding. In general, the data presented in this paper indicate that recombinant TROSPA protein retains the capacity to form a complex with OspA and induces a significant level of IgG in orally immunized rats. Thus, I. ricinus TROSPA may be considered a good candidate component for an animal vaccine against Borrelia.
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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.