Products

Theileria orientalis cDNA and recombinant antigen

Cat#

Products (Recombinant protein)

Swiss Prot#

Size

Price (US$)

Order

PL0763

Recombinant protein-Theileria orientalis Piroplasm major immunodominant protein (a.a.19 to 283)

O15928

100 µg

1195

Order

RPL0763

cDNA-Theileria orientalis Piroplasm major immunodominant protein (a.a.19 to 283)

O15928

2 µg

1584

Order

 

Theileria orientalis cDNA and recombinant antigen

  • Codon-optimized cDNA is cloned into E. coli expression vector with 6x His-tag at N-terminus and ready-to-use for recombinant protein production.
  • Recombinant protein applications: Western Blot may be used for other applications determined by the user.
  • Protein Purity: >90%, as determined by SDS-PAGE under reducing conditions.
  • Protein Activity: N/A
  • Protein Tag:  Contains A 6x histidine tag at N-terminus.
  • Protein Formulation: Liquid
  • Source: Produced from E. coli

Theileria orientalis is a protozoan parasite that infects cattle, buffalo, and other ruminants, causing bovine theileriosis, also known as oriental theileriosis. This disease is widespread in many parts of the world, including Australia, Asia, and Africa, and causes significant economic losses to the livestock industry due to reduced milk production, weight loss, and mortality in infected animals.

Several surface proteins have been identified in T. orientalis, with the piroplasm major immunodominant protein (PMIP) being one of the most promising candidates for the development of diagnostic tests and vaccines. In this article, we will discuss the role of PMIP in controlling the spread of bovine theileriosis and its potential as a target for vaccine development.

The Piroplasm Major Immunodominant Protein:

PMIP is a surface protein of T. orientalis that is highly immunogenic, meaning it elicits a strong immune response in infected animals. This protein is a major target for the host’s immune system and is recognized by antibodies produced during the infection. Therefore, PMIP is a promising candidate for the development of diagnostic tests to detect T. orientalis infections in cattle and other ruminants.

PMIP is a large protein with a molecular weight of approximately 60 kDa, and it is conserved among different T. orientalis isolates. The protein has been shown to bind to red blood cells and invade host cells, indicating its importance in the parasite’s lifecycle. Furthermore, PMIP is expressed on the surface of the merozoites, which are the infective form of the parasite that enter the host’s bloodstream and invade red blood cells.

Potential as a Target for Vaccine Development:

The high immunogenicity and conservation of PMIP make it an ideal target for vaccine development against bovine theileriosis. Several studies have investigated the potential of PMIP as a vaccine candidate and have shown promising results.

One study in Japan demonstrated that vaccination with a recombinant form of PMIP provided protection against T. orientalis infection in cattle. The vaccinated animals had lower levels of parasitemia, and clinical symptoms compared to the unvaccinated controls. Another study in China also showed that vaccination with a PMIP-derived peptide provided protection against T. orientalis infection in sheep.

The potential of PMIP as a target for vaccine development has also been supported by the identification of PMIP-specific CD4+ T cells in T. orientalis-infected cattle. These T cells are responsible for activating the immune response and producing antibodies against the parasite. Therefore, targeting PMIP with a vaccine could stimulate the production of these T cells and enhance the host’s immune response to T. orientalis.


Theileria orientalis cDNA and recombinant antigens can be used for the diagnosis, treatment, and prevention of Theileria orientalis infection. cDNA can be used to identify and characterize the genes of the parasite, while recombinant antigens can be used to develop and improve diagnostic tests. Additionally, these antigens can be used to develop vaccines for the prevention of infection, as well as to evaluate the efficacy of treatment.

The use of recombinant proteins/cDNA in academic research and therapeutic applications has skyrocketed. However, in heterologous expression systems, successful recombinant protein expression is dependent on a variety of factors, including codon preference, RNA secondary structure, and GC content. When compared to pre-optimization, more and more experimental results demonstrated that the expression level was dramatically increased, ranging from two to hundred times depending on the gene. Bioclone has created a proprietary technology platform that has resulted in the creation of over 6,000 artificially synthesized codon-optimized cDNA clones (cloned in E. coli expression Vector), which are ready for production of the recombinant proteins.

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