Schistosoma mansoni, also known as the blood Fluke, is a parasitic worm that infects humans and causes schistosomiasis, a debilitating disease. The disease is prevalent in sub-Saharan Africa, South America, and the Caribbean, affecting millions of people worldwide. The life cycle of Schistosoma mansoni involves two hosts: the intermediate snail host and the definitive human host. When the parasite enters the human host, it releases various antigens that help it to evade the host’s immune system and establish infection.

We will explore the various antigens of Schistosoma mansoni, including Sm28GST, Sm29, Venom allergen-like proteins, and more, and their role in parasitic infections. We will also take a closer look at the surface proteins and glycoproteins of the blood Fluke, including the infested erythrocyte surface antigen and eggshell protein.

Antigens of Schistosoma mansoni:

Sm28GST is a protective 28 kDa antigen of Schistosoma mansoni that has been shown to induce a strong immune response in infected individuals. This antigen is an attractive candidate for developing a vaccine against schistosomiasis, as it can stimulate both humoral and cellular immune responses.

Sm29 is another antigen of Schistosoma mansoni that is localized in the outer tegumental layer of the parasite. This antigen has been shown to induce a protective immune response in animal models and may be a promising target for vaccine development.

Schistosoma mansoni also produces several venom allergen-like proteins, including SmVAL15, which is involved in the modulation of host immune responses. These proteins may contribute to the parasite’s ability to evade the host’s immune system and establish infection.

Surface proteins and glycoproteins:

PspC: Surface protein PspC is a glycoprotein of Schistosoma mansoni that is involved in the attachment of the parasite to the host’s vascular endothelium. This protein may play a role in the establishment of the parasite’s infection.

Gp18-22 Sm: Gp18-22 Sm is another glycoprotein of Schistosoma mansoni that is localized in the tegument of the parasite. This protein has been shown to induce a protective immune response in animal models and may be a promising target for vaccine development.

Infested erythrocyte surface antigen:

The infested erythrocyte surface antigen is a surface protein of Schistosoma mansoni that is exposed on the surface of the parasite’s host erythrocyte. This antigen may play a role in the modulation of the host’s immune response to the parasite.

Eggshell protein: The eggshell protein of Schistosoma mansoni is a 200-kDa GPI-anchored surface glycoprotein that is essential for eggshell formation. This protein may also play a role in the modulation of the host’s immune response to the parasite.

The cDNA (complementary DNA) of Schistosoma mansoni can be used to study the parasite’s molecular biology and genetics. Researchers can isolate and sequence the cDNA to identify genes that are important for the parasite’s survival and pathogenesis. This information can be used to develop new strategies for controlling the spread of intestinal schistosomiasis and other schistosomiasis diseases caused by Schistosoma species.

Recombinant antigens, which are proteins that are produced in the laboratory using genetic engineering techniques, can be used for diagnostic tests and vaccine development for Schistosoma mansoni. Researchers can identify antigens from Schistosoma mansoni and produce them using recombinant DNA technology. These recombinant antigens can be used to develop diagnostic tests for the detection of antibodies against Schistosoma mansoni in human serum or stool samples, which can help in early diagnosis and treatment of intestinal schistosomiasis.

Recombinant antigens can also be used to develop vaccines for intestinal schistosomiasis. Vaccines containing recombinant Schistosoma mansoni antigens can be used to stimulate an immune response in humans, which can help protect them against the infection or reduce the severity of the disease if they do get infected.

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.