Overview of the Protein Molecule Paper Example

Introduction

Protein CD80 is a 45 to 60kDa type one trans-membrane glycoprotein containing two extracellular domains, a distal membrane lg that resembles a variable domain and a proximal membrane lg that resembles a constant domain. Protein CD80 comprises of cell-surface ligands that are structurally connected, twenty to forty percent of amino acid identity, and have an extracellular domain that contains tandem domains connected to flexible and continuous immune-globulin domains. The protein attaches itself to CD28 family of receptors on lymphocytes and controls the immune responses through co-inhibitory signals. The protein CD80 form homodimers at the surface of a cell forming amino-acid identity and relate with CD28. The protein CD80 has extracellular domains revealing IgV-like and IgC-like domains. The immunoglobulin domains consist of a hundred amino acids with two anti-parallel beta sheets structure whereby every sheet contains 3-4 antiparallel strands (Farre et.al, 2017).

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The association between protein CD80 with costimulatory receptors augments immune feedbacks, and the association with co-inhibitory receptors weakens immune feedbacks. The initiation of T-cells and B-cells lymphocytes is started via engaging the cell-surface, antigen-specific T-cell or B-cell receptors; however, added signals provided simultaneously through protein CD80 ligands regulate the final immune response. The protein CD80 has been featured in human beings, other mammals, mice, fish, and birds like chicken. The protein CD80 is vital in the regulation of immune responses. Protein CD80 aids in treating cancer, autoimmunity, and inflammatory illnesses.

Evolutionary History

The protein CD80 are all transmembrane featured with extracellular domains connected to the flexible and continuous domains of immune-globulins. Every IgV and IgC domains of protein CD80 family is encoded through single exons, together with extra exons that encode the leader chains which include the transmembrane and cytoplasmic domains. The protein CD80 can signal into the cell on the surface of their expression. The protein expression pattern in lymphoid cells is induced in T, B, DCs, and monocytes. The protein CD80 is part of a larger protein family because protein B7 consist of seven members of the family that include B7.1, B7.2, ICOS-L, PD-L1, PD-L.2, B7-H3, and B7-H4 (Schildberg et.al, 2018)

Role of Protein CD80

Protein CD80 helps in the development of the costimulatory molecules for immunotherapy of diseases such as cancer. Cancer is an international health problem that leads to morbidity and death in both adults and children. Currently, hospitals are using radiation and chemotherapy to treat cancer; however, these methods have their specific challenges of ineffectiveness and toxicity leading to deteriorating the cancer patient's quality of life. Nevertheless, immunotherapy is an alternative method that is effective in immunotherapy through recognition and identification of tumors. An effective immune response to the tumor is dependent on a chain of particular associations connecting a T cell and an antigen-presenting cell. However, it is unfortunate that when the interaction with the T cells occurs, there is no generation of an effective immune response as tumor cells have established several methods to fight the identification and elimination by the immune system.

Protein CD80 is involved in the costimulatory signal that is crucial in activating the T-lymphocyte. The protein is also known to play a role in the regulation of normal and malignant cells activities. Protein CD80 is down-regulated on many cancerous cells and losing CD80 is enough for the cancer-causing cells to avoid the attack of the immune system and to impart energy and apoptosis in tumor-causing T-cells. If the costimulation is not present, recognizing any antigens by the T-cells may not lead to any response, even after the expression of MCH molecules and particular tumor antigens by the T-cells. Therefore, human malignancies lacking the recognition of protein CD80 have been advised to avoid immune surveillance and thereby participate in the failure of immune identification. Transfecting the tumor cells with protein CD80 is vital in the generation of a strong immune system, which may lead to the establishment of a successful cancer vaccine. Expressing the CD80 on cancerous cells leads to the stimulation of T-cells that aids in imparting the anticancer immunity. Also, showing the CD80 on the tumor cells is vital in the enhancement of natural killer cell identification and lysis of tumors that have a critical responsibility in boosting tumor immunity.

Discussion of the experimental Findings

Horn et al. used soluble Cd8 (CD80-Fc) to test its capability to regulate the progression of PD-L1 tumors in mice. They used in the laboratory treatment of established CT26 and B16F10 tumors and reported that using soluble CD80 prolongs the development of tumor and supports the increase of T-cells into solid tumors. Moreover, Horn et al. sort to clarify the method that soluble CD80 facilitates its influences and demonstrate that it motivates later signaling of the components of the T-cell receptors and CD28 paths. The primary hypothesis of the study was that soluble CD80 acts concurrently as a rival by binding to PD-L1 to restrict signals and constumulating T-cells through CD28.

Studies have demonstrated that soluble CD 80 develops T-cell activation in the tumor sites; hence it prolongs the survival time with immunotherapy or is a relation to another immunotherapy. Horn's results established that these effects are effects occurs in the mice with considerable amounts established in the tumors (16). Horn et al. research indicated that soluble CD80 function to stimulate the tumor-reactive T-cells, hence it has a significant potential for therapeutic that facilitates antitumor immunity. Moreover, Horn et al. established that soluble CD80 functions through stimulating the CD28 and TCR indicator transduction path. Although the literature does not categorically categorize the technique that CTLA-4 suppressed T-cells, Horn et al. demonstrated that it is possible through competing for soluble CD80 while successfully preventing it from binding with PD-L1 and CD28 (16). Therefore, the solubility of CD80 primarily depends on the saturation of CTLA-4 at the site and the lymph node while high levels of solubility are necessary for costimulation through CD28 and neutralization of PD-L1. The excessive solubility of CD80 is admirable because it would be beneficial at preventing CTLA-4 mediated suppression hence decreasing the T-cell exhaustion. The study indicated that soluble CD80 therapy is efficient compared to monotherapy using a PD-L1 antibody in supporting TILs. Because PD-L1 is primarily shown through an activated T-cell, the antibody therapy might be probably efficient when a person has an already activated T-cell.

Zhao et al. investigated the expression of CD80 and CTLA-4 among adults beginning Minimal change disease (MCD). The study hypothesized that adult's onset Minimal change disease (MCD) patients reported a late response to glucocorticoid treatment. Zhao et al. used 55 patients that have a confirmed biopsy with MCD and 26 patients with idiopathic membranous nephropathy, CD80 and CTLA-4 levels in the patient's urine, serum, and renal tissue were analyzed. Serum and urinary CD80 and CTLA-4 measurements were done when patients were experiencing partial/complete remission or remission, the protein level in the urine and serum albumin were all measured on the same day (Zhao et.al, 2018).It was established that urinary CD80 was increased in MCD during the deterioration phase while the levels persistent on the lower range with a decrease of the disease. The urinary concentrations of CTLA-4 were significant amongst patients in the remission compared to relapse. Amongst the Minimal change disease (MCD) patients in decline, the urinary CD80 levels were significant while CTLA-4 was lower in steroid sensitive and steroid-resistant patients. Cytokines including the IL-6 that are formed by DC when CD80 and CD86 are activated. Moreover, Zhao et al. found that through computer analysis (in silico) that murine and human CD80/86 cytoplasmic tails comprise of possible binding themes for the various kinases. They are depicting that they might be notably phosphorylated and start a distinct signal path when activated. It has not yet been established the proximal signal molecule that activates PI3K towards the end of CD80/86 in humans.

Summary of Discussion

The hybrid profile of a Minimal change disease (MCD) marker including the CD80 with significant levels of FSGS and suPAR in the blood as well as the urine can be a probable characteristic of NPHS2 mutations that considerably contribute to the proteinuria. In summary, protein CD80 is a 45 to 60kDa type one trans-membrane glycoprotein containing two extracellular domains, a distal membrane lg that resembles a variable domain and a membrane proximal lg that resembles a constant domain. The protein CD80 has extracellular domains revealing IgV-like and IgC-like domains. The protein CD80 is part protein B7 which is a larger family, and the protein is featured in many organisms such as human beings, mice, fish, and birds like chicken. Protein CD80 aids in treating cancer, autoimmunity, and inflammatory illnesses. Protein CD80 helps in the development of the costimulatory molecules for immunotherapy of diseases such as cancer.

Works Cited

Farre, Domenec, et al. "Immunoglobulin Superfamily Members Encoded by Viruses and Their Multiple Roles in Immune Evasion." European Journal of Immunology, vol. 47, no. 5, 2017, pp. 780-796., doi:10.1002/eji.201746984.

Horn, Lucas A., et al. "Soluble CD80 Protein Delays Tumor Growth and Promotes Tumor-Infiltrating Lymphocytes." Cancer Immunology Research, vol. 6, no. 1, 2017, pp. 59-68., doi:10.1158/2326-6066.cir-17-0026.

Schildberg, Frank A., et al. "Coinhibitory Pathways in the B7-CD28 Ligand-Receptor Family." Immunity, vol. 44, no. 5, 2016, pp. 955-972., doi:10.1016/j.immuni.2016.05.002.

Zhao, Bing, et al. "CD80 And CTLA-4 as Diagnostic and Prognostic Markers in Adult-Onset Minimal Change Disease: a Retrospective Study." PeerJ, vol. 6, 2018, doi:10.7717/peerj.5400.