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CD55

Official Full Name
CD55 molecule (Cromer blood group)
Organism
Homo sapiens
GeneID
1604
Background
This gene encodes a glycoprotein involved in the regulation of the complement cascade. Binding of the encoded protein to complement proteins accelerates their decay, thereby disrupting the cascade and preventing damage to host cells. Antigens present on this protein constitute the Cromer blood group system (CROM). Alternative splicing results in multiple transcript variants. The predominant transcript variant encodes a membrane-bound protein, but alternatively spliced transcripts may produce soluble proteins. [provided by RefSeq, Jul 2014]
Synonyms
CR; TC; DAF; CROM; CHAPLE;
Protein Sequence
MTVARPSVPAALPLLGELPRLLLLVLLCLPAVWGDCGLPPDVPNAQPALEGRTSFPEDTVITYKCEESFVKIPGEKDSVICLKGSQWSDIEEFCNRSCEVPTRLNSASLKQPYITQNYFPVGTVVEYECRPGYRREPSLSPKLTCLQNLKWSTAVEFCKKKSCPNPGEIRNGQIDVPGGILFGATISFSCNTGYKLFGSTSSFCLISGSSVQWSDPLPECREIYCPAPPQIDNGIIQGERDHYGYRQSVTYACNKGFTMIGEHSIYCTVNNDEGEWSGPPPECRGKSLTSKVPPTVQKPTTVNVPTTEVSPTSQKTTTKTTTPNAQATRSTPVSRTTKHFHETTPNKGSGTTSGTTRLLSGHTCFTLTGLLGTLVTMGLLT
Open
Disease
Bladder cancer, Brain cancer, Colorectal cancer, Lung cancer, Melanoma, Prostate cancer, Stomach cancer
Approved Drug
0
Clinical Trial Drug
3 +
Discontinued Drug
0

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Detailed Information

The CD55 gene encodes a glycoprotein that plays a crucial role in the regulation of the complement system, a critical component of the innate immune response. By controlling the complement cascade, this protein—also known as decay-accelerating factor (DAF)—helps host cells withstand the possibly negative consequences of too much complement activation. CD55 does this by attaching to complement proteins, hastening their breakdown and thus reducing the creation of membrane assault complexes potentially damaging the host cells. Apart from its complement-regulatory roles, CD55 is involved in other cellular activities including immunological regulation and viral infection. This review seeks to investigate in health and sickness the structure, function, and clinical consequences of the CD55 gene.

Gene Structure and Protein Characteristics

Found on chromosome 1q32, the CD55 gene spans a region coding many complement-regulating proteins. Comprising eleven exons, it covers a 40 kb segment. Glycosylphosphatidylinositol (GPI)-anchored membrane protein makes up the protein output of the CD55 gene. Tethering the protein to the cell membrane is accomplished in part by the GPI-anchor at its C-terminal end. Along with many short consensus repeat domains mediating interactions with complement proteins C3b and C4b, the protein has a serine/threonine/proline-rich region. Although the computed molecular weight of CD55 is around 43 kDa, depending on the type of cell and the existence of alternative splicing or glycosylation patterns, the mature protein shows a varied molecular weight (50–100 kDa).

Figure 1 illustrates the structure and roles of CD55 in both complement-mediated pathways and its non-complement signaling functions in cancer, including activation of oncogenic pathways and resistance to chemotherapy.Figure. 1. Canonical and non-canonical function of CD55. (Bharti R, et al., 2022)

Function of CD55 in Complement Regulation

CD55 mostly serves to control the complement system, a crucial immunological defense mechanism. Proteins make up the complement system; upon activation, they may form the membrane attack complex (MAC), therefore lysing target cells. By speeding up C3 convertase degradation, the main enzyme in the complement cascade, CD55 reduces complement activation. CD55 specifically binds to C3b and C4b fragments, therefore blocking their interaction with other complement components required for the synthesis of the C3 and C5 convertases. Through destabilizing these convertases, CD55 protects host cells from complement-mediated harm.

Apart from controlling complement activation, CD55 also dissociates Bb from the C3b fragment therefore interfering with the creation of the C3bBb convertace. Protection of host cells from complement-induced lysis is especially crucial as otherwise tissue damage or autoimmune reactions might follow.

CD55 and Viral Infections

CD55 has also been identified as a receptor for several viruses, including enteroviruses and Coxsackieviruses. These viruses exploit CD55 as a means of attaching to host cells, facilitating the entry and subsequent infection. The function of CD55 in viral infections implies that it might be related to viral pathogenesis and that changing CD55 expression could provide possible therapeutic paths in the treatment of viral disorders.

Furthermore under investigation in gene therapy as a way of offering resistance to complement-mediated immune responses are CD55-modified viral vectors With CD55 added to viral envelopes, scientists expect to improve the effectiveness of gene therapy by stopping early immune clearance of the viral vector.

Immune Regulation: CD55 and T Cells

CD55 also modulates immune cell functions through its interactions with T cells and other immune cells. It has been shown to reduce T-cell responses, slow down natural killer (NK) cell activity, and control B-cell proliferation. CD55 binds to CD97, a receptor expressed on immune cells including monocytes, granulocytes, and lymphocytes, thereby accomplishing this. CD55 and CD97 interact to affect several immunological responses, including control of inflammation and T cell activation regulation.

This immune-modulating ability emphasizes the need for CD55 in preserving immunological homeostasis. It also implies, nevertheless, that CD55 could be implicated in the immune evasion strategies used by cancer cells and infections.

CD55 and Cancer

CD55 has been implicated in various types of cancer, where it is often overexpressed. By blocking complement-dependent cytotoxicity, this overexpression helps cancer cells escape immune monitoring. Furthermore shielding tumor cells from natural killer (NK) cell-mediated death is CD55. Many studies have linked poor prognosis in malignancies including colorectal cancer, breast cancer, lung cancer, and ovarian cancer to increased CD55 expression. Within the framework of cancer, CD55's complement regulating function is hypothesized to support tumor development. Reducing complement activation helps CD55 stop the immune system from attacking tumor cells. Furthermore, using its interaction with CD97, a receptor encouraging cell migration and invasion, CD55 has been found to help tumor cell migration and metastases.

With these purposes, CD55 has attracted attention as a potential target for cancer treatments. Monoclonal antibodies and immune checkpoint inhibitors have shown promise in improving the efficacy of cancer therapies by means of strategies meant to limit CD55 expression or inhibition of its function.

CD55 and Malaria

Apart from its function in immunological control and cancer, CD55 is a receptor for the malaria parasite Plasmodium falciparum. Erythrocytes devoid of CD55 have been demonstrated to be resistant to malaria as the parasite cannot effectively attach to the surface of the host cell. This result has prompted the hypothesis that CD55 could be a target for malaria treatments. Red blood cell inhibition of CD55, however, may have unexpected effects including increased vulnerability to anemia resulting from complement-mediated destruction of erythrocytes.

CD55 and Other Diseases

CD55 has also been associated with several other diseases, including protein-losing enteropathy, paroxysmal nocturnal hemoglobinuria (PNH), multiple sclerosis (MS), and rheumatoid arthritis (RA). In PNH, a disorder marked by complement-mediated death of red blood cells, CD55 loss adds to the disease's pathogenesis. Analogous autoimmune diseases such as MS and RA, where complement activation causes tissue damage and inflammation, have also been linked to CD55 malfunction.

References:

  1. Dho SH, Lim JC, Kim LK. Beyond the Role of CD55 as a Complement Component. Immune Netw. 2018;18(1):e11.
  2. Bharti R, Dey G, Lin F, et al. CD55 in cancer: Complementing functions in a non-canonical manner. Cancer Lett. 2022;551:215935.
  3. Lea S. Interactions of CD55 with non-complement ligands. Biochem Soc Trans. 2002;30(Pt 6):1014-1019.
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