CD46 Antibody - #DF6531

Acts as a cofactor for complement factor I, a serine protease which protects autologous cells against complement-mediated injury by cleaving C3b and C4b deposited on host tissue. May be involved in the fusion of the spermatozoa with the oocyte during fertilization. Also acts as a costimulatory factor for T-cells which induces the differentiation of CD4+ into T-regulatory 1 cells. T-regulatory 1 cells suppress immune responses by secreting interleukin-10, and therefore are thought to prevent autoimmunity.

(Microbial infection) A number of viral and bacterial pathogens seem to bind MCP in order to exploit its immune regulation property and directly induce an immunosuppressive phenotype in T-cells.

(Microbial infection) Acts as a receptor for Adenovirus subgroup B2 and Ad3.

(Microbial infection) Acts as a receptor for cultured Measles virus.

(Microbial infection) Acts as a receptor for Herpesvirus 6/HHV-6.

(Microbial infection) May act as a receptor for pathogenic bacteria Neisseria and Streptococcus pyogenes.

N-glycosylated on Asn-83; Asn-114 and Asn-273 in most tissues, but probably less N-glycosylated in testis. N-glycosylation on Asn-114 and Asn-273 is required for cytoprotective function. N-glycosylation on Asn-114 is required for Measles virus binding. N-glycosylation on Asn-273 is required for Neisseria binding. N-glycosylation is not required for human adenovirus binding.

Extensively O-glycosylated in the Ser/Thr-rich domain. O-glycosylation is required for Neisseria binding but not for Measles virus or human adenovirus binding.

In epithelial cells, isoforms B/D/F/H/J/L/3 are phosphorylated by YES1 in response to infection by Neisseria gonorrhoeae; which promotes infectivity. In T-cells, these isoforms may be phosphorylated by LCK.

Cytoplasmic vesicle>Secretory vesicle>Acrosome inner membrane>Single-pass type I membrane protein.
Note: Inner acrosomal membrane of spermatozoa. Internalized upon binding of Measles virus, Herpesvirus 6 or Neisseria gonorrhoeae, which results in an increased susceptibility of infected cells to complement-mediated injury. In cancer cells or cells infected by Neisseria, shedding leads to a soluble peptide.

Expressed by all cells except erythrocytes.

Interacts with C3b. Interacts with C4b. Interacts with moesin/MSN.

(Microbial infection) Interacts with measles virus H protein.

(Microbial infection) Interacts with human herpesvirus 6 GH protein.

(Microbial infection) Interacts with human adenovirus B/D fiber protein.

(Microbial infection) Binds to Streptococcus pyogenes M protein and to type IV pili from Neisseria.

Sushi domains 1 and 2 are required for interaction with human adenovirus B PIV/FIBER protein and with Measles virus H protein. Sushi domains 2 and 3 are required for Herpesvirus 6 binding. Sushi domain 3 is required for Neisseria binding. Sushi domains 3 and 4 are required for interaction with Streptococcus pyogenes M protein and are the most important for interaction with C3b and C4b.