Disease relevance of DDX3X

• Knockdown of DDX3 using either antisense vector or dominant-negative mutants suppressed Rev-RRE-function in the export of incompletely spliced HIV-1 RNAs [1].
• A declined expression of DDX3 mRNA and protein was found in approximately 58% to 73% of hepatoma specimens, which led to the reduction of p21(waf1/cip1) expression in a manner independent of p53 status [2].
• Hepatitis C virus core protein interacts with a human DEAD box protein DDX3 [3].
• In cells infected with a recombinant vaccinia virus expressing HCV structural proteins (core, E1, and E2), DDX3 and core colocalized in distinct spots in the perinuclear region of the cytoplasm [3].
• A significant downregulation of DDX3 expression is found in HCCs from hepatitis B virus (HBV)-positive patients, but not from HCV-positive ones, compared to the corresponding nontumor tissues [4].

High impact information on DDX3X

• We show that DDX3 is a nucleo-cytoplasmic shuttling protein, which binds CRM1 and localizes to nuclear membrane pores [1].
• This dual DBX/DBY antigen is the first mHA to be identified in the context of chronic GVHD [5].
• To test this, we measured antibody responses to a well-characterized H-Y antigen, dead box RNA helicase Y (DBY), and its homolog, DBX, in 150 HSCT patients [6].
• However, translation of DBY was detected only in the male germ line, whereas DBX protein was expressed in all tissues analyzed [7].
• In testis tissue sections, DBY protein was found predominantly in spermatogonia, whereas DBX protein was expressed after meiosis in spermatids [7].

Biological context of DDX3X

• DBY has a structural homologue on the short arm of the X chromosome DBX (DDX3X) (Xp11.4) [7].
• A comparative study of DDX3X and DDX3Y was performed to determine the significance of DDX3Y for cell growth and spermatogenesis [8].
• The human DDX3Y amino acid sequence is similar to that of the X chromosome gene DDX3X (91.7% homology) [8].
• Antibody responses were directed primarily against areas of amino acid disparity between DBY and DBX [6].
• We performed a yeast two-hybrid screen of a human liver cell cDNA library with HCV core protein as bait and isolated the DEAD box protein DBX [9].

Anatomical context of DDX3X

• Human DDX3Y, the Y-encoded isoform of RNA helicase DDX3, rescues a hamster temperature-sensitive ET24 mutant cell line with a DDX3X mutation [8].
• Moreover, the T cell clone responded equally to mature HLA-DRB1*1501 male and female dendritic cells, indicating that both DBY and DBX peptides were endogenously processed [5].
• When expressed in mammalian cells, HCV core protein and DBX were co-localized at the endoplasmic reticulum [9].
• Immunofluorescent staining of HeLa cells with a polyclonal antiserum showed that DDX3 is located predominantly in nuclear speckles and at low levels throughout the cytoplasm [3].
• HLP 2 was found to act at the cell membrane, causing complete loss of membrane potential after 10 min and of membrane integrity within 30 min, with irreversible damage to the cell as shown by rapid loss of viability [10].

Associations of DDX3X with chemical compounds

• RESULTS: Allomatrix, Dynagraft, Regenafil, and poly(DL-lactide) mesh alone had less bone formation than DBX, Grafton, DBX plus mesh, and demineralized bone matrix [11].

Other interactions of DDX3X

• DDX3Y, similar to DDX3X, shuttles between the nucleus and cytoplasm in a crm1-dependent manner [8].

Analytical, diagnostic and therapeutic context of DDX3X

• Bone fill was similar between all groups with DBX paste, putty, and DFDBA control groups demonstrating 2.0 mm, 2.4 mm, and 2.2 mm, respectively [12].
• The purpose of this study was to determine the effectiveness of DBX paste and putty compared to demineralized freeze-dried bone allograft (DFDBA) in the treatment of human intraosseous periodontal defects [12].

References