Infection of human B lymphoma cells byMycoplasma fermentansinduces interaction of its elongation factor with the intracytoplasmic domain of Epstein-Barr virus receptor (gp140, EBV/C3dR, CR2, CD21)

Abstract

Human cell lines are often infected by mycoplama strains. We have demonstrated that when infected by Mycoplasma fermentans, human B lymphoma cell proliferation increased strongly. These infected B cells expressed a p45 kDa protein which interacted with the intracellular domain of CD21, the EBV/C3d receptor. p45 analysis demonstrated that this is a new gene which encodes an elongation factor originating from Mycoplasma fermentans. p45 interaction with CD21 was specific, there being no interaction with CD19. This is the first demonstration that Mycoplasma fermentans, in infecting human B cells, generates a p45 Mycoplasma component that interacts with CD21, which is involved in B cell proliferation.

A novel receptor – ligand pathway for entry of Francisella tularensis in monocyte-like THP-1 cells: interaction between surface nucleolin and bacterial elongation factor Tu

“…Once its sequence confirmed, EF-Tu was subcloned in pGEX-4T1 (Amersham Biosciences) or pET28a+ (Novagen) into Eco RI- Sal I sites, in DH5α. After transforming in E. coli strain BL21or BL21DE3, respectively, GST-fusion proteins and His-fusion proteins were produced as previously described [ 26 ] and purified either on glutathione-Sepharose 4B beads (Amersham Biosciences) or on Ni-column (Novagen), as described by manufacturers. His-fusion EF-Tu protein was used as immunogen for immunizing Balb/c mice.…”

The Diverse Functional Roles of Elongation Factor Tu (EF-Tu) in Microbial Pathogenesis

“…Sera from mice immunized with rEF-Tu also reduced M. ovipneumoniae growth (Jiang et al, 2016). In Mycoplasma fermentans , EF-Tu interacts specifically with the C-terminal 34 amino acids of CD21 in human B lymphoma cells (Balbo et al, 2005). CD21 receptors on the B cells enable the complement system to influence B-cell activation and maturation.…”

Elongation factor Tu is a multifunctional and processed moonlighting protein

“…Ef-Tu is a multifunctional protein in higher order eukaryotes 11 – 16 , parasites 17 – 20 , fungi 21 and it is has been identified on the surface of a wide range of Gram positive and Gram negative pathogenic and commensal bacteria that associate with metazoan species 2 , 22 – 29 . Bacterial Ef-Tu interacts with nucleolin 30 , 31 , fibrinogen and factor H 23 , 26 , plasminogen and several complement factors 26 , 27 , 32 , laminin 33 , CD21 34 , fibronectin 2 , 33 , 35 , 36 , is immunogenic 37 and adheres to the surface of Hep-2 cells 33 underscoring the multifunctional adhesive characteristics that have been assigned to this molecule. Ef-Tu binds sulfated carbohydrate moieties found on glycolipids and sulfomucin and promotes the binding of Lactobacillus reuteri to mucosal surfaces indicating that Ef-Tu can interact with carbohydrates 38 .…”