Category:Team Purple A 2019

Gp39.2, which is a bacteriophage T4 protein, is believed to modulate the host's (E. coli) GroEL/GroES chaperone machine, which aids in the correct folding of both host and bacteriophage proteins. Gp39.2 is thought to play a part in correctly folding the E. coli host protein UmuC, which is part of the DNA Polymerase V complex. The authors believe that the GroEL/GroES complex is required for the DNA PolV to work and proofread in the bacteria cell. This relationship between Gp39.2 and DNA PolV is illustrated in Figure 5 where an E. coli mutant (that was only a mutant for isolation purposes for plating) was plated with and without the plasmid containing Gp39.2. The bacterium were then exposed to UV irradiation and were grown with and without arabinose, which showed which mutant bacteria had Gp39.2 in them. The Gp39.2 mutant bacteria were much more frequently seen while plating as opposed to the non-Gp39.2 mutant bacteria.

Figure 1 displays the results of Indirect Flourescent Antibody assays (IFA) conducted on two B. burgdorferi strains, one containing an empty vector and the other containing a TP0435 vector. In columns A and C, the surfaces of both strains were stained while in columns B and D, the membranes of both strains were permeabilized before staining. Both vector strains were labeled more frequently than the control strains, indicating that the addition of the vector resulted in the expression of TP0435. In addition, permeabilization of the vector strain membrane resulted in significantly more staining than the nonpermeable vector strain, indicating that TP0435 was more frequently present on the periplasmic membrane surface.

In Figure 3, Immuno-SEM, specifically using immunogold labeling, was utilized to analyze the position of TP0435 (also known as gene tpp17) on the plasma membrane. There was not much gold/antibiotic tagging when the outside of the B. burgdorferi cell was labeled. In Figure 4, immunogold labeling was utilized again to show that the tpp17 structural protein is much more present in the inner, periplasmic side of the outer plasma membrane of the B. burgdorferi cell.