Category:Team Green B 2018

The protein Lmo1656 is a virulence factor secreted by Listeria Monocytogenes. In figure 3 C -D orally innoculated mice infected with the mutant version delta lmo1656 were found to have lower bacterial burden 48 hours post infection. The proposed mechanism is through lm protein docking at E-CAD surface protein. They have also done the same test intravenously and it shows no decrease in virulence suggesting that this protein specifically helps the bacteria when infecting through the oral route.

During early infection, Chorella evoke an increase in [K+]. The mechanism for this efflux was hypothesized to be Kcv proteins.As the author used a Kcv blockers like Ba2+ and Cs+ and the usage of them resulted in decrease in potassium efflux (Fig. 5). The Ba2+ inhibition of virus-triggered K+ efflux is also reflected in a reduced release of K+ from the cells (Fig. 5B). Thus Kcv is involved in the potassium ion transport.

The experiment focused on the precise role of PA subunit of RNA-dependent RNA Polymerase in transcription. Previous research has suggested that mutant H510A in PA subunit has impaired endonuclease activity and selective inhibited transcription. They used three mutant phenotypes of PA subunit: K102A, D108A, and K134A to determine the effect on polymerase activity. No significant endonuclease activity was determined for mutations which indicates that PA is involved in endonuclease activity (Fig. 5D and G).

The protein Q9FZR9 is involved in lipolytic activity as shown by figure 3. It was hypothesized to have that activity based on this motif. Gly-Tyr-Ser-Gln-Gly. The enzymatic activity done invitro matches this hypothesis. The paper is investigating additional proteins to help with cell lysis using the specific bacteriophage MS6 a phage that infects Mycobacterium smegmatis. They specifically look at the product of gene LysB which is the protein in question. Figure 3 demonstrates the lipolytic activity by using the product of LysB to produce a zone of clearance in plates coated with triglycerides such as triolein.

According to the paper the protein specifically the C terminus end is involved in the degradation of peptidoglycan . The protein has peptidoglycan hydrolase activity. When mixed with peptidoglycan it was shown to give products and degrade peptidoglycan using it as a substrate. Figure six shows the hydrolytic capability of the protein by comparing it to sonicated ( sonication is a method used to disrupt cell membranes) cells. With the PB2-Cterm we can see that the B galactosidase coming out from the bacteria reached a level 60 percent to that of sonicated cells. Which is further proof of peptidoglycan hyrolysis. The control designed for this part was only adding DDM which didn't end up causing any B galactosidase to come out of the bacteria.

The paper focused on gene EF0737 from Enterococcus faecalis .The authors evaluated interaction of recombinant EF0737 protein with fibrinogen proteins using a western blot (Fig. 6).