CHARACTERIZATION OF SABA VIRULENCE FACTOR OF HELICOBACTER PYLORI VIA IN-SILICO TOOLS

Abstract

Helicobacter pylori infection of human gastrointestinal tract (GIT) largely depend on its attachment with stomach mucosal lining. This adherence is modulated by Sialic acid binding adhesion (SabA) protein. In current project, sequence of this protein was retrieved from Uniprot database and analyzed through SOPMA tool, AlphaFold database and MEME suite. The secondary (2D) configuration analysis showed alpha helix, extended strand, beta turn and random coil contents of 54.29, 11.04, 1.69 and 32.98%. Three dimensional (3D) structural analysis revealed highly complex folding in protein with two major domains. Seven conserved motifs. i. e., cpglenc, lcalsgc, atydkmkklaeelqaaqq, rtnlamkkkedsehsaqh, atyndaktlseeisklph, ffgeskrw and fnsssdvw were found with significant p-values (p < 0.05). The conserved motifs unraveled in this project might help in designing drugs for inhibition of SabA binding with its receptors. In addition, the 2D and 3D configuration might also help in modification and blockage of this virulence factor thus reducing the H. pylori human infections