structural homology modeling and functional characterization of variable lipoprotein hemagglutin proteins.

variable lipoprotein hemagglutin (vlhA) proteins are crucial for immune evasion from the host cells, permitting the persistence and survival of the pathogen. However, the exact molecular mechanism behind the immune evasion function is still not clear. physiochemical analysis, domain analysis, subcellular localization, and homology modeling studies have been carried out to predict the structural and functional properties of these proteins. The outcomes of this study provide significant preliminary data for understanding the immune evasion by vlhA proteins. In this study, we have reported the primary, secondary, and tertiary structural characteristics and subcellular localization, presence of the transmembrane helix and signal peptide, and functional characteristics of vlhA proteins from strain R low. The results show variation between the structural and functional components of the proteins, signifying the role and diverse molecular mechanisms in functioning of vlhA proteins in host immune evasion. Moreover the 3D structure predicted in this study will pave a way for understanding vlhA protein function and its interaction with other molecules to undergo immune evasion. This study forms the basis for future experimental studies improving our understanding in the molecular mechanisms used by vlhA proteins.