MOLECULAR DOCKING ANALYSIS OF HUMAN TRANSFERRIN AND LACTOFERRIN BINDING PROTEINS OF NEISSERIA MENINGITIDIS WITH 5 HYDROXY 1-4 NAPHTHOQINONE.

Abstract

Neisseria meningitidis is the principal cause of bacterial meningitis.. Bacteria can be
transmitted by carriers through the droplets of respiratory secretions and can only infect
humans. The mortality rate of bacterial meningitis is very high even after the discovery
of many antibiotics. Acquisition of iron is the major determinant in the pathogenesis of
Neisseria meningitidis which is fulfilled by human host proteins like transferrin,
lactoferrin, hemoglobin, and haptoglobin-hemoglobin. Present study is performed on
transferrin binding protein A, transferrin binding protein B, lactoferrin binding protein A
and lactoferrin binding protein B which together constitutes receptors for human
transferrin, and lactoferrin iron complex in Neisseria menningitidis which further are
responsible for the transport of essential iron. Crystal structures of TbpA and TbpB are
taken from Protein data bank while sequences of LbpA and LbpB are retrieved from
NCBI and modeled by using Geno3D. Molecular docking studies are performed by
taking Juglone or 5 hydroxy 1-4 naphthoqinone as a ligand. Binding energies are
calculated and interactions are studied. Our findings suggest Juglone shows effective
binding with these proteins with much lesser binding energies can be used for clinical
trials for the treatment of meningitis.