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Volume 11
Journal of Proteomics & Bioinformatics
ISSN: 0974-276X
Structural Biology 2018
September 24-26, 2018
September 24-26, 2018 | Berlin, Germany
14
th
International Conference on
Structural Biology
Sequence to structure and immunological analysis of MOMP from
Chlamydiae
Francis O Atanu
Kogi State University, Nigeria
T
he major outer membrane protein (MOMP) is the most abundant (60% by weight) protein in the cell membrane of
the
Chlamydiae
family. Its cellular localization makes it important for survival, host cell adhesion, invasion and other
pathological schemes of
Chlamydiae
. MOMP has been reported to possess antibody neutralizing properties as well as provoking
unique inflammatory immune response. This protein conserved in all species of
Chlamydiae
is a vaccine target against human
and livestock diseases. This report focuses on bioinformatics and wet laboratory approaches utilized for the analysis of this 40
kDa, 389 aa protein. Bioinformatics analysis revealed that MOMP is a β-barrel protein with surface exposed peptide epitopes.
Further bioinformatics using the SYBYL-X flexible docking protocol shows that the peptides formed stable complexes with
MHC class II and surface exposed aliphatic side chains that may be accessible to T-cell receptors. In fact, other research groups
have shown that these peptides have anti-inflammatory effect in an animal model of atherosclerosis. MOMP was effectively
cloned, expressed and purified for structural studies. Analysis of MOMP by circular dichroism revealed that MOMP is a
β-sheet rich protein which proved to be more thermostable in the presence of fatty acids and intermediates of the citric acid
cycle. Finally, a low-resolution structure 4 Å for MOMP has been obtained by molecular replacement based on FadL of E. coli.
The findings from this work opens new frontier for the development of drugs and vaccines that target MOMP.
J Proteomics Bioinform 2018, Volume 11
DOI: 10.4172/0974-276X-C2-116