OmpW is positively regulated by iron via Fur, and negatively regulated by SoxS contribution to oxidative stress resistance in Escherichia coli.

Iron plays a central role at the interface of pathogen and host. The ability to sequester iron from a host not only reduces host immune defenses but also promotes pathogen virulence, leading to the occurrence of infectious disease. Recently, outer membrane protein OmpW was shown to protect bacteria against harsh environmental conditions and to play a role in infectious disease.

LptD is a promising vaccine antigen and potential immunotherapeutic target for protection against Vibrio species infection.

Outer membrane proteins (OMPs) are unique to Gram-negative bacteria. Several features, including surface exposure, conservation among strains and ability to induce immune responses, make OMPs attractive targets for using as vaccine antigens and immunotherapeutics. LptD is an essential OMP that mediates the final transport of lipopolysaccharide (LPS) to outer leaflet.

Contribution of the outer membrane protein OmpW in Escherichia coli to complement resistance from binding to factor H.

The serum complement system is essential for innate immune defense against invading pathogenic bacteria. Some of the 8-stranded β-barrel outer membrane proteins confer bacterial resistance to the innate host immunity. We have previously demonstrated that OmpW, also an 8-stranded β-barrel protein that was identified a decade ago, protects bacteria against host phagocytosis.

Immunoproteomic Approach for Screening Vaccine Candidates from Bacterial Outer Membrane Proteins.

Outer membrane proteins (OMPs) are unique to Gram-negative bacteria and have been revealed as potential vaccine candidates for conferring protection against infections in recent years. Immunoproteomics is a powerful technique that is ideally suited to screen and identify potential vaccine candidates. This chapter presents a brief outline of the screening of immunogenic OMPs from Vibrio parahaemolyticus by an immunoproteomic strategy that was based on two-dimensional electrophoresis (2-DE) and immunoblotting.

Global Analysis of Protein Lysine Succinylation Profiles and Their Overlap with Lysine Acetylation in the Marine Bacterium Vibrio parahemolyticus.

Protein lysine acylation, including acetylation and succinylation, has been found to be a major post-translational modification (PTM) and is associated with the regulation of cellular processes that are widespread in bacteria. Vibrio parahemolyticus is a model marine bacterium that causes seafood-borne illness in humans worldwide. The lysine acetylation of V.

Identification of a novel vaccine candidate by immunogenic screening of Vibrio parahaemolyticus outer membrane proteins.

Vibrio parahaemolyticus is an important halophilous pathogen that can cause not only a broad range of disease in aquatic animals but also serious seafood-borne illness in humans as a result of the consumption of seafood. To avoid the use of antibiotics, it is critical to identify protective antigens for developing highly effective vaccines against this pathogen. Outer membrane proteins (OMPs) have been suggested as potential vaccine candidates for conferring protection against infection.

Systematic analysis of the lysine acetylome in Vibrio parahemolyticus.

Lysine acetylation of proteins is a major post-translational modification that plays an important regulatory role in almost every aspect of cells, both eukaryotes and prokaryotes. Vibrio parahemolyticus, a model marine bacterium, is a worldwide cause of bacterial seafood-borne illness. Here, we conducted the first lysine acetylome in this bacterium through a combination of highly sensitive immune-affinity purification and high-resolution LC-MS/MS.