CHARACTERIZATION OF THE 49.4 KDA ADHESIN OF PORPHYROMONAS GINGIVALIS OUTER MEMBRANE PROTEIN AND ITS INTERACTION WITH NEUTROPHILS

Abstract

Periodontitis is caused mostly by Porphyromonas  gingivalis (P. gingivalis) and it relates to acute coronary syndrome. P. gingivalis readily invades into blood circulation and potentially induces collagenolytic activity of neutrophil which results in collagen vascular degradation and leads to atherosclerotic plague rupture (APR). Neutrophil has a role event in APR and is responsible for the occurrence of fatal cardiovascular events such as acute myocardial infarction (AMI). This information brought out notion concerning the adhesion interaction of P.gingivalis with neutrophil.  

The aim of the study is to assess adhesion molecule of P. gingivalis outer membrane protein (OMP).

The study was done by partial characterization taken in hemagglutination assay using mice erythrocytes, adhesion inhibition assay by gradual concentration of adhesion blocked in neutrophil, immunologic assay using Western-blotting and immunocytochemistry. 

The results showed that 49.4 kDa P.  gingivalis OMP can agglutinate mice erythrocytes  and adhere to netrophil. The increasing concentration of OMP P.  gingivalis 49.4 kDa reduces adhesion process to netrophil. This protein was recognized by the polyclonal antibody of 49.4 kDa adhesion molecule. 

It can be concluded that 49.4 kDa P. gingivalis outer OMP is a hemagglutinin and an adhesion molecule to netrophil.