Preprint Review Version 1 This version is not peer-reviewed

Bacterial Sialoglycosidases in Virulence and Pathogenesis

Version 1 : Received: 15 January 2019 / Approved: 16 January 2019 / Online: 16 January 2019 (08:49:16 CET)

A peer-reviewed article of this Preprint also exists.

Sudhakara, P.; Sellamuthu, I.; Aruni, A.W. Bacterial sialoglycosidases in Virulence and Pathogenesis. Pathogens 2019, 8, 39. Sudhakara, P.; Sellamuthu, I.; Aruni, A.W. Bacterial sialoglycosidases in Virulence and Pathogenesis. Pathogens 2019, 8, 39.

Journal reference: Pathogens 2019, 8, 39
DOI: 10.3390/pathogens8010039

Abstract

Periodontitis is a chronic inflammatory disease affecting the tissues that surround and support the teeth. In the U. S., approximately 65 million people are affected by this condition. Its occurrence is also associated with many important systemic diseases such as cardiovascular disease, rheumatoid arthritis, and Alzheimer’s disease. Among the most important etiologies of periodontitis is Porphyromonas gingivalis, a keystone bacterial pathogen. Keystone pathogens can orchestrate inflammatory disease by remodeling a normally benign microbiota causing imbalance between normal and pathogenic microbiota (dysbiosis). The important characteristics of P. gingivalis causing dysbiosis are its virulence factors that cause effective subversion of host defenses to its advantage [1], allowing other pathogens to grow. However, the mechanisms involving these processes are poorly understood. However, various microbial strategies target host sialoglycoproteins for immune dysregulation. In addition, the enzymes that break down sialoglycoproteins/sialoglycans are the “sialoglycoproteases”, resulting in exposed terminal sialic acid. This process could lead to pathogen-toll like receptor (TLR) interactions mediated through sialic acid receptor–ligand mechanisms. By assessing the function of P. gingivalis sialoglycoproteases, could pave the way to designing carbohydrate analogues and sialic acid mimetics to serve as drug targets.

Subject Areas

sialidase; sialic acid; sialoglycoprotease; pathogenicity; therapeutic target; siglec

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