Isolation in Pure Culture of Human Oral Organisms capable of producing Neuraminidase

Abstract

PREVIOUS reports^1–3 have indicated that most, if not all, of the carbohydrate components of the mixture of glycoproteins as they exist as saliva in the human mouth are labile and are released by induced enzymes of bacterial origin. One of these enzymes—neuraminidase or sialidase—is of particular interest because the loss of sialic acid from saliva causes some of the glycoprotein components to precipitate out of solution, and this reaction may be an important factor responsible for the formation of dental plaque on the teeth. The loss of the other carbohydrate components (three hexoses, two hexosamines and fucose) must influence the calcium binding capacities of the residual proteins and this reaction must also be of significance in the formation of both dental plaque and calculus. Dental plaque has already been shown to bind more calcium than does an equivalent amount of salivary protein⁴. Neuraminidase is also of interest in other fields, where it has been shown, for example, to be the receptor destroying enzyme of myxovirus to erythrocytes⁵ and its presence could also be responsible for markedly changing the physical characteristics of mucins throughout the body during certain disease processes.