Nuclear Surface N-Acetyl Neuraminic Acid Terminating Receptors for Myxovirus Attachment

Abstract

INSIGHT into the molecular organization of cellular membranes may be gained by defining their molecular components in terms of functional groups which serve as receptors for virus attachment. Thus, the specific attachment of myxovirus to neuraminic acid-terminating glyco-protein groups on the cell surface and the loss of virus binding capacity following exposure of cells to neuraminidase serve to define the neuraminic acid molecule in its role as a functional receptor on the plasma membrane¹. This report describes the first use of this approach to map the surface of nuclei by comparing the characteristics of myxovirus attachment and elution of whole cells with isolated nuclei. Here we demonstrate that the surface of cytoplasm-free nuclei prepared by treating cells with an anionic detergent contains specific receptors for the attachment of myxovirus, and that in terms of viral adsorption and elution the surface of nuclei isolated from HeLa cells reacts much like that of an erythrocyte, or of a host cell the viral engulfment capacity of which has boon destroyed by heat.