Role of sialic acid-containing molecules in paramyxovirus entry into the host cell: A minireview

Abstract

Sialic acid-containing compounds play a key role in the initial steps of the paramyxovirus life cycle. As enveloped viruses, their entry into the host cell consists of two main events: binding to the host cell and membrane fusion. Virus adsorption occurs at the surface of the host cell with the recognition of specific receptor molecules located at the cell membrane by specific viral attachment proteins. The viral attachment protein present in some paramyxoviruses (Respirovirus, Rubulavirus and Avulavirus) is the HN glycoprotein, which binds to cellular sialic acid-containing molecules and exhibits sialidase and fusion promotion activities. Gangliosides of the gangliotetraose series bearing the sialic acid N-acetylneuraminic (Neu5Ac) on the terminal galactose attached in alpha2-3 linkage, such as GD1a, GT1b, and GQ1b, and neolacto-series gangliosides are the major receptors for Sendai virus. Much less is known about the receptors for other paramyxoviruses than for Sendai virus. Human parainfluenza viruses 1 and 3 preferentially recognize oligosaccharides containing N-acetyllactosaminoglycan branches with terminal Neu5Acalpha2-3Gal. In the case of Newcastle disease virus, has been reported the absence of a specific pattern of the gangliosides that interact with the virus. Additionally, several works have described the use of sialylated glycoproteins as paramyxovirus receptors. Accordingly, the design of specific sialic acid analogs to inhibit the sialidase and/or receptor binding activity of viral attachment proteins is an important antiviral strategy. In spite of all these data, the exact nature of paramyxovirus receptors, apart from their sialylated nature, and the mechanism(s) of viral attachment to the cell surface are poorly understood.

Efficient eradication of hormone‐resistant human prostate cancers by inactivated Sendai virus particle

“…Peak 2 from the 4 different cells consisted of SPG, GD1a and LST-a. Because both GD1a and SPG are receptors for HVJ, 32 Peaks 2 were further purified by reversed phase HPLC. Peaks 2 from PC3, DU145, LNcap and PNT2 were separated into 2, 3, 1 and 2 major components, respectively (Fig.…”

“…The receptors of HVJ are GD1a and SPG. 32 Both gangliosides bearing N-acetylneuraminic acid attached on terminal galactose residues by a2-3 linkages that are recognized by HN protein of HVJ. 32 These molecules are thought to be widely distributed among various cell lines.…”

“…32 Both gangliosides bearing N-acetylneuraminic acid attached on terminal galactose residues by a2-3 linkages that are recognized by HN protein of HVJ. 32 These molecules are thought to be widely distributed among various cell lines. 32 However, when the cell surface gangliosides within prostate epithelium was precisely examined, GD1a gangliosides were found to be the most prevalent gangliosides among prostate cancer cell lines, including PC3 and DU145, whereas GD1a gangliosides were barely detectable in both hormone-sensitive prostate cancer LNCap cells and normal prostate epithelium using thin-layer chromatography.…”

“…32 These molecules are thought to be widely distributed among various cell lines. 32 However, when the cell surface gangliosides within prostate epithelium was precisely examined, GD1a gangliosides were found to be the most prevalent gangliosides among prostate cancer cell lines, including PC3 and DU145, whereas GD1a gangliosides were barely detectable in both hormone-sensitive prostate cancer LNCap cells and normal prostate epithelium using thin-layer chromatography. 43,44 Furthermore, when we determined the quantity of gangliosides in prostate cancer cell lines using HPLC, we found that SPG, another receptor for HVJ, also increased in hormonerefractory prostate cancer cells as well as GD1a.…”

“…This is also a receptor for HVJ. 32 The terminal sialic acid of SPG is transferred by ST3Gal VI. 45 Human ST3Gal VI gene is expressed by alternative promoter utilization and one of the 2 promoters is specifically activated in PC3 cells.…”