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An In vitro Model to Study Immune Responses of Human Peripheral Blood Mononuclear Cells to Human Respiratory Syncytial Virus Infection
Published on: December 10, 2013
Receptor specificities of human respiroviruses
T Suzuki1, A Portner, R A Scroggs
1Department of Virology and Molecular Biology, St. Jude Children's Research Hospital, Memphis, Tennessee 38105.
Journal of Virology
|April 20, 2001
Summary
Human parainfluenza viruses (hPIV-1 and hPIV-3) bind to specific sialic acid structures on host cells. Understanding these viral receptors is key to developing new antiviral therapies.
Area of Science:
- Virology
- Glycobiology
- Molecular Biology
Background:
- Human parainfluenza viruses (hPIVs) initiate infection by binding to sialic acid-containing glycoconjugates via their hemagglutinin-neuraminidase glycoprotein.
- The precise nature of the receptors recognized by hPIVs remains largely undetermined, hindering the development of targeted antiviral strategies.
Purpose of the Study:
- To investigate the binding specificities of human parainfluenza virus type 1 (hPIV-1) and type 3 (hPIV-3) to various gangliosides.
- To elucidate the role of specific sialic acid linkages and oligosaccharide core structures in hPIV-hPIV-receptor interactions.
- To identify potential targets for developing inhibitors against hPIV infections.
Main Methods:
- Evaluated the binding capabilities of hPIV-1 and hPIV-3 to different types of gangliosides.
- Analyzed the influence of terminal sialic acid linkages (alpha2-3 and alpha2-6) and sialic acid types (NeuAc and NeuGc) on viral binding.
- Assessed the impact of oligosaccharide core structures, specifically branched N-acetyllactosaminoglycans, on viral avidity.
- Correlated erythrocyte agglutination patterns with ganglioside receptor presence.
- Tested the inhibitory potential of a specific ganglioside (NeuAcalpha2-3I) on virus infection in cell cultures.
Main Results:
- Both hPIV-1 and hPIV-3 preferentially bound to neolacto-series gangliosides with terminal N-acetylneuraminic acid (NeuAc) linked via an alpha2-3 linkage.
- hPIV-3 exhibited broader binding, recognizing gangliosides with NeuAc linked via alpha2-6 or N-glycolylneuraminic acid (NeuGc) linked via alpha2-3.
- Gangliosides with branched N-acetyllactosaminoglycans in their core structure demonstrated higher binding avidity for both viruses.
- Erythrocyte agglutination correlated with the presence of sialic acid-linked branched N-acetyllactosaminoglycans.
- NeuAcalpha2-3I significantly inhibited hPIV infection in a dose-dependent manner.
Conclusions:
- hPIV-1 and hPIV-3 primarily recognize oligosaccharides with branched N-acetyllactosaminoglycans and terminal NeuAcalpha2-3Gal as receptors.
- hPIV-3 demonstrates additional binding capabilities to receptors containing NeuAcalpha2-6Gal or NeuGcalpha2-3Gal.
- These findings offer crucial insights for the development of novel inhibitors to prevent human parainfluenza virus infections.
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