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Journal of Virology, May 2001, p. 4604-4613, Vol. 75, No. 10
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.10.4604-4613.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Receptor Specificities of Human Respiroviruses

Takashi Suzuki,1,2,* Allen Portner,1,3 Ruth Ann Scroggs,1 Makoto Uchikawa,4 Noriko Koyama,2 Kazuko Matsuo,2 Yasuo Suzuki,2 and Toru Takimoto1,*

Department of Virology and Molecular Biology, St. Jude Children's Research Hospital, Memphis, Tennessee 381051; Department of Biochemistry, School of Pharmaceutical Sciences, University of Shizuoka, 52-1 Yada, Shizuoka 422-8526,2 and Central Blood Center, Japanese Red Cross, 4-1-31 Hiroo, Shibuya-ku, Tokyo 150-0012,4 Japan; and Department of Pathology, The Health Science Center, University of Tennessee, Memphis, Tennessee 381633

Received 6 November 2000/Accepted 13 February 2001

Through their hemagglutinin-neuraminidase glycoprotein, parainfluenza viruses bind to sialic acid-containing glycoconjugates to initiate infection. Although the virus-receptor interaction is a key factor of infection, the exact nature of the receptors that human parainfluenza viruses recognize has not been determined. We evaluated the abilities of human parainfluenza virus types 1 (hPIV-1) and 3 (hPIV-3) to bind to different types of gangliosides. Both hPIV-1 and hPIV-3 preferentially bound to neolacto-series gangliosides containing a terminal N-acetylneuraminic acid (NeuAc) linked to N-acetyllactosamine (Galbeta 1-4GlcNAc) by the alpha 2-3 linkage (NeuAcalpha 2-3Galbeta 1-4GlcNAc). Unlike hPIV-1, hPIV-3 bound to gangliosides with a terminal NeuAc linked to Galbeta 1-4GlcNAc through an alpha 2-6 linkage (NeuAcalpha 2-6Galbeta 1-4GlcNAc) or to gangliosides with a different sialic acid, N-glycolylneuraminic acid (NeuGc), linked to Galbeta 1-4GlcNAc (NeuGcalpha 2-3Galbeta 1-4GlcNAc). These results indicate that the molecular species of glycoconjugate that hPIV-1 recognizes are more limited than those recognized by hPIV-3. Further analysis using purified gangliosides revealed that the oligosaccharide core structure is also an important element for binding. Gangliosides that contain branched N-acetyllactosaminoglycans in their core structure showed higher avidity than those without them. Agglutination of human, cow, and guinea pig erythrocytes but not equine erythrocytes by hPIV-1 and hPIV-3 correlated well with the presence or the absence of sialic acid-linked branched N-acetyllactosaminoglycans on the cell surface. Finally, NeuAcalpha 2-3I, which bound to both viruses, inhibited virus infection of Lewis lung carcinoma-monkey kidney cells in a dose-dependent manner. We conclude that hPIV-1 and hPIV-3 preferentially recognize oligosaccharides containing branched N-acetyllactosaminoglycans with terminal NeuAcalpha 2-3Gal as receptors and that hPIV-3 also recognizes NeuAcalpha 2-6Gal- or NeuGcalpha 2-3Gal-containing receptors. These findings provide important information that can be used to develop inhibitors that prevent human parainfluenza virus infection.

* Corresponding author. Mailing address for Takashi Suzuki or Toru Takimoto: Department of Virology and Molecular Biology, St. Jude Children's Research Hospital, 332 N. Lauderdale, Memphis, TN 38105-2794. Phone: (901) 495-3438. Fax: (901) 523-2622. E-mail: toru.takimoto{at}stjude.org.

Journal of Virology, May 2001, p. 4604-4613, Vol. 75, No. 10
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.10.4604-4613.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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