title: Porcine Sapelovirus Uses α2,3-Linked Sialic Acid on GD1a Ganglioside as a Receptor.
abstract: The receptor(s) for porcine sapelovirus (PSV), which causes diarrhea, pneumonia, polioencephalomyelitis, and reproductive disorders in pigs, remains largely unknown. Given the precedent for other picornaviruses which use terminal sialic acids (SAs) as receptors, we examined the role of SAs in PSV binding and infection. Using a variety of approaches, including treating cells with a carbohydrate-destroying chemical (NaIO4), mono- or oligosaccharides (N-acetylneuraminic acid, galactose, and 6'-sialyllactose), linkage-specific sialidases (neuraminidase and sialidase S), lectins (Maakia amurensislectin andSambucus nigralectin), proteases (trypsin and chymotrypsin), and glucosylceramide synthase inhibitors (dl-threo-1-phenyl-2-decanoylamino-3-morpholino-1-propanol and phospholipase C), we demonstrated that PSV could recognize α2,3-linked SA on glycolipids as a receptor. On the other hand, PSVs had no binding affinity for synthetic histo-blood group antigens (HBGAs), suggesting that PSVs could not use HBGAs as receptors. Depletion of cell surface glycolipids followed by reconstitution studies indicated that GD1a ganglioside, but not other gangliosides, could restore PSV binding and infection, further confirming α2,3-linked SA on GD1a as a PSV receptor. Our results could provide significant information on the understanding of the life cycle of sapelovirus and other picornaviruses. For the broader community in the area of pathogens and pathogenesis, these findings and insights could contribute to the development of affordable, useful, and efficient drugs for anti-sapelovirus therapy.
  
  
  OBJECTIVE
  The porcine sapelovirus (PSV) is known to cause enteritis, pneumonia, polioencephalomyelitis, and reproductive disorders in pigs. However, the receptor(s) that the PSV utilizes to enter host cells remains largely unknown. Using a variety of approaches, we showed that α2,3-linked terminal sialic acid (SA) on the cell surface GD1a ganglioside could be used for PSV binding and infection as a receptor. On the other hand, histo-blood group antigens also present in the cell surface carbohydrates could not be utilized as PSV receptors for binding and infection. These findings should contribute to the understanding of the sapelovirus life cycle and to the development of affordable, useful and efficient drugs for anti-sapelovirus therapy.
authors: Laboratory of Veterinary Pathology, College of Veterinary Medicine, Chonnam National University, Gwangju, Republic of Korea.
authors: Deok-Song
authors: DS
authors: Kim
authors: Laboratory of Veterinary Pathology, College of Veterinary Medicine, Chonnam National University, Gwangju, Republic of Korea.
authors: Kyu-Yeol
authors: KY
authors: Son
authors: Laboratory of Veterinary Pathology, College of Veterinary Medicine, Chonnam National University, Gwangju, Republic of Korea.
authors: Kyung-Min
authors: KM
authors: Koo
authors: Laboratory of Veterinary Pathology, College of Veterinary Medicine, Chonnam National University, Gwangju, Republic of Korea.
authors: Ji-Yun
authors: JY
authors: Kim
authors: Laboratory of Veterinary Pathology, College of Veterinary Medicine, Chonnam National University, Gwangju, Republic of Korea.
authors: Mia Madel
authors: MM
authors: Alfajaro
authors: Laboratory of Veterinary Pathology, College of Veterinary Medicine, Chonnam National University, Gwangju, Republic of Korea.
authors: Jun-Gyu
authors: JG
authors: Park
authors: Laboratory of Veterinary Pathology, College of Veterinary Medicine, Chonnam National University, Gwangju, Republic of Korea.
authors: Myra
authors: M
authors: Hosmillo
authors: Laboratory of Veterinary Pathology, College of Veterinary Medicine, Chonnam National University, Gwangju, Republic of Korea.
authors: Mahmoud
authors: M
authors: Soliman
authors: Laboratory of Veterinary Pathology, College of Veterinary Medicine, Chonnam National University, Gwangju, Republic of Korea.
authors: Yeong-Bin
authors: YB
authors: Baek
authors: Laboratory of Veterinary Pathology, College of Veterinary Medicine, Chonnam National University, Gwangju, Republic of Korea.
authors: Eun-Hyo
authors: EH
authors: Cho
authors: Chonnam National University Veterinary Teaching Hospital, Gwangju, Republic of Korea.
authors: Ju-Hwan
authors: JH
authors: Lee
authors: Laboratory of Veterinary Pathology, College of Veterinary Medicine, Chonnam National University, Gwangju, Republic of Korea.
authors: Mun-Il
authors: MI
authors: Kang
authors: Division of Virology, Department of Pathology, University of Cambridge, Addenbrooke's Hospital, Cambridge, United Kingdom ig299@cam.ac.uk choko@chonnam.ac.kr.
authors: Ian
authors: I
authors: Goodfellow
authors: Laboratory of Veterinary Pathology, College of Veterinary Medicine, Chonnam National University, Gwangju, Republic of Korea ig299@cam.ac.uk choko@chonnam.ac.kr.
authors: Kyoung-Oh
authors: KO
authors: Cho
mesh_terms: D000818:Animals; D001789:Blood Group Antigens / Q000378:metabolism; D002241:Carbohydrates / Q000737:chemistry; D002460:Cell Line; D004771:Enteroviruses, Porcine / Q000378:metabolism*; D005732:Gangliosides / Q000378:metabolism*; D006367:HeLa Cells; D006801:Humans; D019158:N-Acetylneuraminic Acid / Q000737:chemistry / Q000378:metabolism*; D011991:Receptors, Virus / Q000737:chemistry / Q000378:metabolism*; D013552:Swine; D053585:Virus Attachment
chemical_list: D001789:Blood Group Antigens; D002241:Carbohydrates; D005732:Gangliosides; D011991:Receptors, Virus; C021298:ganglioside, GD1a; D019158:N-Acetylneuraminic Acid