Influenza D virus diverges from its related influenza C virus in the recognition of 9-O-acetylated N-acetyl- or N-glycolyl-neuraminic acid-containing glycan receptors

Runxia Liu, Chithra Sreenivasan, Hai Yu, Zizhang Sheng, Simon J. Newkirk, Wenfeng An, David F. Smith, Xi Chen, Dan Wang, Feng Li

Research output: Contribution to journalArticlepeer-review

19 Scopus citations

Abstract

Influenza D virus (IDV) utilizes bovines as a primary reservoir with periodical spillover to other mammalian hosts. By using traditional hemagglutination assay coupled with sialoglycan microarray (SGM) platform and functional assays, we demonstrated that IDV is more efficient in recognizing both 9-O-acetylated N-acetylneuraminic acid (Neu5,9Ac2) and 9-O-acetylated N-glycolylneuraminic acid (Neu5Gc9Ac) than influenza C virus (ICV), a ubiquitous human pathogen. ICV seems to strongly prefer Neu5,9Ac2 over Neu5Gc9Ac. Since Neu5Gc9Ac is different from Neu5,9Ac2 only by an additional oxygen in the group at the C5 position, our results reveal that the hydroxyl group in Neu5Gc9Ac plays a critical role in determining receptor binding specificity, which as a result may discriminate IDV from ICV in communicating with 9-O-acetylated SAs. These findings shall provide a framework for further investigation towards better understanding of how newly discovered multiple-species-infecting IDV exploits natural 9-O-acetylated SA variations to expand its host range.

Original languageEnglish
Pages (from-to)16-23
Number of pages8
JournalVirology
Volume545
DOIs
StatePublished - Jun 2020

Bibliographical note

Funding Information:
This work was partially supported by NIH grants R01AI141889 and R01AI130684 and NIH Grant GM62116 , by SDSU AES 3AH-477 , by National Science Foundation/EPSCoR ( http://www.nsf.gov/od/iia/programs/epscor/index.jsp ) award IIA-1335423, and by the state of South Dakota’s Governor’s Office of Economic Development as a South Dakota Research Innovation Center.

Funding Information:
We thank all the members of the Li and Wang laboratories for their input into this work. We thank Dr. Reinhard Vlasak at University of Salzburg, Austria, for many valuable suggestions about our experiments. We also thank Peter Palese (Mt. Sinai Medical School, New York) for providing the C/Johannesburg/1/66 virus. We thank the Consortium for Functional Glycomics (Core H) that conducted glycan microarray assays. which was supported by NIH Grant GM62116 .

Funding Information:
This work was partially supported by NIH grants R01AI141889 and R01AI130684 and NIH Grant GM62116, by SDSU AES 3AH-477, by National Science Foundation/EPSCoR (http://www.nsf.gov/od/iia/programs/epscor/index.jsp) award IIA-1335423, and by the state of South Dakota's Governor's Office of Economic Development as a South Dakota Research Innovation Center.We thank all the members of the Li and Wang laboratories for their input into this work. We thank Dr. Reinhard Vlasak at University of Salzburg, Austria, for many valuable suggestions about our experiments. We also thank Peter Palese (Mt. Sinai Medical School, New York) for providing the C/Johannesburg/1/66 virus. We thank the Consortium for Functional Glycomics (Core H) that conducted glycan microarray assays. which was supported by NIH Grant GM62116.

Publisher Copyright:
© 2020

Keywords

  • Glycan receptors
  • Influenza C virus
  • Influenza D virus

ASJC Scopus subject areas

  • Virology

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