Receptor binding and immunogenic properties of the receptor binding domain of influenza D virus hemagglutinin-esterase-fusion protein expressed from Escherichia coli.

Autor: Naveed A; Maxwell H. Gluck Equine Research Center, Department of Veterinary Science, University of Kentucky, Lexington, KY, 40546, USA., Yu J; Maxwell H. Gluck Equine Research Center, Department of Veterinary Science, University of Kentucky, Lexington, KY, 40546, USA., Lawson S; Department of Veterinary and Biomedical Science, South Dakota State University, Brookings, SD, 57007, USA., Gao R; Department of Biology and Microbiology, South Dakota State University, Brookings, SD, 57007, USA., Ni S; Department of Chemistry and Biochemistry, Miami University, Oxford, OH, 45056, USA., Paulchakrabarti M; Department of Cellular and Molecular Medicine, Glycobiology Research and Training Center, University of California, San Diego, La Jolla, CA, 92093, USA., Choudhury B; Department of Cellular and Molecular Medicine, Glycobiology Research and Training Center, University of California, San Diego, La Jolla, CA, 92093, USA., Christopher-Hennings J; Department of Veterinary and Biomedical Science, South Dakota State University, Brookings, SD, 57007, USA., Nelson E; Department of Veterinary and Biomedical Science, South Dakota State University, Brookings, SD, 57007, USA., Sheng Z; Zuckerman Mind Brian Behavior Institute, Columbia University, New York, NY, USA., Kennedy MA; Department of Chemistry and Biochemistry, Miami University, Oxford, OH, 45056, USA., Li F; Maxwell H. Gluck Equine Research Center, Department of Veterinary Science, University of Kentucky, Lexington, KY, 40546, USA. Electronic address: Feng.Li@uky.edu., Wang D; Maxwell H. Gluck Equine Research Center, Department of Veterinary Science, University of Kentucky, Lexington, KY, 40546, USA. Electronic address: Dan.Wang@uky.edu.
Jazyk: angličtina
Zdroj: Virology [Virology] 2024 Sep; Vol. 597, pp. 110138. Date of Electronic Publication: 2024 Jun 12.
DOI: 10.1016/j.virol.2024.110138
Abstrakt: The hemagglutinin-esterase-fusion (HEF) protein binds 9-O-acetylated sialic acids-containing glycans on the cell surface and drives influenza D virus (IDV) entry. The HEF is a primary determinant of the exceptional thermal and acid stability observed in IDV infection biology. Here, we expressed and purified the receptor binding domain (RBD) of the IDV HEF protein in Escherichia coli and characterized its receptor binding and antigenic properties. The data from these experiments indicate that (i) the RBD can bind with specificity to turkey red blood cells (RBC), and its binding can be specifically inhibited by IDV antibody; (ii) the RBD efficiently binds to the cell surface of MDCK cells expressing the receptor of IDV; and (iii) anti-RBD antibodies are capable of blocking RBD attachment to MDCK cells as well as of inhibiting the virus from agglutinating RBCs. These observations support the utility of this RBD in future receptor and entry studies of IDV.
Competing Interests: Declaration of competing interest The authors have read the journal's policy and declare that there are no conflicts of interest.
(Copyright © 2024 Elsevier Inc. All rights reserved.)
Databáze: MEDLINE
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