Substrate Specificity of Equine and Human Influenza A Virus Sialidase to Molecular Species of Sialic Acid.
Abstract: Most equine influenza A viruses (IAVs) show strong binding to glycoconjugates containing N-glycolylneuraminic acid (Neu5Gc) as well as N-acetylneuraminic acid (Neu5Ac). Therefore, the progeny of equine IAV is thought to be released from the infected cell surface through removal of sialic acids by the viral sialidase. In the present study, equine IAV sialidases showed significantly lower substrate affinity than that of human IAV sialidases to artificial and natural Neu5Gc-conjugated substrates. The substrate specificity of equine IAV sialidases is in disagreement with their binding specificity to molecular species of sialic acid. The results suggest that substrate specificity of equine IAV sialidase for Neu5Ac, rather than for Neu5Gc, is important for an advantage at the early infection stage and the process of progeny virus release from the surface of infected cells.
Publication Date: 2016-10-12 PubMed ID: 27725453DOI: 10.1248/bpb.b16-00345Google Scholar: Lookup
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Summary
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This research examines the difference in substrate specificity of the sialidase enzyme in equine and human influenza A viruses (IAVs). Despite the expected preference for N-glycolylneuraminic acid (Neu5Gc), the study found that equine IAV sialidases showed a notably lower substrate affinity for Neu5Gc than human IAV sialidases. The findings suggest that equine IAV sialidase’s specificity for N-acetylneuraminic acid (Neu5Ac) perhaps contributes to its advantage during the early stages of infection and the process of progeny virus release from infected cells.
Investigating Viral Sialidase Substrate Specificity
- In this study, researchers studied the substrate specificity of the viral sialidase enzyme in both equine and human influenza A viruses (IAVs).
- The focus of the research was on the virus’s potential preference for N-glycolylneuraminic acid (Neu5Gc) and N-acetylneuraminic acid (Neu5Ac); these two types of molecular species of sialic acid normally found in glycoconjugates—complex sugars crucial to various biological processes.
- It was presumed that the progeny of equine IAV would be able to be released from the surface of an infected cell through clear removal of sialic acids- this hypothesis required an analysis of both artificial and natural Neu5Gc-conjugated substrates.
Findings on Equine Influenza A Virus Sialidase
- To the researchers’ surprise, the substrate affinity of equine IAV sialidases for Neu5Gc-conjugated substrates was significantly lower than that of human IAV sialidases.
- This finding led to a disagreement between the substrate specificity of equine IAV sialidases and their binding specificity to molecular species of sialic acid.
- It was found that the equine IAV sialidase showed a higher affinity for Neu5Ac instead of Neu5Gc which was contrary to the initial hypothesis of the study.
Implications of The Study
- The results suggest that the substrate specificity of equine IAV sialidase for Neu5Ac, rather than Neu5Gc, might be significant for giving the virus an advantage at the early infection stage.
- The specificity for Neu5Ac may also play a key role in the process through which progeny virus is released from the infected cells’ surface.
- This novel finding could pave the way for deeper understanding of the infection process of equine influenza A viruses and may lead to innovations in effective treatments or mitigation strategies.
Cite This Article
APA
Takahashi T, Unuma S, Kawagishi S, Kurebayashi Y, Takano M, Yoshino H, Minami A, Yamanaka T, Otsubo T, Ikeda K, Suzuki T.
(2016).
Substrate Specificity of Equine and Human Influenza A Virus Sialidase to Molecular Species of Sialic Acid.
Biol Pharm Bull, 39(10), 1728-1733.
https://doi.org/10.1248/bpb.b16-00345 Publication
Researcher Affiliations
- Department of Biochemistry, School of Pharmaceutical Sciences, University of Shizuoka and Global COE Program for Innovation in Human Health Sciences, Shizuoka.
MeSH Terms
- Animals
- Erythrocytes / drug effects
- Erythrocytes / metabolism
- HEK293 Cells
- Horses
- Humans
- Influenza A virus
- Neuraminic Acids / pharmacology
- Neuraminidase / metabolism
- Substrate Specificity
- Viral Proteins / metabolism
Citations
This article has been cited 1 times.- Singh RK, Dhama K, Karthik K, Khandia R, Munjal A, Khurana SK, Chakraborty S, Malik YS, Virmani N, Singh R, Tripathi BN, Munir M, van der Kolk JH. A Comprehensive Review on Equine Influenza Virus: Etiology, Epidemiology, Pathobiology, Advances in Developing Diagnostics, Vaccines, and Control Strategies.. Front Microbiol 2018;9:1941.
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