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Tulane virus recognizes sialic acids as cellular receptors
Ming Tan1, Chao Wei2, Pengwei Huang2
11] Division of Infectious Diseases, Cincinnati Children's Hospital Medical Center, Cincinnati, OH [2] Department of Pediatrics, University of Cincinnati College of Medicine, Cincinnati, OH.
Scientific Reports
|July 7, 2015
Summary
Tulane virus (TV), a primate calicivirus, recognizes sialic acids (SAs) like human noroviruses (huNoVs). This discovery advances understanding of calicivirus-host interactions and TV
Area of Science:
- Virology
- Carbohydrate Chemistry
- Cell Biology
Background:
- Human noroviruses (huNoVs) infection studies are limited by the lack of effective cell culture models.
- Recent findings indicate huNoVs recognize sialic acids (SAs) and histo-blood group antigens (HBGAs).
Purpose of the Study:
- To investigate if Tulane virus (TV), a cultivable primate calicivirus, also interacts with SAs.
- To explore TV as a surrogate model for studying huNoV-host interactions involving multiple receptors.
Main Methods:
- Assessing TV virion binding to synthetic sialoglycoconjugates (SGCs).
- Evaluating the effect of neuraminidases and SA-binding lectins on TV infectivity in LLC-MK2 cells.
- Investigating the interaction of Maackia amurensis leukoagglutinin (MAL) with TV and LLC-MK2 cells.
Main Results:
- TV virions demonstrated binding to SGCs, indicating SA recognition.
- Enzymatic or lectin-based removal of SAs significantly inhibited TV infectivity.
- MAL, an α-2,3 linked SA-binding lectin, bound TV and LLC-MK2 cells, enhancing TV infectivity.
Conclusions:
- Tulane virus recognizes sialic acids, expanding the known host interactions for this calicivirus.
- TV serves as a valuable model for studying complex virus-host interactions, including those involving dual carbohydrate receptors like SAs and HBGAs.
- These findings offer new avenues for understanding calicivirus pathogenesis and developing antiviral strategies.
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