Elevated heparan sulfate affinity is associated with in vivo viral attenuation and diminished inflammatory responses in enterovirus A71 and chikungunya virus infections.
Absolute Event Rate: 0% vs 0%
ABSTRACT Heparan sulfate (HS), a ubiquitously expressed glycosaminoglycan, functions as an attachment and/or internalization factor for diverse RNA and DNA viruses. Its broad viral attachment capacity arises from structural heterogeneity in sulfation patterns. This review examines HS interactions in enterovirus A71 (EV‐A71), severe acute respiratory syndrome coronavirus 2 (SARS‐CoV‐2), and chikungunya virus (CHIKV), emphasizing shared features and virus‐specific distinctions. HS mediates viral attachment in all three, and additionally promotes SARS‐CoV‐2 internalization when host receptor angiotensin‐converting enzyme 2 is absent. Positively charged residues on the virion dictate HS affinity. High HS affinity enhances in vitro infectivity and plaque size in EV‐A71 and SARS‐CoV‐2, though evidence for CHIKV remains inconclusive. In vivo, elevated HS affinity is associated with viral attenuation and diminished inflammatory responses for both EV‐A71 and CHIKV; in EV‐A71 specifically, increased HS affinity further correlates with reduced capsid stability and heightened sensitivity to neutralizing antibodies. HS mimetics targeting viral‐HS interactions represent promising broad‐spectrum antivirals, particularly those advancing in clinical trials.
Theo et al. (Tue,) reported a other. Elevated heparan sulfate affinity is associated with in vivo viral attenuation and diminished inflammatory responses in enterovirus A71 and chikungunya virus infections.