Glycan-dependent chikungunya viral infection divulged by antiviral activity of NAG specific chi-like lectin

Ramanjit Kaur, Neetu, Rajat Mudgal, Joyce Jose, Pravindra Kumar, Shailly Tomar

Research output: Contribution to journalArticle

5 Scopus citations

Abstract

Highly pathogenic alphaviruses display complex glycans on their surface. These glycans play a crucial role in viral pathogenesis by facilitating glycan-host interaction during viral entry which can be targeted. Various studies have reported antiviral activity of lectins that bind to the glycans present on the surface of enveloped viruses. This study evaluates the antiviral potential of a chitinase (chi)-like lectin from Tamarind (TCLL) having specificity for N-acetylglucosamine (NAG). Thus, TCLL might bind to N-glycan rich surface of alphavirus and inhibit the entry of virus into the host cells. The direct treatment of TCLL with virus reduced the virus infection. Remarkably, the addition of NAG to TCLL abolished antiviral activity confirming that NAG binding property of TCLL is accountable for its antiviral activity. Further, an ELISA assay confirmed the binding of TCLL to alphaviruses. Taken together, this study will prove to be beneficial in developing lectin therapeutics targeting alphavirus glycan.

Original languageEnglish (US)
Pages (from-to)91-98
Number of pages8
JournalVirology
Volume526
DOIs
StatePublished - Jan 2 2019

All Science Journal Classification (ASJC) codes

  • Virology

Fingerprint Dive into the research topics of 'Glycan-dependent chikungunya viral infection divulged by antiviral activity of NAG specific chi-like lectin'. Together they form a unique fingerprint.

Cite this