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 language | English (US) |
|---|---|
| Pages (from-to) | 91-98 |
| Number of pages | 8 |
| Journal | Virology |
| Volume | 526 |
| DOIs | |
| State | Published - Jan 2 2019 |
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All Science Journal Classification (ASJC) codes
- Virology
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Glycan-dependent chikungunya viral infection divulged by antiviral activity of NAG specific chi-like lectin. / Kaur, Ramanjit; Neetu; Mudgal, Rajat; Jose, Joyce; Kumar, Pravindra; Tomar, Shailly.
In: Virology, Vol. 526, 02.01.2019, p. 91-98.Research output: Contribution to journal › Article
TY - JOUR
T1 - Glycan-dependent chikungunya viral infection divulged by antiviral activity of NAG specific chi-like lectin
AU - Kaur, Ramanjit
AU - Neetu,
AU - Mudgal, Rajat
AU - Jose, Joyce
AU - Kumar, Pravindra
AU - Tomar, Shailly
PY - 2019/1/2
Y1 - 2019/1/2
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=85055353231&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=85055353231&partnerID=8YFLogxK
U2 - 10.1016/j.virol.2018.10.009
DO - 10.1016/j.virol.2018.10.009
M3 - Article
VL - 526
SP - 91
EP - 98
JO - Virology
JF - Virology
SN - 0042-6822
ER -