tetano
Editor, Senior Moderator
Carbohydr Res
. 2022 Jul 8;520:108631.
doi: 10.1016/j.carres.2022.108631. Online ahead of print.
Oseltamivir modified bovine serum albumin inhibits neuraminidase activity and accumulates virion particles to disturb influenza virus replication
Hai-Juan Qin[SUP] 1 [/SUP], Shuang Li[SUP] 2 [/SUP], Yu-Bo Zhu[SUP] 2 [/SUP], Yan-Bin Bao[SUP] 2 [/SUP], Qi Tang[SUP] 2 [/SUP], Wen-Bin Liu[SUP] 2 [/SUP], Ming Zhong[SUP] 3 [/SUP], YueTao Zhao[SUP] 4 [/SUP], Yang Yang[SUP] 5 [/SUP]
Affiliations
Abstract
The preparation of oseltamivir-bovine serum albumin conjugate (OS-BSA) for use as a multivalent influenza neuraminidase (NA) inhibitor is reported. Briefly, the oseltamivir azidohexyl ester was synthesized and covalently bound via an orthogonal attachment to bicyclononyne-modified BSA using copper-free click chemistry. Primary antiviral assays on NA protein and cellular levels showed that the synthetic multivalent OS-BSA conjugate was a more effective inhibitor than monomeric OS azidohexyl ester. Further investigation of the antiviral mechanism found that the prepared OS-BSA could not only be used as a multivalent NA inhibitor but also acted as an adsorbent for the aggregation of virion particles, contributing to the inhibition of the influenza viral replication cycle. Our findings provide insight into the antiviral mechanism of multivalent NA inhibitors and form a basis for the development of novel antiviral agents.
Keywords: Bovine serum albumin conjugate; Click chemistry; Multivalent neuraminidase inhibitor; Oseltamivir.
. 2022 Jul 8;520:108631.
doi: 10.1016/j.carres.2022.108631. Online ahead of print.
Oseltamivir modified bovine serum albumin inhibits neuraminidase activity and accumulates virion particles to disturb influenza virus replication
Hai-Juan Qin[SUP] 1 [/SUP], Shuang Li[SUP] 2 [/SUP], Yu-Bo Zhu[SUP] 2 [/SUP], Yan-Bin Bao[SUP] 2 [/SUP], Qi Tang[SUP] 2 [/SUP], Wen-Bin Liu[SUP] 2 [/SUP], Ming Zhong[SUP] 3 [/SUP], YueTao Zhao[SUP] 4 [/SUP], Yang Yang[SUP] 5 [/SUP]
Affiliations
- PMID: 35839640
- DOI: 10.1016/j.carres.2022.108631
Abstract
The preparation of oseltamivir-bovine serum albumin conjugate (OS-BSA) for use as a multivalent influenza neuraminidase (NA) inhibitor is reported. Briefly, the oseltamivir azidohexyl ester was synthesized and covalently bound via an orthogonal attachment to bicyclononyne-modified BSA using copper-free click chemistry. Primary antiviral assays on NA protein and cellular levels showed that the synthetic multivalent OS-BSA conjugate was a more effective inhibitor than monomeric OS azidohexyl ester. Further investigation of the antiviral mechanism found that the prepared OS-BSA could not only be used as a multivalent NA inhibitor but also acted as an adsorbent for the aggregation of virion particles, contributing to the inhibition of the influenza viral replication cycle. Our findings provide insight into the antiviral mechanism of multivalent NA inhibitors and form a basis for the development of novel antiviral agents.
Keywords: Bovine serum albumin conjugate; Click chemistry; Multivalent neuraminidase inhibitor; Oseltamivir.