tetano
Editor, Senior Moderator
Immunity
. 2024 May 29:S1074-7613(24)00253-X.
doi: 10.1016/j.immuni.2024.05.002. Online ahead of print. Isolation of human antibodies against influenza B neuraminidase and mechanisms of protection at the airway interface
Rachael M Wolters[SUP] 1 [/SUP], James A Ferguson[SUP] 2 [/SUP], Ivette A Nuñez[SUP] 3 [/SUP], Elaine E Chen[SUP] 1 [/SUP], Ty Sornberger[SUP] 1 [/SUP], Luke Myers[SUP] 3 [/SUP], Svearike Oeverdieck[SUP] 2 [/SUP], Sai Sundar Rajan Raghavan[SUP] 2 [/SUP], Chandrahaas Kona[SUP] 3 [/SUP], Laura S Handal[SUP] 3 [/SUP], Trevor E Esilu[SUP] 4 [/SUP], Edgar Davidson[SUP] 4 [/SUP], Benjamin J Doranz[SUP] 4 [/SUP], Taylor B Engdahl[SUP] 1 [/SUP], Nurgun Kose[SUP] 3 [/SUP], Lauren E Williamson[SUP] 5 [/SUP], C Buddy Creech[SUP] 6 [/SUP], Katherine N Gibson-Corley[SUP] 7 [/SUP], Andrew B Ward[SUP] 8 [/SUP], James E Crowe Jr[SUP] 9 [/SUP]
Affiliations
Influenza B viruses (IBVs) comprise a substantial portion of the circulating seasonal human influenza viruses. Here, we describe the isolation of human monoclonal antibodies (mAbs) that recognized the IBV neuraminidase (NA) glycoprotein from an individual following seasonal vaccination. Competition-binding experiments suggested the antibodies recognized two major antigenic sites. One group, which included mAb FluB-393, broadly inhibited IBV NA sialidase activity, protected prophylactically in vivo, and bound to the lateral corner of NA. The second group contained an active site mAb, FluB-400, that broadly inhibited IBV NA sialidase activity and virus replication in vitro in primary human respiratory epithelial cell cultures and protected against IBV in vivo when administered systemically or intranasally. Overall, the findings described here shape our mechanistic understanding of the human immune response to the IBV NA glycoprotein through the demonstration of two mAb delivery routes for protection against IBV and the identification of potential IBV therapeutic candidates.
Keywords: adaptive immunity; antibodies; human; influenza B; monoclonal; neuraminidase.
. 2024 May 29:S1074-7613(24)00253-X.
doi: 10.1016/j.immuni.2024.05.002. Online ahead of print. Isolation of human antibodies against influenza B neuraminidase and mechanisms of protection at the airway interface
Rachael M Wolters[SUP] 1 [/SUP], James A Ferguson[SUP] 2 [/SUP], Ivette A Nuñez[SUP] 3 [/SUP], Elaine E Chen[SUP] 1 [/SUP], Ty Sornberger[SUP] 1 [/SUP], Luke Myers[SUP] 3 [/SUP], Svearike Oeverdieck[SUP] 2 [/SUP], Sai Sundar Rajan Raghavan[SUP] 2 [/SUP], Chandrahaas Kona[SUP] 3 [/SUP], Laura S Handal[SUP] 3 [/SUP], Trevor E Esilu[SUP] 4 [/SUP], Edgar Davidson[SUP] 4 [/SUP], Benjamin J Doranz[SUP] 4 [/SUP], Taylor B Engdahl[SUP] 1 [/SUP], Nurgun Kose[SUP] 3 [/SUP], Lauren E Williamson[SUP] 5 [/SUP], C Buddy Creech[SUP] 6 [/SUP], Katherine N Gibson-Corley[SUP] 7 [/SUP], Andrew B Ward[SUP] 8 [/SUP], James E Crowe Jr[SUP] 9 [/SUP]
Affiliations
- PMID: 38823390
- DOI: 10.1016/j.immuni.2024.05.002
Influenza B viruses (IBVs) comprise a substantial portion of the circulating seasonal human influenza viruses. Here, we describe the isolation of human monoclonal antibodies (mAbs) that recognized the IBV neuraminidase (NA) glycoprotein from an individual following seasonal vaccination. Competition-binding experiments suggested the antibodies recognized two major antigenic sites. One group, which included mAb FluB-393, broadly inhibited IBV NA sialidase activity, protected prophylactically in vivo, and bound to the lateral corner of NA. The second group contained an active site mAb, FluB-400, that broadly inhibited IBV NA sialidase activity and virus replication in vitro in primary human respiratory epithelial cell cultures and protected against IBV in vivo when administered systemically or intranasally. Overall, the findings described here shape our mechanistic understanding of the human immune response to the IBV NA glycoprotein through the demonstration of two mAb delivery routes for protection against IBV and the identification of potential IBV therapeutic candidates.
Keywords: adaptive immunity; antibodies; human; influenza B; monoclonal; neuraminidase.