Generation of a recombinant chickenized monoclonal antibody against the neuraminidase of H9N2 avian influenza virus

Wang, Fei; Wang, Yajuan; Wan, Zhimin; Shao, Hongxia; Qian, Kun; Ye, Jianqiang; Qin, Aijian

doi:10.1186/s13568-020-01086-4

Cited by 7 publications

(5 citation statements)

References 26 publications

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“…We previously reported a mAb 1G8 against NA of H9N2 AIV, which possesses NI activity ( Wan et al, 2016 ; Wang et al, 2020 ). We now further identified that mAb 1G8 cannot only cross-react with NAs of H9N2 AIV and H3N2 HSIV but also have NI activity to them in NI assays.…”

Section: Discussionmentioning

confidence: 99%

A Cross-Reactive Monoclonal Antibody Against Neuraminidases of Both H9N2 and H3N2 Influenza Viruses Shows Protection in Mice Challenging Models

Wang

Wan

et al. 2021

Front. Microbiol.

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Neuraminidases (NAs) of H9N2 avian influenza virus (AIV) and H3N2 human seasonal influenza virus (HSIV) share similar antigenic structures. However, there are few reports on epitopes shared by these two NAs. We previously reported a monoclonal antibody (mAb) 1G8 against the NA of H9N2 AIV with neuraminidase inhibition (NI) ability. In this study, 1G8 was shown to cross-react with and inhibit the NA of H3N2 HSIV. In a passive transfer experiment, 1G8 provided protection to mice challenged with rescued H1N2 viruses carrying H9N2 NA or H3N2 NA. Mutation at amino acid position 199 was also selected and proved to be crucial for H3N2 HSIV to escape from mAb 1G8. Moreover, we found that residue 199 contributed to inducing broad protective antibodies without the influence of the N-linked glycosylation at amino acid position 200 in NAs. Residues as residue 199, which are not shielded by glycosylation modification, would form ideal epitopes for developing universal vaccine and protective antibodies.

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Section: Discussionmentioning

confidence: 99%

A Cross-Reactive Monoclonal Antibody Against Neuraminidases of Both H9N2 and H3N2 Influenza Viruses Shows Protection in Mice Challenging Models

Wang

Wan

et al. 2021

Front. Microbiol.

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“…However, components in raw sera have anti-NA properties that result in inhibition of NA activity. The ELLA is used to measure antibody-mediated NA inhibition for cleaving a large substrate, and has been used to assess the effectiveness of NA-containing vaccines and anti-NA antibodies (29)(30)(31)(32).…”

Section: Discussionmentioning

confidence: 99%

Inherent Serum Inhibition of Influenza Virus Neuraminidases

Skarlupka

Ross

2021

Front. Vet. Sci.

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Influenza virus vaccines have been designed for human and veterinary medicine. The development for broadly protective influenza virus vaccines has propelled the vaccine field to investigate and include neuraminidase (NA) components into new vaccine formulations. The antibody-mediated protection induced by NA vaccines is quantified by inhibition of sialic acid cleavage. Non-immune inhibitors against influenza viruses naturally occur in varying proportions in sera from different species. In this brief report, the inherent ability of raw animal sera to inhibit a panel of influenza virus NA was determined. Raw sera from the same species inhibited more than 50% of influenza viruses tested from four different subtypes, but the breadth of inhibiting NA activity depended on the source of sera. Furthermore, different influenza viruses were inhibited by different sources of sera. Overall, additional studies are needed to ensure that scientific methods are consistent across studies in order to compare NA inhibition results. Through future investigation into the differences between sera from different animal species and how they influence NA inhibition assays, there can be effective development of a broadly protective influenza virus vaccines for veterinary and human use.

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“…Allantoic fluid of each virus was harvested at 120 h post-inoculation and stored at −70°C. The pCAGGS plasmid, containing NA gene sequence of a wild-type (WT) A/Chicken/Jiangsu/XXM/1999 (XXM) H9N2 virus, was constructed, as previously reported [ 23 ].…”

Section: Methodsmentioning

confidence: 99%

Identification of key residues involved in the neuraminidase antigenic variation of H9N2 influenza virus

Wang

et al. 2021

Emerging Microbes & Infections

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Influenza A H9N2 virus causes economic loss to the poultry industry and has likely contributed to the genesis of H5N1 and H7N9 viruses. The neuraminidase (NA) of H9N2 virus, like haemagglutinin, is under antibody selective pressure and may undergo antigenic change; however, its antigenic structure remains to be elucidated. In this study, we used monoclonal antibodies (mAbs) to probe the H9N2 viral NA residues that are key for antibody binding/inhibition. These mAbs fell into three groups based on their binding/inhibition of the NA of H9N2 viruses isolated during 1999–2019: group I only bounded the NA of the early 2000 H9N2 viruses but possessed no neutralizing ability, group II bounded and inhibited the NA of H9N2 viruses isolated before 2012, and group III reacted with most or all tested H9N2 viruses. We showed that NA residue 356 is key for the recognition by group I mAbs, residues 344, 368, 369, and 400 are key for the binding/inhibition of NA by group II antibodies, whereas residues 248, 253, and the 125/296 combination are key for neutralizing antibodies in group III. Our findings highlighted NA antigenic change of the circulating H9N2 viruses, and provided data for a more complete picture of the antigenic structure of H9N2 viral NA.

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Generation of a recombinant chickenized monoclonal antibody against the neuraminidase of H9N2 avian influenza virus

Cited by 7 publications

References 26 publications

A Cross-Reactive Monoclonal Antibody Against Neuraminidases of Both H9N2 and H3N2 Influenza Viruses Shows Protection in Mice Challenging Models

A Cross-Reactive Monoclonal Antibody Against Neuraminidases of Both H9N2 and H3N2 Influenza Viruses Shows Protection in Mice Challenging Models

Inherent Serum Inhibition of Influenza Virus Neuraminidases

Identification of key residues involved in the neuraminidase antigenic variation of H9N2 influenza virus

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