Preparation and characterization of a Llama VHH-hFc chimeric antibody recognizing conserved neutralization epitope of H5N1 hemagglutinin with high affinity.

Lingyan Liu, Liliang Xia, Biao Wu, Ying Wang, Jie Xu

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Article in Archives of microbiology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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Lingyan LiuDepartment of Clinical Laboratory, Shanghai Ninth People's Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai, 200011, China.

Liliang XiaShanghai-MOST Key Laboratory of Health and Disease Genomics, Chinese National Human Genome Center at Shanghai, Shanghai, 201203, China.

Biao WuShanghai-MOST Key Laboratory of Health and Disease Genomics, Chinese National Human Genome Center at Shanghai, Shanghai, 201203, China.

Ying WangShanghai-MOST Key Laboratory of Health and Disease Genomics, Chinese National Human Genome Center at Shanghai, Shanghai, 201203, China.

Jie XuDepartment of Infectious Disease, Shanghai Ninth People's Hospital, Shanghai Jiao Tong University School of Medicine, No. 639, Zhizaoju Road, Huangpu District, Shanghai, 200011, China. jxx328@sohu.com.

Funding

National Key Research and Development Program of China 2021YF2301500Shanghai Municipal Optimization Program for Hospital Clinical Management SHDC22021207Shanghai Program for Outstanding Medical Academic Leader 2022LJ016the Fundamental Research Funds for the Central Universities YG2023ZD02

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Abstract

Highly pathogenic avian influenza (HPAI) H5N1 virus poses a continuing global public health threat due to its outbreaks in poultry farms and zoonotic transmission from birds to humans. In the quest of effective therapeutics against H5N1 infection, antibodies with broad neutralizing activity have attracted significant attention. In this study, we employed a phage display technique to select and identify VHH antibodies with specific neutralizing activity against H5N1 hemagglutinin (HA) from an immune llama-derived antibody library. Subsequently, we prepared fusions of VHH10 antibody with human Fc fragment. The chimeric antibody VHH10-hFc was characterized and evaluated for its specificity, binding affinity, serum persistence and antigen recognition epitope. Following purification from 293 F cell cultures, VHH10-hFc chimeric antibody retained its specificity to H5N1 HA. Its antigen-binding affinity was enhanced by up to 130-fold, and its serum persistence was extended by up to 170-fold compared to VHH10. The VHH10-hFc chimeric antibody demonstrated high affinity, excellent thermal stability, and broad reactivity against H5N1 HA in clades 0, 1, 2, and 4. Through epitope mapping, we identified a conformational epitope consisting amino acid residues at positions Q187, K189, L190, Y191, N193, T215, S217 and N220 located on the top region of HA, which was specific and conserved epitopes among H5N1 strains. Consequently, VHH10-hFc, with great specificity, high affinity, prolonged serum persistence and good thermal stability, recognizes a conserved neutralization epitope on the globular head of H5N1 HA, indicating great potential in therapeutic strategies against H5N1 infection.

Indexed as

Antibodies, NeutralizingAntibodies, ViralCamelids, New WorldEpitopesHemagglutinin Glycoproteins, Influenza VirusInfluenza A Virus, H5N1 SubtypeSingle-Domain AntibodiesAnimalsAntibody AffinityEpitope MappingHumansInfluenza in BirdsPeptide LibraryAntibodies, NeutralizingAntibodies, ViralEpitopesHemagglutinin Glycoproteins, Influenza VirusPeptide LibrarySingle-Domain AntibodiesChimeric antibodyConserved neutralization epitopeH5N1 hemagglutininVHH antibody

Identifiers

PMID40920240

DOI10.1007/s00203-025-04460-7

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.