Antibodies against H1N1 influenza virus hemagglutinin cross-react with prohibitin

Sun, Lijun; Li, Huijin; Sun, Jingying; Guo, Chunyan; Feng, Yangmeng; Li, Yan; Zhao, Xueqiang; Xie, Xin; Hu, Jun

doi:10.1016/j.bbrc.2019.03.188

Cited by 4 publications

(6 citation statements)

References 22 publications

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“…Although the protein expressed in the bacterial system cannot simulate the natural protein in nuclear organisms, the current research field mostly uses prokaryotic expression methods to identify heterophilic antigens. Sun et al (13) used a prokaryotic expression method to report that the anti-influenza virus H1-50mAb recognizes target antigen inhibin on pancreatic islet cells. Furthermore, an article published in Nature Medicine confirmed that an antibody produced by human T lymphotropic virus type 1 (HTLV-1) infection reacts with hnRNPA1 to cause myelopathy/tropical paraplegia (HAM/TSP) by prokaryotic expression (14).…”

Section: Discussionmentioning

confidence: 99%

“…Although hnRNP is widely distributed in various cells and tissues of different species, H1-84mAb specifically binds to brain tissue. Furthermore, Sun et al (13) reported that anti-influenza virus H1-50mAb recognises a target antigen on islet cells, which has been revealed to be prohibitin. Prohibitin is an antiproliferative protein that is widely distributed in various cell types in different species, and serves an important regulatory role in cell metabolism, growth, differentiation, senescence and apoptosis (24).…”

Section: Discussionmentioning

confidence: 99%

“…The present study compared the similarity between the HA of influenza virus and the Gly-rich domain of hnRNPA1 and hnRNPA2/B1; and they were found to have no homologous sequences. Sun et al (13) revealed that an influenza virus mAb (H1-50) cross-reacts with islet cells, but there is no homologous sequence between HA and prohibitin. Previous studies (14,25) revealed that an antibody produced by human T lymphotropic virus type 1 infection reacts with hnRNPA1 to cause myelopathy/tropical paraplegia.…”

Section: Discussionmentioning

confidence: 99%

“…As previously described ( 13 ), total protein was extracted from rat brain tissues using RIPA lysis buffer, and lysed on ice or at 4°C for 30 min. The supernatant was collected following centrifugation at 12,000 × g for 30 min at 4°C.…”

Section: Methodsmentioning

confidence: 99%

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Monoclonal antibody against H1N1 influenza virus hemagglutinin cross reacts with hnRNPA1 and hnRNPA2/B1

Guo

Sun

Hao³

et al. 2020

Mol Med Rep

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Following influenza A vaccination, certain individuals exhibit adverse reactions in the nervous system, which causes a problem with the safety of the influenza A vaccine. However, to the best of our knowledge, the underlying mechanism of this is unknown. The present study revealed that a monoclonal antibody (H1-84mAb) against the H1N1 influenza virus hemagglutinin (HA) protein cross-reacted with an antigen from brain tissue. Total brain tissue protein was immunoprecipitated with this cross-reactive antibody, and mass spectrometry revealed that the bound antigens were heterogeneous nuclear ribonucleoprotein (hnRNP) A1 and hnRNPA2/B1. Subsequently, the two proteins were expressed in bacteria and it was demonstrated that H1-84mAb bound to hnRNPA1 and hnRNPA2/B1. These two proteins were expressed in three segments and the cross-reactivity of H1-84mAb with the glycine (Gly)-rich domains of hnRNPA1 (195aa-320aa) and hnRNPA2/B1 (202aa-349aa) was determined using ELISA blocking experiments. It was concluded that the Gly-rich domains of these two proteins are heterophilic antigens that cross-react with influenza virus HA. The association between the heterophilic antigen Gly-rich domains and the safety of influenza A vaccines remains to be investigated.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

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Monoclonal antibody against H1N1 influenza virus hemagglutinin cross reacts with hnRNPA1 and hnRNPA2/B1

Guo

Sun

Hao³

et al. 2020

Mol Med Rep

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“…Levin's use of the mimotope multipin peptide system identified the dominant epitope KHFRETEV in HTLV‐1, which does not correspond to any similar sequence or conformational epitopes on hnRNPA1 8 . Similarly, monoclonal antibodies (mAbs) of H1N1 influenza virus hemagglutinin (HA) have been found to interact with islet cell prohibition proteins without any homologous sequence or conformational epitopes with similar structures between HA and prohibition proteins 9 . In most cases, there is no homologous sequence or conformational epitopes with similar structure between autoantigens and microbial antigens, and this phenomenon remains unexplained.…”

Section: Introductionmentioning

confidence: 99%

Cross‐reaction mediated by distinct key amino acid combinations in the complementary‐determining region (CDR) of a monoclonal antibody

Guo,

Feng,

Xie

et al. 2024

Journal of Medical Virology

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In immunology, cross‐reaction between antigens and antibodies are commonly observed. Prior research has shown that various monoclonal antibodies (mAbs) can recognize a broad spectrum of epitopes related to influenza viruses. However, existing theories on cross‐reactions fall short in explaining the phenomena observed. This study explored the interaction characteristics of H1‐74 mAb with three peptides: two natural peptides, LVLWGIHHP and LPFQNI, derived from the hemagglutinin (HA) antigen of the H1N1 influenza virus, and one synthetic peptide, WPFQNY. Our findings indicate that the complementarity‐determining region (CDR) of H1‐74 mAb comprised five antigen‐binding sites, containing eight key amino acid residues from the light chain variable region and 16 from the heavy chain variable region. These critical residues formed distinct hydrophobic or hydrophilic clusters and functional groups within the binding sites, facilitating interaction with antigen epitopes through hydrogen bonding, salt bridge formation, and π–π stacking. The study revealed that the formation of the antibody molecule led to the creation of binding groups and small units in the CDR, allowing the antibody to attach to a variety of antigen epitopes through diverse combinations of these small units and functional groups. This unique ability of the antibody to bind with antigen epitopes provides a new molecular basis for explaining the phenomenon of antibody cross‐reaction.

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Identification of Heterophilic Epitopes of H1N1 Influenza Virus Hemagglutinin

et al. 2023

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Antibodies against H1N1 influenza virus hemagglutinin cross-react with prohibitin

Cited by 4 publications

References 22 publications

Monoclonal antibody against H1N1 influenza virus hemagglutinin cross reacts with hnRNPA1 and hnRNPA2/B1

Monoclonal antibody against H1N1 influenza virus hemagglutinin cross reacts with hnRNPA1 and hnRNPA2/B1

Cross‐reaction mediated by distinct key amino acid combinations in the complementary‐determining region (CDR) of a monoclonal antibody

Identification of Heterophilic Epitopes of H1N1 Influenza Virus Hemagglutinin

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