tetano
Editor, Senior Moderator
Mol Med Rep
. 2020 Sep 7.
doi: 10.3892/mmr.2020.11494. Online ahead of print.
Monoclonal antibody against H1N1 influenza virus hemagglutinin cross reacts with hnRNPA1 and hnRNPA2/B1
Chunyan Guo[SUP] 1 [/SUP], Lijun Sun[SUP] 1 [/SUP], Shuangping Hao[SUP] 2 [/SUP], Xiaoyan Huang[SUP] 1 [/SUP], Hanyu Hu[SUP] 3 [/SUP], Daoyan Liang[SUP] 1 [/SUP], Qing Feng[SUP] 1 [/SUP], Yan Li[SUP] 1 [/SUP], Yangmeng Feng[SUP] 1 [/SUP], Xin Xie[SUP] 4 [/SUP], Jun Hu[SUP] 1 [/SUP]
Affiliations
Abstract
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.
. 2020 Sep 7.
doi: 10.3892/mmr.2020.11494. Online ahead of print.
Monoclonal antibody against H1N1 influenza virus hemagglutinin cross reacts with hnRNPA1 and hnRNPA2/B1
Chunyan Guo[SUP] 1 [/SUP], Lijun Sun[SUP] 1 [/SUP], Shuangping Hao[SUP] 2 [/SUP], Xiaoyan Huang[SUP] 1 [/SUP], Hanyu Hu[SUP] 3 [/SUP], Daoyan Liang[SUP] 1 [/SUP], Qing Feng[SUP] 1 [/SUP], Yan Li[SUP] 1 [/SUP], Yangmeng Feng[SUP] 1 [/SUP], Xin Xie[SUP] 4 [/SUP], Jun Hu[SUP] 1 [/SUP]
Affiliations
- PMID: 32901845
- DOI: 10.3892/mmr.2020.11494
Abstract
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.