Solar-driven interfacial evaporation (SIE) is a sustainable and efficient technology for producing clean water, which offers a promising application in seawater desalination and wastewater treatment. In this review, the latest...

Epitopes serve an important role in influenza infection. It may be useful to screen universal influenza virus vaccines, analyzing the epitopes of multiple subtypes of the hemagglutinin (HA) protein. A total of 40 monoclonal antibodies (mAbs) previously obtained from flu virus HA antigens (development and characterization of 40 mAbs generated using H1N1 influenza virus split vaccines were previously published) were used to detect and classify mAbs into distinct flu virus sub-categories using the ELISA method. Following this, the common continuous amino acid sequences were identified by multiple sequence alignment analysis with the GenBank database and DNAMAN software, for use in predicting the epitopes of the HA protein. Synthesized peptides of these common sequences were prepared, and used to verify and determine the predicted linear epitopes through localization and distribution analyses. With these methods, nine HA linear epitopes distributed among different strains of influenza virus were identified, which included three from influenza A, four from 2009 H1N1 and seasonal influenza, and two from H1. The present study showed that considering a combination of the antigen-antibody reaction specificity, variation in the influenza virus HA protein and linear epitopes may present a useful approach for designing effective multi-epitope vaccines. Furthermore, the study aimed to clarify the cause and pathogenic mechanism of influenza virus HA-induced flu, and presents a novel idea for identifying the epitopes of other pathogenic microorganisms.

Epidemiological studies have documented that the incidence of human type 1 diabetes was significantly increased after H1N1 epidemic. However, a direct link between human type 1 diabetes and virus infection remains elusive. We generated 84 clones of murine monoclonal antibodies against the H1N1, and carried out immunohistochemistry in normal human tissue microarray. The results showed that two clones specifically cross‐reacted with human α‐cells of pancreatic islets. Reverse transcription polymerase chain reaction and deoxyribonucleic acid sequencing showed that the amino acid sequences of light and heavy chains of these clones were different. Importantly, the expression profiles of two monoclonal antibodies were individual different. For the first time, we provide direct evidence that monoclonal antibodies against H1N1 can cross‐react with human pancreas α‐cells, another source of β‐cells, suggesting α‐cells might be a novel target to be investigated in diabetes research.

Influenza is the most common infectious disease and is caused by influenza A virus (IAV) infection. Hemagglutinin (HA) is an important viral protein of influenza A and is a major component of current IAV vaccines. The side effects associated with IAV vaccination are well studied; however, the HA‑induced immunopathological changes have remained largely elusive. The primary objective of the present study was to determine the tissue cross‑reactive epitopes of HA proteins. Monoclonal antibodies (McAbs) were generated according to traditional methods using purified HA proteins from influenza vaccine lysates. The specificity of these McAbs was analyzed using western blot analysis and ELISA. Human tissue microarrays were employed for immunohistochemical staining to screen these McAbs. Rat brain tissues were subjected to immunohistochemical staining and electron microscopy to demonstrate the subcellular localization of antibodies targeting specific antigens. A total of 67 hybridoma cell lines positive for McAb against HA antigen were obtained. Three cross‑reactive McAbs (H1‑13, H1‑15 and A1‑10) were discovered through tissue screening. Based on the 3 cross‑reactive McAbs and the amino acid sequence of HA, the presence of two broadly cross‑reactive HA epitopes, 194‑WGIHH‑198 and 365‑WYGYHH‑370, was assumed. McAbs against these synthetic epitope peptides were obtained. They reacted with porphyrin ring‑containing molecules, including hemoglobin (Hb) and protoporphyrin, and with numerous types of normal tissue. In conclusion, the present study identified two broadly cross‑reactive epitopes on HA (194‑WGIHH‑198 and 365‑WYGYHH‑370). Antibodies against these epitopes react with Hb and numerous types of important normal tissues/organs. These newly identified cross‑reactive epitopes from IAV HA may provide crucial information for influenza research.

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.