AI Article Synopsis
- Researchers previously found that a specific protein fragment from a virus (spike protein of SARS coronavirus) can trigger the production of neutralizing antibodies in response to infection.
- In the current study, they developed monoclonal antibodies (MAbs) to identify the specific parts of this protein that antibodies bind to for neutralization.
- They discovered several key binding sites, two of which are located in the heptad repeat 2 (HR2) region, and confirmed that antibodies targeting these sites can effectively block the virus's ability to fuse with host cells.
Article Abstract
We have previously shown that an Escherichia coli-expressed, denatured spike (S) protein fragment of the severe acute respiratory coronavirus, containing residues 1029 to 1192 which include the heptad repeat 2 (HR2) domain, was able to induce neutralizing polyclonal antibodies (C. T. Keng, A. Zhang, S. Shen, K. M. Lip, B. C. Fielding, T. H. Tan, C. F. Chou, C. B. Loh, S. Wang, J. Fu, X. Yang, S. G. Lim, W. Hong, and Y. J. Tan, J. Virol. 79:3289-3296, 2005). In this study, monoclonal antibodies (MAbs) were raised against this fragment to identify the linear neutralizing epitopes in the functional domain and to investigate the mechanisms involved in neutralization. Eighteen hybridomas secreting the S protein-specific MAbs were obtained. Binding sites of these MAbs were mapped to four linear epitopes. Two of them were located within the HR2 region and two immediately upstream of the HR2 domain. MAbs targeting these epitopes showed in vitro neutralizing activities and were able to inhibit cell-cell membrane fusion. These results provide evidence of novel neutralizing epitopes that are located in the HR2 domain and the spacer region immediately upstream of the HR2 of the S protein.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1346840 | PMC |
| http://dx.doi.org/10.1128/JVI.80.2.941-950.2006 | DOI Listing |
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