期刊
ACS INFECTIOUS DISEASES
卷 2, 期 5, 页码 313-321出版社
AMER CHEMICAL SOC
DOI: 10.1021/acsinfecdis.6b00026
关键词
astrovirus; antibody; X-ray crystallography; mass spectrometry; protein sequencing; protein engineering
资金
- NIH Grant [K22 AI095369, R42 GM103362]
- NIH/ORIP Grant [S10OD010582]
- Office of Science, Office of Basic Energy Sciences, U.S. Department of Energy [DE-AC02-05CH11231]
Monoclonal-antibody (mAb) therapeutics targeting cancer, autoimmune diseases, inflammatory diseases, and infectious diseases are growing exponentially. Although numerous panels of mAbs targeting infectious disease agents have been developed, their progression into clinically useful mAbs is often hindered by the lack of sequence information and/or loss of hybridoma cells that produce them. Here we combine the power of crystallography and mass spectrometry to determine the amino acid sequence and glycosylation modification of the Fab fragment of a potent human astrovirus-neutralizing mAb. We used this information to engineer a recombinant antibody single-chain variable fragment that has the same specificity as the parent monoclonal antibody to bind to the astrovirus capsid protein. This antibody can now potentially be developed as a therapeutic and diagnostic agent.
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