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Antibody to S1 protein neutralizes SARS coronavirus.
2004 MAY 5 - (NewsRx.com & NewsRx.net) -- A human monoclonal antibody to S1 protein that blocks receptor association neutralized the severe acute respiratory syndrome (SARS) coronavirus.
"Effective prophylaxis and antiviral therapies are urgently needed in the event of reemergence of the highly contagious and often fatal severe acute respiratory syndrome (SARS) coronavirus (SARS-CoV) infection. We have identified eight recombinant human single-chain variable region fragments (scFvs) against the S1 domain of spike (S) protein of the SARS-CoV from two nonimmune human antibody libraries. One scFv 80R efficiently neutralized SARS-CoV and inhibited syncytia formation between cells expressing the S protein and those expressing the SARS-CoV receptor angiotensin-converting enzyme 2 (ACE2)," scientists in the United States report.
"Mapping of the 80R epitope showed it is located within the N-terminal 261-672 amino acids of S protein and is not glycosylation-dependent," stated Jianhua Sui and collaborators at the Dana-Farber Cancer Institute, Harvard Medical School, and the Centers for Disease Control and Prevention. "80R scFv competed with soluble ACE2 for association with the S1 domain and bound S1 with high affinity (equilibrium dissociation constant, K[subscript]d=32.3 nM). A human IgG1 form of 80R bound S1 with a 20-fold higher affinity of 1.59 nM comparable to that of ACE2 (K[subscript]d=1.70 nM), and neutralized virus 20-fold more ...
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Source: HighBeam Research, Antibody to S1 protein neutralizes SARS coronavirus.