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Broadly neutralizing antibodies from human survivors target a conserved site in the Ebola virus glycoprotein HR2-MPER region.

Nat Microbiol. 2018; 
FlyakAndrew I,KuzminaNatalia,MurinCharles D,BryanChristopher,DavidsonEdgar,GilchukPavlo,GulkaChristopher P,IlinykhPhilipp A,ShenXiaoli,HuangKai,RamanathanPalaniappan,TurnerHannah,FuscoMarnie L,LampleyRebecca,KoseNurgun,KingHannah,SapparapuGopal,DoranzBenjamin J,KsiazekThomas G,WrightDavid W,SaphireErica Ollmann,WardAndrew B,BukreyevAlexander,CroweJam
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Peptide Synthesis Polyclonal antibodies were purified using BDBV2p or SUDV2p peptides conjugated to iodoacetyl resin (polyclonal antibody service, GenScript).... The presence of antibodies bound to the antigen was determined using a mouse anti-rabbit IgG horseradish peroxidase conjugate (A01827-200, GenScript). Get A Quote

摘要

Ebola virus (EBOV) in humans causes a severe illness with high mortality rates. Several strategies have been developed in the past to treat EBOV infection, including the antibody cocktail ZMapp, which has been shown to be effective in nonhuman primate models of infection and has been used under compassionate-treatment protocols in humans . ZMapp is a mixture of three chimerized murine monoclonal antibodies (mAbs) that target EBOV-specific epitopes on the surface glycoprotein. However, ZMapp mAbs do not neutralize other species from the genus Ebolavirus, such as Bundibugyo virus (BDBV), Reston virus (RESTV) or Sudan virus (SUDV). Here, we describe three naturally occurring human cross-neutralizing ... More

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