2012
DOI: 10.1016/j.molimm.2012.03.015
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A novel disulfide-stabilized single-chain variable antibody fragment against rabies virus G protein with enhanced in vivo neutralizing potency

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Cited by 22 publications
(8 citation statements)
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“…The antibody variable domains can be engineered into small fragments ( Table 2), including scFvs and F[ab] molecules [76][77][78] which do not require production in costly eukaryotic expression systems. Several of these small antibody fragments have been investigated regarding their antiviral activities [79,80], including camelid VHH domains.…”
Section: Antibody Engineeringmentioning
confidence: 99%
“…The antibody variable domains can be engineered into small fragments ( Table 2), including scFvs and F[ab] molecules [76][77][78] which do not require production in costly eukaryotic expression systems. Several of these small antibody fragments have been investigated regarding their antiviral activities [79,80], including camelid VHH domains.…”
Section: Antibody Engineeringmentioning
confidence: 99%
“…reports that a bivalent disulfide‐stabilized Fv could bind to erbB2 with improved antigen‐binding activity compared to Fv. Duan et al . constructed a disulfide‐stabilized scFv against RV (ds‐FV57); the stability of ds‐FV57 was notably improved, and its neutralizing potency against RV infection was enhanced in vitro .…”
Section: Discussionmentioning
confidence: 99%
“…Owing to their several advantages, single chain antibodies could serve as useful tools for antibody-based therapies. Better penetration to target tissues because of the small size [16,40] has made scFvs more effective than antibodies in therapeutic applications especially when viral antigens are the targets [41,42].…”
Section: Discussionmentioning
confidence: 99%