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Modular design of bi- and multi-specific knob domain fusions [PDF]

open access: yesFrontiers in Immunology
IntroductionThe therapeutic potential of bispecific antibodies is becoming widely recognised, with over a hundred formats already described. For many applications, enhanced tissue penetration is sought, so bispecifics with low molecular weight may offer ...
Mikhail Kuravsky   +5 more
doaj   +6 more sources

Isolation of antigen-specific, disulphide-rich knob domain peptides from bovine antibodies. [PDF]

open access: yesPLoS Biology, 2020
As a novel alternative to established surface display or combinatorial chemistry approaches for the discovery of therapeutic peptides, we present a method for the isolation of small, cysteine-rich domains from bovine antibody ultralong complementarity ...
Alex Macpherson   +9 more
doaj   +6 more sources

Precise location of three novel linear epitopes using the generated monoclonal antibodies against the Knob domain of FAdV-4 surface structural protein, fiber1 [PDF]

open access: yesFrontiers in Cellular and Infection Microbiology
BackgroundFowl adenovirus serotype 4 (FAdV-4) is the main pathogen of hepatitis-hydropericardium syndrome (HHS), which brings huge economic losses to the poultry industry worldwide.
Yongxiao Chai   +12 more
doaj   +6 more sources

The allosteric modulation of complement C5 by knob domain peptides [PDF]

open access: yeseLife, 2021
Bovines have evolved a subset of antibodies with ultra-long heavy chain complementarity determining regions that harbour cysteine-rich knob domains. To produce high-affinity peptides, we previously isolated autonomous 3–6 kDa knob domains from bovine ...
Alex Macpherson   +17 more
doaj   +9 more sources

Knob domain of Fiber 2 protein provides full protection against fowl adenovirus serotype 4 [PDF]

open access: yesVirus Research, 2023
Highly pathogenic fowl adenovirus serotype 4 (FAdV-4) is an acute infectious disease with severe economic impact, causing chicken hepatitis hydropericardium syndrome (HHS) and high mortality. In the present study, we evaluated the immunogenicity of the recombinant Fiber2-knob protein (F2-Knob) as an FAdV-4 candidate subunit vaccine in 14-day-old SPF ...
Yapeng Song
exaly   +4 more sources

An Antibody with a Variable‐Region Coiled‐Coil “Knob” Domain [PDF]

open access: yesAngewandte Chemie - International Edition, 2014
AbstractThe X‐ray crystal structure of a bovine antibody (BLV1H12) revealed a unique structure in its ultralong heavy chain complementarity determining region 3 (CDR3H) that folds into a solvent‐exposed β‐strand “stalk” fused to a disulfide crosslinked “knob” domain.
Yong Zhang   +2 more
exaly   +5 more sources

A novel subunit vaccine based on Fiber1/2 knob domain provides full protection against fowl adenovirus serotype 4 and induces stronger immune responses than a Fiber2 subunit vaccine [PDF]

open access: yesPoultry Science
: Outbreaks of hepatitis-hydropericardium syndrome (HHS) caused by fowl adenovirus serotype 4 (FAdV-4) have resulted in huge economic losses to the poultry industry in China since 2015.
Shuaifeng Liu   +6 more
doaj   +4 more sources

The Knob Domain of the Fiber-1 Protein Affects the Replication of Fowl Adenovirus Serotype 4 [PDF]

open access: yesMicroorganisms
Fowl adenovirus serotype 4 (FAdV-4) outbreaks have caused significant economic losses in the Chinese poultry industry since 2015. The relationships among viral structural proteins in infected hosts are relatively unknown. To explore the role of different
Xiaofeng Li   +8 more
doaj   +4 more sources

Serum albumin binding knob domains engineered within a VH framework III bispecific antibody format and as chimeric peptides

open access: yesFrontiers in Immunology, 2023
BackgroundSerum albumin binding is an established mechanism to extend the serum half-life of antibody fragments and peptides. The cysteine rich knob domains, isolated from bovine antibody ultralong CDRH3, are the smallest single chain antibody fragments ...
Ralph Adams   +18 more
doaj   +5 more sources

The proximity of the N- and C- termini of bovine knob domains enable engineering of target specificity into polypeptide chains

open access: yesmAbs, 2022
Cysteine-rich knob domains can be isolated from the ultralong heavy-chain complementarity-determining region (CDR) 3, which are unique to a subset of bovine antibodies, to create antibody fragments of ~4 kDa.
Alice Hawkins   +9 more
doaj   +5 more sources

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