Isolation of antigen-specific, disulphide-rich knob domain peptides from bovine antibodies. [PDF]
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 +3 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]
: 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 allosteric modulation of complement C5 by knob domain peptides [PDF]
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 +2 more sources
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 +3 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]
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 +2 more sources
Modular design of bi- and multi-specific knob domain fusions [PDF]
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 +2 more sources
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 +3 more sources
Comparative Molecular Dynamics Study of 19 Bovine Antibodies with Ultralong CDR H3 [PDF]
Background/Objectives: Cows produce antibodies with ultralong CDRH3 segments (ulCABs) that contain a disulfide-stabilized knob domain. This domain is connected to the globular core of the antibody by a β-strand stalk. In the crystal structures, the stalk
Olena Denysenko +2 more
doaj +2 more sources
The Knob Domain of the Fiber-1 Protein Affects the Replication of Fowl Adenovirus Serotype 4 [PDF]
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 +2 more sources
Insights into the molecular determinants of host specificity in Pseudomonas aeruginosa-infecting phages: a structural and functional analysis of tail fibre proteins [PDF]
Background Bacteriophages and bacteria frequently occupy the same ecological niches, driving complex and dynamic host–virus interactions. In Pseudomonas aeruginosa, phages from the Migulavirinae subfamily, tail fibre proteins (TFPs) are crucial to host ...
Aleksandra Zalewska +4 more
doaj +2 more sources

