Hoefavidin: A dimeric bacterial avidin with a C-terminal binding tail

Avraham, Orly; Meir, Amit; Fish, Alexander; Bayer, Edward A.; Livnah, Oded

doi:10.1016/j.jsb.2015.06.020

Cited by 17 publications

(62 citation statements)

References 53 publications

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“…As a result, avidin analogues, such as hoefavidin and rhizavidin, which have dimeric arrangement, are of interest. [38] [39] Their tertiary topologies remain the same as avidin.…”

Section: Biochemical Insights Of Avidin Biotin and Analoguesmentioning

confidence: 99%

The principles and applications of avidin-based nanoparticles in drug delivery and diagnosis

Jain

Cheng

2017

Journal of Controlled Release

227

286

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Avidin-biotin interaction is one of the strongest non-covalent interactions in the nature. Avidin and its analogues have therefore been extensively utilized as probes and affinity matrices for a wide variety of applications in biochemical assays, diagnosis, affinity purification, and drug delivery. Recently, there has been a growing interest in exploring this non-covalent interaction in nanoscale drug delivery systems for pharmaceutical agents, including small molecules, proteins, vaccines, monoclonal antibodies, and nucleic acids. Particularly, the ease of fabrication without losing the chemical and biological properties of the coupled moieties makes the avidin-biotin system a versatile platform for nanotechnology. In addition, avidin-based nanoparticles have been investigated as diagnosis systems for various tumors and surface antigens. In this review, we will highlight the various fabrication principles and biomedical applications of avidin-based nanoparticles in drug delivery and diagnosis. The structures and biochemical properties of avidin, biotin and their respective analogues will also be discussed.

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“…As a result, avidin analogues, such as hoefavidin and rhizavidin, which have dimeric arrangement, are of interest. [38] [39] Their tertiary topologies remain the same as avidin.…”

Section: Biochemical Insights Of Avidin Biotin and Analoguesmentioning

confidence: 99%

The principles and applications of avidin-based nanoparticles in drug delivery and diagnosis

Jain

Cheng

2017

Journal of Controlled Release

227

286

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“…A breakthrough in this context was the discovery of high‐affinity dimeric avidins from bacterial sources, where the valency is 2 rather than 4 although the high affinity towards biotin is maintained . These include bacterial avidin‐like proteins from Rhizobium etli , (rhizavidin), Shewanella denitrificans (shwanavidin) and Hoeflea phototrophica DFL‐43 (hoefavidin) .…”

Section: Introductionmentioning

confidence: 99%

“…For hoefavidin, however, the oligomeric configuration is different, whereby four dimers assemble to form a cylindrical octamer (Fig. B right) . In the respective biotin complexes, the crystal packing is more diverse with limited indications of higher oligomeric states.…”

Section: Introductionmentioning

confidence: 99%

Crystal structure of afifavidin reveals common features of molecular assemblage in the bacterial dimeric avidins

2018

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The subfamily of bacterial dimeric avidins is being extended through the discovery of additional members originating from diverse sources. All of these newly discovered dimeric avidin forms exhibit high affinity towards biotin, despite their lack of critical Trp in the classical tetrameric forms. The common feature of forming cylinder‐like multimers (hexamers and octamers) seems to be more than a random occurrence, which generally characterizes their apo forms in the crystalline state and also in some cases in solution. Afifavidin from the Gram‐negative α‐proteobacterium Afifella pfennigii is the fourth member of the subfamily of dimers, which, in the intact apo form, also congregates into octamers both in the solution and in the crystalline state, whereby the C‐terminal extended segments stretch into the biotin‐binding sites of adjacent non‐canonical monomers. The intact apo afifavidin molecule self‐assembles into toroid‐shaped nanostructures that dissociate into the inherent dimers upon binding biotin. On removal of the C‐terminal regions, the short‐form of afifavidin forms dimers both in the solution and in the crystalline states. The high affinity of the dimeric forms of afifavidin towards biotin is maintained, due to the conserved disulfide bridge between L3,4 and L5,6 and the presence of Phe50 in L3,4 that compensate for the lack of the critical Trp in the tetrameric avidins. These cyclic multimeric‐avidin assemblies may be exploited in the future to further diversify biotin‐based nanotechnology or to serve as building blocks in the construction of bio‐inspired materials. Database Structural data are available in the PDB databases under the accession numbers: http://www.rcsb.org/pdb/search/structidSearch.do?structureId=6HDV, http://www.rcsb.org/pdb/search/structidSearch.do?structureId=6HDS, http://www.rcsb.org/pdb/search/structidSearch.do?structureId=6HDT.

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“…In bradavidin, however, cysteine Cys39 of the L3,4 loop is located one residue earlier in the sequence, as reported recently by Avraham et al (2015) for hoefavidin [21]. Thus, Cys39 is not exactly structurally equivalent to Cys50 in rhizavidin, Cys45 in shwanavidin, Cys57 in hoefavidin and Cyss44 in bradavidin II, whereas the other cysteine of the disulfide bond within the L5,6 loop, Cys69 in bradavidin, is conserved despite the fact that the conformation of the L5,6 loop varies within these proteins.…”

Section: Resultsmentioning

confidence: 61%

“…However, certain Avds, such as bradavidin [32] and streptavidin [16], and the recently discovered hoefavidin [21], are known to bind ligands other than biotin, i . e .…”

Section: Discussionmentioning

confidence: 99%

Structural characterization of core-bradavidin in complex with biotin

et al. 2017

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Bradavidin is a tetrameric biotin-binding protein similar to chicken avidin and bacterial streptavidin, and was originally cloned from the nitrogen-fixing bacteria Bradyrhizobium diazoefficiens. We have previously reported the crystal structure of the full-length, wild-type (wt) bradavidin with 138 amino acids, where the C-terminal residues Gly129-Lys138 (“Brad-tag”) act as an intrinsic ligand (i.e. Gly129-Lys138 bind into the biotin-binding site of an adjacent subunit within the same tetramer) and has potential as an affinity tag for biotechnological purposes. Here, the X-ray structure of core-bradavidin lacking the C-terminal residues Gly114-Lys138, and hence missing the Brad-tag, was crystallized in complex with biotin at 1.60 Å resolution [PDB:4BBO]. We also report a homology model of rhodavidin, an avidin-like protein from Rhodopseudomonas palustris, and of an avidin-like protein from Bradyrhizobium sp. Ai1a-2, both of which have the Brad-tag sequence at their C-terminus. Moreover, core-bradavidin V1, an engineered variant of the original core-bradavidin, was also expressed at high levels in E. coli, as well as a double mutant (Cys39Ala and Cys69Ala) of core-bradavidin (CC mutant). Our data help us to further engineer the core-bradavidin–Brad-tag pair for biotechnological assays and chemical biology applications, and provide deeper insight into the biotin-binding mode of bradavidin.

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Hoefavidin: A dimeric bacterial avidin with a C-terminal binding tail

Cited by 17 publications

References 53 publications

The principles and applications of avidin-based nanoparticles in drug delivery and diagnosis

The principles and applications of avidin-based nanoparticles in drug delivery and diagnosis

Crystal structure of afifavidin reveals common features of molecular assemblage in the bacterial dimeric avidins

Structural characterization of core-bradavidin in complex with biotin

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