Indirect immobilization of recombinant proteins to a solid phase using the albumin binding domain of streptococcal protein G and immobilized albumin

Baumann, Sigrid; Grob, Philipp; Stuart, Fiona; Pertlik, Doris; Ackermann, Mathias; Suter, Mark

doi:10.1016/s0022-1759(98)00168-9

Cited by 18 publications

(11 citation statements)

References 26 publications

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“…Several biotechnology applications rely on the molecular recognition between two proteinaceous partners, providing valuable tools for selective and affinity‐driven complex formation. Such protein–protein interactions between defined binding partners are, for example, widely employed in various formats for protein recovery,1, 2 detection,3 and immobilization 4. Proteins capable of spontaneous dimerization or multimerization are frequently recruited as carrier fusion partners to obtain higher‐order presentation of fused passenger proteins through carrier protein‐mediated complex assembly.…”

Section: Introductionmentioning

confidence: 99%

Anti‐idiotypic protein domains selected from protein A‐based affibody libraries

et al. 2002

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Three pairs of small protein domains showing binding behavior in analogy with anti-idiotypic antibodies have been selected using phage display technology. From an affibody protein library constructed by combinatorial variegation of the Fc binding surface of the 58 residue staphylococcal protein A (SPA)-derived domain Z, affibody variants have been selected to the parental SPA scaffold and to two earlier identified SPA-derived affibodies. One selected affibody (Z(SPA-1)) was shown to recognize each of the five domains of wild-type SPA with dissociation constants (K(D)) in the micromolar range. The binding of the Z(SPA-1) affibody to its parental structure was shown to involve the Fc binding site of SPA, while the Fab-binding site was not involved. Similarly, affibodies showing anti-idiotypic binding characteristics were also obtained when affibodies previously selected for binding to Taq DNA polymerase and human IgA, respectively, were used as targets for selections. The potential applications for these types of affinity pairs were exemplified by one-step protein recovery using affinity chromatography employing the specific interactions between the respective protein pair members. These experiments included the purification of the Z(SPA-1) affibody from a total Escherichia coli cell lysate using protein A-Sepharose, suggesting that this protein A/antiprotein A affinity pair could provide a basis for novel affinity gene fusion systems. The use of this type of small, robust, and easily expressed anti-idiotypic affibody pair for affinity technology applications, including self-assembled protein networks, is discussed.

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Section: Introductionmentioning

confidence: 99%

Anti‐idiotypic protein domains selected from protein A‐based affibody libraries

et al. 2002

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“…This has been demonstrated for several formats involving different parts of the albuminbinding regions of SPG (Baumann et al 1998;Konig & Skerra 1998;Stahl et al 1989). Albumin-binding fusions have also found interesting applications in vivo for delivery of subunit vaccines or protein therapeutics (Nilsson, J. et al 1997b;Sjolander et al 1997;.…”

Section: The Albumin-binding Domains Derived From Spgmentioning

confidence: 90%

Purification Systems Based on Bacterial Surface Proteins

Boström¹,

Nilvebrant²,

Hober³

2012

Protein Purification

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“…This proline-rich region contains residues PMSPLR, a typical motif (PXXPX+) (+ is either arginine or lysine, X can be any aa) for class II SRC homology 3 (SH3) domains. SH3 domains are known to bind to proline-rich sequences containing a core PXXP motif flanked by a positively charged residue (Baumann et al, 1998;Raeder et al, 1998). SH3 domains comprise of about 60 residues and proteins containing SH3 domains typically play a role in signaling pathways involved in cell growth, differentiation and other regulatory functions (Zarrinpar et al, 2003).…”

Section: Orf3-encoded Protein Vp13mentioning

confidence: 99%

Molecular Biology and Infection of Hepatitis E Virus

2016

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Hepatitis E virus (HEV) is a viral pathogen transmitted primarily via fecal-oral route. In humans, HEV mainly causes acute hepatitis and is responsible for large outbreaks of hepatitis across the world. The case fatality rate of HEV-induced hepatitis ranges from 0.5 to 3% in young adults and up to 30% in infected pregnant women. HEV strains infecting humans are classified into four genotypes. HEV strains from genotypes 3 and 4 are zoonotic, whereas those from genotypes 1 and 2 have no known animal reservoirs. Recently, notable progress has been accomplished for better understanding of HEV biology and infection, such as chronic HEV infection, in vitro cell culture system, quasi-enveloped HEV virions, functions of the HEV proteins, mechanism of HEV antagonizing host innate immunity, HEV pathogenesis and vaccine development. However, further investigation on the cross-species HEV infection, host tropism, vaccine efficacy, and HEV-specific antiviral strategy is still needed. This review mainly focuses on molecular biology and infection of HEV and offers perspective new insight of this enigmatic virus.

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Indirect immobilization of recombinant proteins to a solid phase using the albumin binding domain of streptococcal protein G and immobilized albumin

Cited by 18 publications

References 26 publications

Anti‐idiotypic protein domains selected from protein A‐based affibody libraries

Anti‐idiotypic protein domains selected from protein A‐based affibody libraries

Purification Systems Based on Bacterial Surface Proteins

Molecular Biology and Infection of Hepatitis E Virus

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