Expression of V&lt;sub&gt;HH&lt;/sub&gt; Antibody Fragments in Saccharomyces cerevisiae

Vaart, J.M. van der

doi:10.1385/1-59259-240-6:359

Cited by 8 publications

(6 citation statements)

References 8 publications

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“…There is only one example of VHH production in filamentous fungi, which resulted in limited proteolytic degradation of the secreted product (Joosten et al 2005 ) because of the high levels of proteases secreted by filamentous fungi (Gerngross 2004 ). VHHs have also often been produced in the yeast Saccharomyces cerevisiae (Frenken et al 2000 ; Thomassen et al 2002 ; Van der Vaart 2002 ). VHH production by the favored yeast expression host Pichia pastoris was only recently described (Rahbarizadeh et al 2006 ).…”

Section: Production In Microorganismsmentioning

confidence: 99%

Properties, production, and applications of camelid single-domain antibody fragments

Harmsen

Haard

2007

Appl Microbiol Biotechnol

670

537

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Camelids produce functional antibodies devoid of light chains of which the single N-terminal domain is fully capable of antigen binding. These single-domain antibody fragments (VHHs or Nanobodies®) have several advantages for biotechnological applications. They are well expressed in microorganisms and have a high stability and solubility. Furthermore, they are well suited for construction of larger molecules and selection systems such as phage, yeast, or ribosome display. This minireview offers an overview of (1) their properties as compared to conventional antibodies, (2) their production in microorganisms, with a focus on yeasts, and (3) their therapeutic applications.

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Section: Production In Microorganismsmentioning

confidence: 99%

Properties, production, and applications of camelid single-domain antibody fragments

Harmsen

Haard

2007

Appl Microbiol Biotechnol

670

537

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“…Yeast expression systems are the common alternative that provides higher yields, sharing some of the features of both prokaryotic and eukaryotic cells. 38 The crucial advantages of yeast include the ability to provide proper posttranslational modification processes, fast growth, inexpensive medium, and safe pathogen-free production. S. cerevisiae was the first yeast strain used for the expression of VHH (with yields greater than 100 mg/mL).…”

Section: Nanobody Expression Systemsmentioning

confidence: 99%

Recent advances of nanobody applications in diagnosis and detection

Su,

Shi,

Huang

et al. 2023

MedComm – Biomaterials and Applications

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Nanobodies (Nbs) are the variable domain of heavy‐chain antibodies derived from the blood of camelids or sharks. Nanobodies are the smallest antibody fragment with intact antigen‐binding ability. Compared to conventional antibodies, nanobodies have unique properties such as small size, excellent stability and solubility, low immunogenicity, ability to recognize hidden epitopes, high tissue penetration, and industrialized production. More excitingly, the camelid‐specific amino acid sequences in the framework are mutated to their human heavy‐chain variable domain equivalent, which is humanized, to a wide range of applications. These superior characteristics make nanobody an ideal alternative to conventional antibody, showing excellent prospects for various applications in structural biology, molecular imaging, disease diagnosis and therapy, agricultural products, and environmental chemicals detection. With the continuous updating of theories and the rapid development of technology, the screening and expression methods of nanobodies are increasingly mature. Consequently, several technologies to identify and express nanobodies have been established, and various use cases have been described. In this review, we summarize recent advances in the discovery and production of novel nanobodies, and their use in detection and diagnosis platforms.

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“…Some extra refolding steps, such as co- or over-expression of chaperons, should be applied to overcome these limitations [ 68 ]. In contrast, S. cerevisiae is the best expression system for VHH [ 69 ], as organelles like ER or Golgi ensure proper disulfide bonds and glycosylation [ 70 ]. Because of these difficulties, E.coli remains the best host for scFv expression [ 10 , 64 , 68 ].…”

Section: Nanobody and Scfv In Propertiesmentioning

confidence: 99%

A comprehensive comparison between camelid nanobodies and single chain variable fragments

et al. 2021

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By the emergence of recombinant DNA technology, many antibody fragments have been developed devoid of undesired properties of natural immunoglobulins. Among them, camelid heavy-chain variable domains (VHHs) and single-chain variable fragments (scFvs) are the most favored ones. While scFv is used widely in various applications, camelid antibodies (VHHs) can serve as an alternative because of their superior chemical and physical properties such as higher solubility, stability, smaller size, and lower production cost. Here, these two counterparts are compared in structure and properties to identify which one is more suitable for each of their various therapeutic, diagnosis, and research applications.

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Expression of V<sub>HH</sub> Antibody Fragments in Saccharomyces cerevisiae

Cited by 8 publications

References 8 publications

Properties, production, and applications of camelid single-domain antibody fragments

Properties, production, and applications of camelid single-domain antibody fragments

Recent advances of nanobody applications in diagnosis and detection

A comprehensive comparison between camelid nanobodies and single chain variable fragments

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