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Structure of a VHH isolated from a naive phage display library.

ABSTRACT: OBJECTIVE:To determine the X-ray structure and biophysical properties of a Camelid VHH isolated from a naïve phage display library. RESULTS:Single domain antibodies (VHH) derived from the unique immune system of the Camelidae family have gained traction as useful tools for biotechnology as well as a source of potentially novel therapeutics. Here we report the structure and biophysical characterization of a VHH originally isolated from a naïve camelid phage display library. VHH R419 has a melting temperate of 66 °C and was found to be a monomer in solution. The protein crystallized in space group P6522 and the structure was solved by molecular replacement to a resolution of 1.5 Å. The structure revealed a flat paratope with CDR loops that could be classified into existing canonical loop structures. A combination of high expression yield, stability and rapid crystallization might make R419 into a candidate scaffold for CDR grafting and homology modeling.

SUBMITTER: White B

PROVIDER: S-EPMC6425610 | biostudies-literature | 2019 Mar

REPOSITORIES: biostudies-literature

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Structure of a V<sub>H</sub>H isolated from a naïve phage display library.

White Brandy B Huh Ian I Brooks Cory L CL

BMC research notes 20190319 1

<h4>Objective</h4>To determine the X-ray structure and biophysical properties of a Camelid V<sub>H</sub>H isolated from a naïve phage display library.<h4>Results</h4>Single domain antibodies (V<sub>H</sub>H) derived from the unique immune system of the Camelidae family have gained traction as useful tools for biotechnology as well as a source of potentially novel therapeutics. Here we report the structure and biophysical characterization of a V<sub>H</sub>H originally isolated from a naïve camel ...[more]

PMID: 30890176

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Highly potent multivalent VHH antibodies against Chikungunya isolated from an alpaca naive phage display library.

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| S-EPMC9107221 | biostudies-literature

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