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Protein-protein fusion catalyzed by sortase A.

ABSTRACT: Chimeric proteins boast widespread use in areas ranging from cell biology to drug delivery. Post-translational protein fusion using the bacterial transpeptidase sortase A provides an attractive alternative when traditional gene fusion fails. We describe use of this enzyme for in vitro protein ligation and report the successful fusion of 10 pairs of protein domains with preserved functionality--demonstrating the robust and facile nature of this reaction.

SUBMITTER: Levary DA

PROVIDER: S-EPMC3071835 | biostudies-literature | 2011

REPOSITORIES: biostudies-literature

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Protein-protein fusion catalyzed by sortase A.

Levary David A DA Parthasarathy Ranganath R Boder Eric T ET Ackerman Margaret E ME

PloS one 20110406 4

Chimeric proteins boast widespread use in areas ranging from cell biology to drug delivery. Post-translational protein fusion using the bacterial transpeptidase sortase A provides an attractive alternative when traditional gene fusion fails. We describe use of this enzyme for in vitro protein ligation and report the successful fusion of 10 pairs of protein domains with preserved functionality--demonstrating the robust and facile nature of this reaction. ...[more]

PMID: 21494692

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Receptor-directed chimeric toxins created by sortase-mediated protein fusion.

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