title: Secretion of circular proteins using sortase.
abstract: Circular proteins occur naturally and have been found in microorganisms, plants, and eukaryotes where they are commonly involved in host defense. Properties of circular proteins include enhanced resistance to exoproteases, increased thermostability, longer life spans, and increased activity. Using an enzymatic approach based on the bacterial sortase A (SrtA) transpeptidase, N- and C-termini of conventional linear proteins can be linked resulting in a circular protein. Circularization of bioengineered linear substrate proteins can indeed confer the desirable properties associated with circular proteins. Here, we describe how cells can be manipulated to secrete circularized proteins for substrates of choice via sortase-mediated circularization in the lumen of the endoplasmic reticulum.
authors.affiliation: Department of Infectious Diseases & Immunology, Utrecht University, Utrecht, The Netherlands.
authors.forename: Karin
authors.initials: K
authors.lastname: Strijbis
authors.forename: Hidde L
authors.initials: HL
authors.lastname: Ploegh
mesh_terms: D019881:Aminoacyltransferases / Q000235:genetics / Q000378:metabolism*; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D003546:Cysteine Endopeptidases / Q000235:genetics / Q000378:metabolism*; D015870:Gene Expression; D010957:Plasmids / Q000235:genetics; D011506:Proteins / Q000737:chemistry / Q000378:metabolism*; D013379:Substrate Specificity; D015003:Yeasts / Q000235:genetics / Q000378:metabolism
chemical_list: D001426:Bacterial Proteins; D011506:Proteins; D019881:Aminoacyltransferases; C120542:sortase A; D003546:Cysteine Endopeptidases