Work

Staphylococcal protein A consists of five IgG-binding domains

Year: 1986

Type: article

Abstract: A genetic approach is described to clarify the IgG-binding properties of the N-terminal portion of staphylococcal protein A (region E). Several gene fragments, encoding region E or B or protein A, have been cloned and expressed in Escherichia coli. The gene products were purified by IgG-affinity chromatography and subjected to structural and functional analyses. Both fragments can be efficiently purified using this method, suggesting that region B as well as region E has Fc-binding activity. In addition, gene fusions were assembled giving fragments EB and EE, which both showed a divalent Fc-binding. These results demonstrate that protein A consists of five IgG-binding domains. The implications of these findings for the structure of protein-A--immunoglobulin-G complexes are discussed.

Source: European Journal of Biochemistry

DOI: 10.1111/j.1432-1033.1986.tb09625.x

Authors: Tomas MOKS, Lars ABRAHMSEN, Bjorn NILSSON, Ulf HELLMAN, John SJOQUIST, Mathias UHLEN

Institutions: KTH Royal Institute of Technology, Uppsala University, European Molecular Biology Laboratory

Language: English

Topic: Monoclonal and Polyclonal Antibodies Research

Subfield: Immunology

Field: Immunology and Microbiology

Domain: Life Sciences

Open Access status: bronze

Funder: Medical Research Council

OpenAlex ID: W2029677323

FWCI: 1.436

Cites: 45

Cited by: 374

Related to: 10