Jan Johansson group

Protein biochemistry for medical applications

Research focus

Three major research lines are pursued; one concerns the BRICHOS domain for treatment of protein aggregation diseases, another line concerns development of synthetic surfactant for treatment of lung diseases and the third line focuses on molecular biology of spider silk proteins. Current activities include elucidation of the BRICHOS mechanism of action using a combination of structural biology, fibrillation kinetics, structure-function analyses, BRICHOS treatment of Alzheimer knock-in mouse models, a clinical trial of the first synthetic surfactant based on designed analogues of surfactant proteins SP-B and SP-C, studies of new surfactant protein analogues, and structure-function analyses of recombinant spider silk proteins.

Group members

Professor

Janne Johansson

Organizational unit: Johansson
E-mail: janne.johansson@ki.se

Postdoc

Gefei Chen

Organizational unit: Johansson
E-mail: gefei.chen@ki.se

PhD student

Axel Leppert

Organizational unit: Johansson
E-mail: axel.leppert@ki.se

Assistant professor

Nina Kronqvist

Organizational unit: Johansson
E-mail: nina.kronqvist@ki.se

PhD student

Médoune Sarr

Organizational unit: Division of Neurogeriatrics
E-mail: medoune.sarr@ki.se

Graduate Student

Lorena Galán Acosta

Organizational unit: Division of Neurogeriatrics
E-mail: lorena.galan.acosta@ki.se

Associated

Simone Tambaro

Organizational unit: Nilsson
E-mail: simone.tambaro@ki.se

Postdoc

Shaffi Manchanda

Organizational unit: Johansson
E-mail: shaffi.manchanda@ki.se

PhD student

Oihana Basabe Burgos

Organizational unit: Johansson
E-mail: oihana.basabe.burgos@ki.se

Selected publications

Sequential pH-driven dimerization and stabilization of the N-terminal domain enables rapid spider silk formation.
Kronqvist N, Otikovs M, Chmyrov V, Chen G, Andersson M, Nordling K, et al
Nat Commun 2014 ;5():3254

A molecular chaperone breaks the catalytic cycle that generates toxic Aβ oligomers.
Cohen S, Arosio P, Presto J, Kurudenkandy F, Biverstal H, Dolfe L, et al
Nat. Struct. Mol. Biol. 2015 Mar;22(3):207-213

Kinetic analysis reveals the diversity of microscopic mechanisms through which molecular chaperones suppress amyloid formation.
Arosio P, Michaels T, Linse S, Månsson C, Emanuelsson C, Presto J, et al
Nat Commun 2016 Mar;7():10948

Efficient protein production inspired by how spiders make silk.
Kronqvist N, Sarr M, Lindqvist A, Nordling K, Otikovs M, Venturi L, et al
Nat Commun 2017 05;8():15504

Bri2 BRICHOS client specificity and chaperone activity are governed by assembly state.
Chen G, Abelein A, Nilsson H, Leppert A, Andrade-Talavera Y, Tambaro S, et al
Nat Commun 2017 12;8(1):2081

Transthyretin and BRICHOS: The Paradox of Amyloidogenic Proteins with Anti-Amyloidogenic Activity for Aβ in the Central Nervous System.
Buxbaum J, Johansson J
Front Neurosci 2017 ;11():119

BRICHOS domain of Bri2 inhibits islet amyloid polypeptide (IAPP) fibril formation and toxicity in human beta cells.
Oskarsson M, Hermansson E, Wang Y, Welsh N, Presto J, Johansson J, et al
Proc. Natl. Acad. Sci. U.S.A. 2018 03;115(12):E2752-E2761

A spidroin-derived solubility tag enables controlled aggregation of a designed amyloid protein.
Sarr M, Kronqvist N, Chen G, Aleksis R, Purhonen P, Hebert H, et al
FEBS J. 2018 May;285(10):1873-1885

Dissertations

Lisa Dolfe, 2016. BRICHOS interactions with amyloid proteins and implications for Alzheimer disease.

Erik Hermansson Wik, 2015. Studies of amyloid toxicity in drosophila models and effects of the BRICHOS domain.

Address

Department of Neurobiology, Care Sciences and Society Neurobiologi, vårdvetenskap och samhälle (NVS)
Division of  Neurogeriatrics
Neo
Blickagången 16
141 52 HUDDINGE