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Human factor H-related protein 2 (CFHR2) regulates complement activation

Standard

Human factor H-related protein 2 (CFHR2) regulates complement activation. / Eberhardt, Hannes U; Buhlmann, Denise; Hortschansky, Peter; Chen, Qian; Böhm, Sascha; Kemper, Markus J; Wallich, Reinhard; Hartmann, Andrea; Hallström, Teresia; Zipfel, Peter F; Skerka, Christine.

in: PLOS ONE, Jahrgang 8, Nr. 11, 01.01.2013, S. e78617.

Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung

Harvard

Eberhardt, HU, Buhlmann, D, Hortschansky, P, Chen, Q, Böhm, S, Kemper, MJ, Wallich, R, Hartmann, A, Hallström, T, Zipfel, PF & Skerka, C 2013, 'Human factor H-related protein 2 (CFHR2) regulates complement activation', PLOS ONE, Jg. 8, Nr. 11, S. e78617. https://doi.org/10.1371/journal.pone.0078617

APA

Eberhardt, H. U., Buhlmann, D., Hortschansky, P., Chen, Q., Böhm, S., Kemper, M. J., Wallich, R., Hartmann, A., Hallström, T., Zipfel, P. F., & Skerka, C. (2013). Human factor H-related protein 2 (CFHR2) regulates complement activation. PLOS ONE, 8(11), e78617. https://doi.org/10.1371/journal.pone.0078617

Vancouver

Eberhardt HU, Buhlmann D, Hortschansky P, Chen Q, Böhm S, Kemper MJ et al. Human factor H-related protein 2 (CFHR2) regulates complement activation. PLOS ONE. 2013 Jan 1;8(11):e78617. https://doi.org/10.1371/journal.pone.0078617

Bibtex

@article{a7dea9e3537b4996aaf4e8988b9e6232,
title = "Human factor H-related protein 2 (CFHR2) regulates complement activation",
abstract = "Mutations and deletions within the human CFHR gene cluster on chromosome 1 are associated with diseases, such as dense deposit disease, CFHR nephropathy or age-related macular degeneration. Resulting mutant CFHR proteins can affect complement regulation. Here we identify human CFHR2 as a novel alternative pathway complement regulator that inhibits the C3 alternative pathway convertase and terminal pathway assembly. CFHR2 is composed of four short consensus repeat domains (SCRs). Two CFHR2 molecules form a dimer through their N-terminal SCRs, and each of the two C-terminal ends can bind C3b. C3b bound CFHR2 still allows C3 convertase formation but the CFHR2 bound convertases do not cleave the substrate C3. Interestingly CFHR2 hardly competes off factor H from C3b. Thus CFHR2 likely acts in concert with factor H, as CFHR2 inhibits convertases while simultaneously allowing factor H assisted degradation by factor I.",
author = "Eberhardt, {Hannes U} and Denise Buhlmann and Peter Hortschansky and Qian Chen and Sascha B{\"o}hm and Kemper, {Markus J} and Reinhard Wallich and Andrea Hartmann and Teresia Hallstr{\"o}m and Zipfel, {Peter F} and Christine Skerka",
year = "2013",
month = jan,
day = "1",
doi = "10.1371/journal.pone.0078617",
language = "English",
volume = "8",
pages = "e78617",
journal = "PLOS ONE",
issn = "1932-6203",
publisher = "Public Library of Science",
number = "11",

}

RIS

TY - JOUR

T1 - Human factor H-related protein 2 (CFHR2) regulates complement activation

AU - Eberhardt, Hannes U

AU - Buhlmann, Denise

AU - Hortschansky, Peter

AU - Chen, Qian

AU - Böhm, Sascha

AU - Kemper, Markus J

AU - Wallich, Reinhard

AU - Hartmann, Andrea

AU - Hallström, Teresia

AU - Zipfel, Peter F

AU - Skerka, Christine

PY - 2013/1/1

Y1 - 2013/1/1

N2 - Mutations and deletions within the human CFHR gene cluster on chromosome 1 are associated with diseases, such as dense deposit disease, CFHR nephropathy or age-related macular degeneration. Resulting mutant CFHR proteins can affect complement regulation. Here we identify human CFHR2 as a novel alternative pathway complement regulator that inhibits the C3 alternative pathway convertase and terminal pathway assembly. CFHR2 is composed of four short consensus repeat domains (SCRs). Two CFHR2 molecules form a dimer through their N-terminal SCRs, and each of the two C-terminal ends can bind C3b. C3b bound CFHR2 still allows C3 convertase formation but the CFHR2 bound convertases do not cleave the substrate C3. Interestingly CFHR2 hardly competes off factor H from C3b. Thus CFHR2 likely acts in concert with factor H, as CFHR2 inhibits convertases while simultaneously allowing factor H assisted degradation by factor I.

AB - Mutations and deletions within the human CFHR gene cluster on chromosome 1 are associated with diseases, such as dense deposit disease, CFHR nephropathy or age-related macular degeneration. Resulting mutant CFHR proteins can affect complement regulation. Here we identify human CFHR2 as a novel alternative pathway complement regulator that inhibits the C3 alternative pathway convertase and terminal pathway assembly. CFHR2 is composed of four short consensus repeat domains (SCRs). Two CFHR2 molecules form a dimer through their N-terminal SCRs, and each of the two C-terminal ends can bind C3b. C3b bound CFHR2 still allows C3 convertase formation but the CFHR2 bound convertases do not cleave the substrate C3. Interestingly CFHR2 hardly competes off factor H from C3b. Thus CFHR2 likely acts in concert with factor H, as CFHR2 inhibits convertases while simultaneously allowing factor H assisted degradation by factor I.

U2 - 10.1371/journal.pone.0078617

DO - 10.1371/journal.pone.0078617

M3 - SCORING: Journal article

C2 - 24260121

VL - 8

SP - e78617

JO - PLOS ONE

JF - PLOS ONE

SN - 1932-6203

IS - 11

ER -