Structural basis of the interaction between the putative adhesion-involved and iron-regulated FrpD and FrpC proteins of Neisseria meningitidis

0474984 - ÚOCHB 2018 RIV GB eng J - Článek v odborném periodiku
Sviridova, E. - Řezáčová, Pavlína - Bondar, Alexey - Veverka, Václav - Novák, P. - Schenk, G. - Svergun, D. I. - Kutá Smatanová, I. - Bumba, L.
Structural basis of the interaction between the putative adhesion-involved and iron-regulated FrpD and FrpC proteins of Neisseria meningitidis.
Scientific Reports. Roč. 7, Jan 13 (2017), č. článku 40408. ISSN 2045-2322. E-ISSN 2045-2322
Grant CEP: GA MŠMT(CZ) LK11205; GA MŠMT(CZ) LO1304; GA MŠMT(CZ) LM2015064
Institucionální podpora: RVO:61388963
Klíčová slova: membrane lipoprotein FrpD * RTX proteins * cross-linking
Obor OECD: Biochemistry and molecular biology
Impakt faktor: 4.122, rok: 2017
https://www.nature.com/articles/srep40408

The iron-regulated protein FrpD from Neisseria meningitidis is an outer membrane lipoprotein that interacts with very high affinity (K-d similar to 0.2 nM) with the N-terminal domain of FrpC, a Type I-secreted protein from the Repeat in ToXin (RTX) protein family. In the presence of Ca2+, FrpC undergoes Ca2+ -dependent protein trans-splicing that includes an autocatalytic cleavage of the Asp(414)-Pro(415) peptide bond and formation of an Asp(414)-Lys isopeptide bond. Here, we report the high-resolution structure of FrpD and describe the structure-function relationships underlying the interaction between FrpD and FrpC(1-414). We identified FrpD residues involved in FrpC(1-414) binding, which enabled localization of FrpD within the low-resolution SAXS model of the FrpD-FrpC(1-414) complex. Moreover, the trans-splicing activity of FrpC resulted in covalent linkage of the FrpC(1-414) fragment to plasma membrane proteins of epithelial cells in vitro, suggesting that formation of the FrpD-FrpC(1-414) complex may be involved in the interaction of meningococci with the host cell surface.
Trvalý link: http://hdl.handle.net/11104/0271870