High affinity streptococcal binding to human fibronectin requires specific recognition of sequential F1 modules

E.S. Pilka; A.R. Pickford; J.H. Kim; I.D. Campbell; J.R. Potts; U. Schwarz-Linek; M. Höök

doi:10.1074/jbc.M405083200

High affinity streptococcal binding to human fibronectin requires specific recognition of sequential F1 modules

E.S. Pilka, A.R. Pickford, J.H. Kim, I.D. Campbell, J.R. Potts, U. Schwarz-Linek, M. Höök

Chemistry

Research output: Contribution to journal › Article › peer-review

Abstract

Fibronectin (Fn) binding by the Streptococcus pyogenes protein SfbI has been shown to trigger integrin-dependent internalization of this pathogen by human epithelial and endothelial cells. Here, using nuclear magnetic resonance spectroscopy and isothermal titration calorimetry in a dissection approach, the basis for the specificity and high affinity of the interaction between the N-terminal domain of Fn and SfbI is revealed. Each of the five Fn type 1 modules is directly involved in the interaction and is recognized by short consecutive motifs within the repeat region of SfbI. Crucially, these motifs must be combined in the correct order to form a high affinity ligand for the N-terminal domain of Fn.

Original language	English
Pages (from-to)	39017-25
Number of pages	9
Journal	Journal of Biological Chemistry
Volume	279
Issue number	37
DOIs	https://doi.org/10.1074/jbc.M405083200
Publication status	Published - 2004

Keywords

Amino Acid Motifs
Amino Acid Sequence
Binding, Competitive
Calorimetry
Cell Nucleus
Fibronectins
Humans
Hydrogen-Ion Concentration
Kinetics
Ligands
Magnetic Resonance Spectroscopy
Models, Molecular
Molecular Sequence Data
Peptides
Pichia
Protein Binding
Protein Structure, Tertiary
Recombinant Proteins
Sequence Homology, Amino Acid
Streptococcus
Thermodynamics
Time Factors

Access to Document

10.1074/jbc.M405083200

http://dx.doi.org/10.1074/jbc.M405083200

Cite this

@article{31275d001f934dc6ad027d86e7a7e2f8,

title = "High affinity streptococcal binding to human fibronectin requires specific recognition of sequential F1 modules",

abstract = "Fibronectin (Fn) binding by the Streptococcus pyogenes protein SfbI has been shown to trigger integrin-dependent internalization of this pathogen by human epithelial and endothelial cells. Here, using nuclear magnetic resonance spectroscopy and isothermal titration calorimetry in a dissection approach, the basis for the specificity and high affinity of the interaction between the N-terminal domain of Fn and SfbI is revealed. Each of the five Fn type 1 modules is directly involved in the interaction and is recognized by short consecutive motifs within the repeat region of SfbI. Crucially, these motifs must be combined in the correct order to form a high affinity ligand for the N-terminal domain of Fn.",

keywords = "Amino Acid Motifs, Amino Acid Sequence, Binding, Competitive, Calorimetry, Cell Nucleus, Fibronectins, Humans, Hydrogen-Ion Concentration, Kinetics, Ligands, Magnetic Resonance Spectroscopy, Models, Molecular, Molecular Sequence Data, Peptides, Pichia, Protein Binding, Protein Structure, Tertiary, Recombinant Proteins, Sequence Homology, Amino Acid, Streptococcus, Thermodynamics, Time Factors",

author = "E.S. Pilka and A.R. Pickford and J.H. Kim and I.D. Campbell and J.R. Potts and U. Schwarz-Linek and M. H{\"o}{\"o}k",

year = "2004",

doi = "10.1074/jbc.M405083200",

language = "English",

volume = "279",

pages = "39017--25",

journal = "Journal of Biological Chemistry",

issn = "0021-9258",

publisher = "American Society for Biochemistry and Molecular Biology Inc.",

number = "37",

}

TY - JOUR

T1 - High affinity streptococcal binding to human fibronectin requires specific recognition of sequential F1 modules

AU - Pilka, E.S.

AU - Pickford, A.R.

AU - Kim, J.H.

AU - Campbell, I.D.

AU - Potts, J.R.

AU - Schwarz-Linek, U.

AU - Höök, M.

PY - 2004

Y1 - 2004

N2 - Fibronectin (Fn) binding by the Streptococcus pyogenes protein SfbI has been shown to trigger integrin-dependent internalization of this pathogen by human epithelial and endothelial cells. Here, using nuclear magnetic resonance spectroscopy and isothermal titration calorimetry in a dissection approach, the basis for the specificity and high affinity of the interaction between the N-terminal domain of Fn and SfbI is revealed. Each of the five Fn type 1 modules is directly involved in the interaction and is recognized by short consecutive motifs within the repeat region of SfbI. Crucially, these motifs must be combined in the correct order to form a high affinity ligand for the N-terminal domain of Fn.

AB - Fibronectin (Fn) binding by the Streptococcus pyogenes protein SfbI has been shown to trigger integrin-dependent internalization of this pathogen by human epithelial and endothelial cells. Here, using nuclear magnetic resonance spectroscopy and isothermal titration calorimetry in a dissection approach, the basis for the specificity and high affinity of the interaction between the N-terminal domain of Fn and SfbI is revealed. Each of the five Fn type 1 modules is directly involved in the interaction and is recognized by short consecutive motifs within the repeat region of SfbI. Crucially, these motifs must be combined in the correct order to form a high affinity ligand for the N-terminal domain of Fn.

KW - Amino Acid Motifs

KW - Amino Acid Sequence

KW - Binding, Competitive

KW - Calorimetry

KW - Cell Nucleus

KW - Fibronectins

KW - Humans

KW - Hydrogen-Ion Concentration

KW - Kinetics

KW - Ligands

KW - Magnetic Resonance Spectroscopy

KW - Models, Molecular

KW - Molecular Sequence Data

KW - Peptides

KW - Pichia

KW - Protein Binding

KW - Protein Structure, Tertiary

KW - Recombinant Proteins

KW - Sequence Homology, Amino Acid

KW - Streptococcus

KW - Thermodynamics

KW - Time Factors

U2 - 10.1074/jbc.M405083200

DO - 10.1074/jbc.M405083200

M3 - Article

C2 - 15247227

SN - 0021-9258

VL - 279

SP - 39017

EP - 39025

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

IS - 37

ER -