A novel fibronectin binding motif in MSCRAMMs targets F3 modules

Sabitha Prabhakaran; Xiaowen Liang; Jonathan T Skare; Jennifer R Potts; Magnus Höök

doi:10.1371/journal.pone.0005412

A novel fibronectin binding motif in MSCRAMMs targets F3 modules

Sabitha Prabhakaran, Xiaowen Liang, Jonathan T Skare, Jennifer R Potts, Magnus Höök

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

Abstract

BBK32 is a surface expressed lipoprotein and fibronectin (Fn)-binding microbial surface component recognizing adhesive matrix molecule (MSCRAMM) of Borrelia burgdorferi, the causative agent of Lyme disease. Previous studies from our group showed that BBK32 is a virulence factor in experimental Lyme disease and located the Fn-binding region to residues 21-205 of the lipoprotein.

Original language	English
Article number	e5412
Pages (from-to)	e5412
Journal	PLoS ONE
Volume	4
Issue number	4
DOIs	https://doi.org/10.1371/journal.pone.0005412
Publication status	Published - 30 Apr 2009

Keywords

Adhesins, Bacterial
Amino Acid Motifs
Bacterial Proteins
Binding Sites
Borrelia burgdorferi
Cells, Cultured
Endothelial Cells
Fibroblasts
Fibronectins
Humans
Lyme Disease
Peptide Fragments
Protein Binding
Protein Multimerization
Receptors, Virus
Virulence Factors

Access to Document

10.1371/journal.pone.0005412

Cite this

@article{9ae6c1008fb84f29ad13f12f2630b23b,

title = "A novel fibronectin binding motif in MSCRAMMs targets F3 modules",

abstract = "BBK32 is a surface expressed lipoprotein and fibronectin (Fn)-binding microbial surface component recognizing adhesive matrix molecule (MSCRAMM) of Borrelia burgdorferi, the causative agent of Lyme disease. Previous studies from our group showed that BBK32 is a virulence factor in experimental Lyme disease and located the Fn-binding region to residues 21-205 of the lipoprotein.",

keywords = "Adhesins, Bacterial, Amino Acid Motifs, Bacterial Proteins, Binding Sites, Borrelia burgdorferi, Cells, Cultured, Endothelial Cells, Fibroblasts, Fibronectins, Humans, Lyme Disease, Peptide Fragments, Protein Binding, Protein Multimerization, Receptors, Virus, Virulence Factors",

author = "Sabitha Prabhakaran and Xiaowen Liang and Skare, {Jonathan T} and Potts, {Jennifer R} and Magnus H{\"o}{\"o}k",

year = "2009",

month = apr,

day = "30",

doi = "10.1371/journal.pone.0005412",

language = "English",

volume = "4",

pages = "e5412",

journal = "PLoS ONE",

issn = "1932-6203",

publisher = "Public Library of Science",

number = "4",

}

TY - JOUR

T1 - A novel fibronectin binding motif in MSCRAMMs targets F3 modules

AU - Prabhakaran, Sabitha

AU - Liang, Xiaowen

AU - Skare, Jonathan T

AU - Potts, Jennifer R

AU - Höök, Magnus

PY - 2009/4/30

Y1 - 2009/4/30

N2 - BBK32 is a surface expressed lipoprotein and fibronectin (Fn)-binding microbial surface component recognizing adhesive matrix molecule (MSCRAMM) of Borrelia burgdorferi, the causative agent of Lyme disease. Previous studies from our group showed that BBK32 is a virulence factor in experimental Lyme disease and located the Fn-binding region to residues 21-205 of the lipoprotein.

AB - BBK32 is a surface expressed lipoprotein and fibronectin (Fn)-binding microbial surface component recognizing adhesive matrix molecule (MSCRAMM) of Borrelia burgdorferi, the causative agent of Lyme disease. Previous studies from our group showed that BBK32 is a virulence factor in experimental Lyme disease and located the Fn-binding region to residues 21-205 of the lipoprotein.

KW - Adhesins, Bacterial

KW - Amino Acid Motifs

KW - Bacterial Proteins

KW - Binding Sites

KW - Borrelia burgdorferi

KW - Cells, Cultured

KW - Endothelial Cells

KW - Fibroblasts

KW - Fibronectins

KW - Humans

KW - Lyme Disease

KW - Peptide Fragments

KW - Protein Binding

KW - Protein Multimerization

KW - Receptors, Virus

KW - Virulence Factors

UR - http://www.scopus.com/inward/record.url?scp=65549112108&partnerID=8YFLogxK

U2 - 10.1371/journal.pone.0005412

DO - 10.1371/journal.pone.0005412

M3 - Article

C2 - 19404402

SN - 1932-6203

VL - 4

SP - e5412

JO - PLoS ONE

JF - PLoS ONE

IS - 4

M1 - e5412

ER -

A novel fibronectin binding motif in MSCRAMMs targets F3 modules

Abstract

Keywords

Access to Document

Other files and links

Cite this