Fibronectin binding to the Salmonella enterica serotype typhimurium ShdA autotransporter protein is inhibited by a monoclonal antibody recognizing the A3 repeat

Robert A. Kingsley, Daad Abi Ghanem, Nahum Puebla-Osorio, A. Marijke Keestra, Luc Berghman, Andreas J Baumler

Research output: Contribution to journalArticle

27 Citations (Scopus)

Abstract

ShdA is a large outer membrane protein of the autotransporter family whose passenger domain binds the extracellular matrix proteins fibronectin and collagen I, fibronectin and collagen I, possibly by mimicking the host ligand heparin. The ShdA passenger domain consists of ∼1,500 amino acid residues that can be divided into two regions based on features of the primary amino acid sequence: an N-terminal nonrepeat region followed by a repeat region composed of two types of imperfect direct amino acid repeats, called type A and type B. The repeat region bound bovine fibronectin with an affinity similar to that for the complete ShdA passenger domain, while the nonrepeat region exhibited comparatively low fibronectin-binding activity. A number of fusion proteins containing truncated fragments of the repeat region did not bind bovine fibronectin. However, binding of the passenger domain to fibronectin was inhibited in the presence of immune serum raised to one truncated fragment of the repeat region that contained repeats A2, B8, A3, and B9. Furthermore, a monoclonal antibody that specifically recognized an epitope in a recombinant protein containing the A3 repeat inhibited binding of ShdA to fibronectin.

Original languageEnglish (US)
Pages (from-to)4931-4939
Number of pages9
JournalJournal of Bacteriology
Volume186
Issue number15
DOIs
StatePublished - Aug 2004
Externally publishedYes

Fingerprint

Salmonella enterica
Fibronectins
Monoclonal Antibodies
Proteins
Collagen
Amino Acids
Extracellular Matrix Proteins
Serogroup
Type V Secretion Systems
Recombinant Proteins
varespladib methyl
Heparin
Immune Sera
Epitopes
Amino Acid Sequence
Membrane Proteins
Ligands

ASJC Scopus subject areas

  • Applied Microbiology and Biotechnology
  • Immunology

Cite this

Fibronectin binding to the Salmonella enterica serotype typhimurium ShdA autotransporter protein is inhibited by a monoclonal antibody recognizing the A3 repeat. / Kingsley, Robert A.; Ghanem, Daad Abi; Puebla-Osorio, Nahum; Keestra, A. Marijke; Berghman, Luc; Baumler, Andreas J.

In: Journal of Bacteriology, Vol. 186, No. 15, 08.2004, p. 4931-4939.

Research output: Contribution to journalArticle

Kingsley, Robert A. ; Ghanem, Daad Abi ; Puebla-Osorio, Nahum ; Keestra, A. Marijke ; Berghman, Luc ; Baumler, Andreas J. / Fibronectin binding to the Salmonella enterica serotype typhimurium ShdA autotransporter protein is inhibited by a monoclonal antibody recognizing the A3 repeat. In: Journal of Bacteriology. 2004 ; Vol. 186, No. 15. pp. 4931-4939.
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abstract = "ShdA is a large outer membrane protein of the autotransporter family whose passenger domain binds the extracellular matrix proteins fibronectin and collagen I, fibronectin and collagen I, possibly by mimicking the host ligand heparin. The ShdA passenger domain consists of ∼1,500 amino acid residues that can be divided into two regions based on features of the primary amino acid sequence: an N-terminal nonrepeat region followed by a repeat region composed of two types of imperfect direct amino acid repeats, called type A and type B. The repeat region bound bovine fibronectin with an affinity similar to that for the complete ShdA passenger domain, while the nonrepeat region exhibited comparatively low fibronectin-binding activity. A number of fusion proteins containing truncated fragments of the repeat region did not bind bovine fibronectin. However, binding of the passenger domain to fibronectin was inhibited in the presence of immune serum raised to one truncated fragment of the repeat region that contained repeats A2, B8, A3, and B9. Furthermore, a monoclonal antibody that specifically recognized an epitope in a recombinant protein containing the A3 repeat inhibited binding of ShdA to fibronectin.",
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